Vasoactive intestinal polypeptide (VIP) receptor antagonists FC fusions and methods of use

Description

VASOACTIVE INTESTINAL POLYPEPTIDE (VIP) RECEPTOR ANTAGONISTS FC FUSIONS AND METHODS OF USEI. CROSS REFERENCE TO RELATED APPLICATIONSThis application claims the benefit of U.S. Provisional Application No. 63 / 631,024, filed on April 8, 2024 which is incorporated herein by reference in its entirety.IL BACKGROUND1. Vasoactive intestinal polypeptide (VIP) is a 28-residue neuropeptide with potent antiinflammatory activity and immunosuppressive effects on T cells. The VIP receptors VPAC1 and VPAC2 are widely expressed throughout the body with differential expression on the surface of immune cells. Furthermore, overexpression of VIP and its receptors is in breast, prostate, and lung cancers, wherein VIP promotes growth and metastasis in tumors.2. We have recently developed a series of VIP-receptor antagonists. These peptides possess a modified, positively charged N-terminus. The ANT peptides enhance immune responses to cancers. Despite the promising anti-tumor properties of these VIP antagonist derivatives, peptide therapeutics commonly suffer from poor metabolic stability and consequently exhibit short half-life and fast elimination in vivo. These limitations pose a significant barrier to the utility of therapeutic peptides as competent drug candidates. What are needed are new or modified VIP antagonists that due not suffer from stability and half-life issues.III. SUMMARY3. Disclosed are methods and compositions related to modified VIP receptor antagonists. In some aspects, disclosed are methods and compositions related to vasoactive intestinal peptide (VIP) receptor antagonists for uses in managing the treatment or prevention of cancer and viral infections. In certain embodiments, this disclosure relates to chimeric variants of VIP-R antagonists, as peptides disclosed herein, and pharmaceutical composition comprising the same. In certain embodiments, this disclosure contemplates methods of stimulating immune cells to target cancer by mixing immune cells in vitro with peptides disclosed herein and further administering an effective amount of stimulated immune cells to a subject in need of cancer treatment.4. In one aspect, disclosed herein are modified vasoactive intestinal peptide receptor (VIP-R) antagonists comprising KPRRPYX1X2X3X4TXsLRKQX6AVX7X8KYLX9X10ILN (SEQ ID NO: 3) or a fragment thereof, wherein X1is T or A; X2is D, V, or S; X3is N or D; X4is Y orC; X5is R or S; X6is M or 1; X7is K or N; X8is K; X9is N or M; X10is S, or L; and provided that the peptide is not KPRRPYTDNYTRLRKQMAVKKYLNSILN (SEQ ID NO: 2) or the peptide is not the combination wherein X1is T, X2is D, X3is N; X4is Y, X5is R, X6is M, X7is K, X9is N, and X10is S (such as, for example, ANT005 KPRRPYTDNCTRLRKQMAVKKYLNSILN (SEQ ID NO: 4), ANT008 KPRRPYTDNYTRLRKQMAVKKYLNLILN (SREQ ID NO: 5), ANT058 KPRRPYADNYTRLRKQMAVNKYLNLILN (SEQ ID NO: 6), ANT105 KPRRPYAVNYTRLRKQIAVKKYLMSILN (SEQ ID NO: 7), ANT107 KPRRPYAVNYTRLRKQMAVNKYLMSILN (SEQ ID NO: 8), ANTI 14 KPRRPYADNCTRLRKQIAVNKKYLNSILN (SEQ ID NO: 9), ANT195 KPRRPYTVNYTSLRKQIAVKKYLMLILN (SEQ ID NO: 10), ANT197 KPRRPYTDNCTSLRKQIAVNKYLNLILN (SEQ ID NO: 11), ANT202 KPRRPYAVNCTSLRKQIAVNKYLNSILN (SEQ ID NO: 12), ANT203 KPRRPYAVNCTSLRKQIAVKKYLMSILN (SEQ ID NO: 13), ANT219 KPRRPYTVNCTSLRKQIAVKKYLMLILN (SEQ ID NO: 14), ANT300 KPRRPYTSDYTRLRKQMAVKKYLNSILN (SEQ ID NO: 15), or ANT308 KPRRPYTSDYTRLRKQMAVKKYLNLILN (SEQ ID NO: 16); and wherein the VIP-R antagonist is conjugated to an immunoglobulin Fc domain (such as, for example SEQ ID NO: 52) at the carboxyl terminus of the VIP-R antagonist peptide).5. Also disclosed herein are modified vasoactive intestinal peptide receptor (VIP-R) antagonists comprising KPRRPYX]X2X3X4TX5LRKQX6AVX7KYLX8X9ILN (SEQ ID NO: 21) or a fragment thereof, wherein X1is T or A; X2is D, V, or S; X3is N or D; X4is Y or C; Xsis R or S; X6is M or I; X7is K or N; X8is N or M; X9is S, or L; and provided that the peptide is not KPRRPYTDNYTRLRKQMAVKKYLNSILN (SEQ ID NO: 2) or the peptide is not the combination wherein X1is T, X2is D, X3is N; X4is Y, X5is R, X6is M, X7is K, X8is N, and X9is S (such as, for example, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, and / or SEQ ID NO: 16); and wherein the VIP-R antagonist is conjugated to an immunoglobulin Fc domain (such as, for example SEQ ID NO: 52) at the carboxyl terminus of the VIP-R antagonist peptide).6. In one aspect disclosed herein are modified VIP-R antagonists of any preceding aspect, wherein the Fc domain (such as, for example, SEQ ID NO: 26) is conjugated to the carboxyl terminus of the VIP-R antagonist peptide (such as, for example, ANT005 KPRRPYTDNCTRLRKQMAVKKYLNSILN (SEQ ID NO: 4), ANT008KPRRPYTDNYTRLRKQMAVKKYLNL1LN (SREQ ID NO: 5), ANT058 KPRRPYADNYTRLRKQMAVNKYLNLILN (SEQ ID NO: 6), ANT105 KPRRPYAVNYTRLRKQIAVKKYLMSILN (SEQ ID NO: 7), ANT107 KPRRPYAVNYTRLRKQMAVNKYLMSILN (SEQ ID NO: 8), ANTI 14 KPRRPYADNCTRLRKQIAVNKKYLNSILN (SEQ ID NO: 9), ANT195 KPRRPYTVNYTSLRKQIAVKKYLMLILN (SEQ ID NO: 10), ANTI 97 KPRRPYTDNCTSLRKQIAVNKYLNLILN (SEQ ID NO: 11), ANT202 KPRRPYAVNCTSLRKQIAVNKYLNSILN (SEQ ID NO: 12), ANT203 KPRRPYAVNCTSLRKQIAVKKYLMSILN (SEQ ID NO: 13), ANT219 KPRRPYTVNCTSLRKQIAVKKYLMLILN (SEQ ID NO: 14), ANT300 KPRRPYTSDYTRLRKQMAVKKYLNSILN (SEQ ID NO: 15), or ANT308 KPRRPYTSDYTRLRKQMAVKKYLNLILN (SEQ ID NO: 16). In some aspects the Fc domain conjugated modified VIP-R antagonist (also referred to herein as a VIP-R antagonist Fc fusion) further comprises a linker (such as, for example a GS linker (SEQ ID NO: 22)), a signal peptide (such as, for example, SEQ ID NO: 24), and a hinge domain (such as, for example, SEQ ID NO: 25). For example, disclosed herein are modified VIP-R antagonists of any preceding aspect, wherein the modification comprises an Fc domain conjugated to the carboxyl terminus of the VIP-R antagonist peptide as set forth in SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39.7. Also disclosed herein are pharmaceutical compositions comprising the VIP-R antagonist of any preceding aspect and a pharmaceutically acceptable carrier.8. In one aspect, disclosed herein are nucleic acids encoding the modified VIP-R antagonists of any preceding aspect. Also disclosed herein are recombinant vectors comprising said nucleic acids. In one aspect, disclosed herein are expression systems or cells comprising a recombinant vector of any preceding aspect.9. Also disclosed herein are methods of treating, decreasing, inhibiting, reducing, ameliorating, and / or preventing a cancer and / or metastasis (such as, for example, pancreatic cancer, colon cancer, leukemia, liver cancer, lung cancer, or melanoma) in a subject or enhancing the immune response to cancer and / or metastasis (such as, for example, pancreatic cancer, colon cancer, leukemia, liver cancer, lung cancer, or melanoma) in a subject comprising administering to the subject a therapeutically effective amount of the modified VIP-R antagonists of any preceding aspect (including, but not limited to SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO:11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO:32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39) or pharmaceutical composition of any preceding aspect. For example, disclosed herein are methods of treating, decreasing, inhibiting, reducing, ameliorating, and / or preventing a cancer and / or metastasis (such as, for example, pancreatic cancer, colon cancer, leukemia, liver cancer, lung cancer, or melanoma) in a subject or enhancing the immune response to cancer and / or metastasis (such as, for example, pancreatic cancer, colon cancer, leukemia, liver cancer, lung cancer, or melanoma) in a subject comprising administering to the subject a therapeutically effective amount of SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO:33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39. In certain embodiments, the modified VIP-R antagonist or the pharmaceutical composition is administered in combination with another anti-cancer agent. In some aspect, the method can further comprise exposing the subject to radiation and / or transplanting allogeneic hematopoietic stem cells into the subject and / or other adoptive cellular therapies (such as, for example, administration of CAR T cells, TCR Modified T Cells, CAR NK cells, TILs, TINKs, and / or MILs). In certain embodiments, the method further comprises administering to the subject a therapeutically effective amount of a phosphatidylinositol 3-kinase (PI3K) inhibitor (including, for example, a PI3Ka inhibitor, a PI3KP inhibitor, a PI3K5 inhibitor, or a PI3Ky inhibitor including, but not limited to idelalisib, copanlisib, duvelisib, alpelisib, umbralisib, buparlisib, copanlisib, dactolisib, leniolisib, parsaclisib, paxalisib, taselisib, zandelisib, inavolisib, apitolisib, bimiralisib, eganelisib, fimepinostat, gedatolisib, linperlisib, nemiralisib, pilaralisib, samotolisib, seletalisib, serabelisib, sonolisib, tenalisib, voxtalisib, AMG 319, AZD8186, GSK2636771, SF1126, acalisib, omipalisib, AZD8835, CAL263, GSK1059615, MEN1611, PWT33597, TG100-115, or ZSTK474). In certain embodiments, the method further comprises administering to the subject a therapeutically effective amount of an immune checkpoint blockade. In some embodiments, the immune checkpoint blockade is a PD-1 inhibitor, a PD-L1 inhibitor, a CTLA-4 inhibitor, an anti-TIM3 inhibitor, an anti-LAG3 inhibitor, an anti-CD47 inhibitor, imiquimod, polyinosinic-polycytidylic acid-poly-l-lysine carboxymethylcellulose (poly-ICLC) , pexidartinib, an anti-TIGIT inhibitor, an anti-B7-H3 inhibitor, an anti-B7-H4 inhibitor, an anti-A2aR inhibitor, an anti-CD73 inhibitor, an anti-NKG2A inhibitor, an anti-PVR!G / PVRL2 inhibitor, an anti-CEACAMl inhibitor, an anti- CEACAM5 inhibitor, an anti-CEACAM6 inhibitor, an focal adhesion kinase (FAK) inhibitor, a CCL2 / CCR2 inhibitor, an anti-leukemia inhibitory factor (LIF) inhibitor, an anti-CD47 / SIRPa inhibitor, an anti-colony-stimulating factor (CSF)-l inhibitor, an anti-IL-1 inhibitor, an anti-IL- 1R3 inhibitor, an anti-IL-8 inhibitor, an anti-semaphorin 4D (Sema4D) inhibitor, an angiopoietin(Ang)-2 inhibitor, a CLEVER-1 inhibitor, Axl-targeted enapotamab vedotin (EnaV), or an anti-phosphatidylserine inhibitor including, but not limited to pembrolizumab, nivolumab, cemiplimab, dostarlimab, atezolizumab, avelumab, durvalumab, or ipilimumab.10. In one aspect, disclosed herein are methods of treating, decreasing, inhibiting, reducing, and / or ameliorating a microbial in a subject infected with a microbe or at risk for a microbial infection comprising administering to the subject a therapeutically effective amount of the modified VIP-R antagonists of any preceding aspect (including, but not limited to SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39) or pharmaceutical composition of any preceding aspect. For example, disclosed herein are methods of treating, decreasing, inhibiting, reducing, and / or ameliorating a microbial in a subject infected with a microbe or at risk for a microbial infection comprising administering to the subject a therapeutically effective amount of SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39. In certain embodiments, the method further comprises administering to the subject a therapeutically effective amount of a phosphatidylinositol 3-kinase (PI3K) inhibitor (including, for example, a PI3Ka inhibitor, a PI3K inhibitor, a PI3K5 inhibitor, or a PI3Ky inhibitor including, but not limited to idelalisib, copanlisib, duvelisib, alpelisib, umbralisib, buparlisib, copanlisib, dactolisib, leniolisib, parsaclisib, paxalisib, taselisib, zandelisib, inavolisib, apitolisib, bimiralisib, eganelisib, fimepinostat, gedatolisib, linperlisib, nemiralisib, pilaralisib, samotolisib, seletalisib, serabelisib, sonolisib, tenalisib, voxtalisib, AMG 319, AZD8186, GSK2636771, SF1126, acalisib, omipalisib, AZD8835, CAL263, GSK1059615, MEN1611, PWT33597, TG100-115, or ZSTK474). In certain embodiments, the method further comprises administering to the subject atherapeutically effective amount of an immune checkpoint blockade. In some embodiments, the immune checkpoint blockade is a PD-1 inhibitor, a PD-L1 inhibitor, a CTLA-4 inhibitor, an anti-TIM3 inhibitor, an anti-LAG3 inhibitor, an anti-CD47 inhibitor, imiquimod, polyinosinic- polycytidylic acid-poly-l-lysine carboxymethylcellulose (poly-ICLC) , pexidartinib, an anti- TIGIT inhibitor, an anti-B7-H3 inhibitor, an anti-B7-H4 inhibitor, an anti-A2aR inhibitor, an anti-CD73 inhibitor, an anti-NKG2A inhibitor, an anti-PVRIG / PVRL2 inhibitor, an anti- CEACAM1 inhibitor, an anti-CEACAM5 inhibitor, an anti-CEACAM6 inhibitor, an focal adhesion kinase (FAK) inhibitor, a CCL2 / CCR2 inhibitor, an anti-leukemia inhibitory factor (LIF) inhibitor, an anti-CD47 / SIRPa inhibitor, an anti-colony-stimulating factor (CSF)-l inhibitor, an anti-IL-1 inhibitor, an anti-IL-lR3 inhibitor, an anti-IL-8 inhibitor, an anti- semaphorin 4D (Sema4D) inhibitor, an angiopoietin(Ang)-2 inhibitor, a CLEVER- 1 inhibitor, Axl-targeted enapotamab vedotin (EnaV), or an anti-phosphatidylserine inhibitor including, but not limited to pembrolizumab, nivolumab, cemiplimab, dostarlimab, atezolizumab, avelumab, durvalumab, or ipilimumab.11. Also disclosed herein are methods of ex vivo augmenting T cell activation and / or expansion, comprising mixing one or more T cells with the modified VIP-R antagonists of any preceding aspect (including, but not limited to SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39) or pharmaceutical composition of any preceding aspect. For example, disclosed herein are methods of ex vivo augmenting T cell activation and / or expansion, comprising mixing one or more T cells with the modified VIP-R antagonist as set forth in SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39. In some aspect, the method further comprises mixing the one or more T cells is in combination with an anti-CD3 antibody and / or an anti-CD28 antibody. In certain embodiments, the method further comprises administering to the subject a therapeutically effective amount of a phosphatidylinositol 3-kinase (PI3K) inhibitor (including, for example, a PI3Ka inhibitor, a PI3KP inhibitor, a PI3K5 inhibitor, or a PI3Ky inhibitor including, but not limited to idelalisib, copanlisib, duvelisib, alpelisib, umbralisib,buparlisib, copanlisib, dactolisib, leniolisib, parsaclisib, paxalisib, taselisib, zandelisib, inavolisib, apitolisib, bimiralisib, eganelisib, fimepinostat, gedatolisib, linperlisib, nemiralisib, pilaralisib, samotolisib, seletalisib, serabelisib, sonolisib, tenalisib, voxtalisib, AMG 319, AZD8186, GSK2636771, SF1126, acalisib, omipalisib, AZD8835, CAL263, GSK1059615, MEN1611, PWT33597, TG100-115, or ZSTK474). In certain embodiments, the method further comprises administering to the subject a therapeutically effective amount of an immune checkpoint blockade. In some embodiments, the immune checkpoint blockade is a PD-1 inhibitor, a PD-L1 inhibitor, a CTLA-4 inhibitor, an anti-TIM3 inhibitor, an anti-LAG3 inhibitor, an anti-CD47 inhibitor, imiquimod, polyinosinic-polycytidylic acid-poly-l-lysine carboxymethylcellulose (poly-ICLC) , pexidartinib, an anti-TIGIT inhibitor, an anti-B7-H3 inhibitor, an anti-B7-H4 inhibitor, an anti-A2aR inhibitor, an anti-CD73 inhibitor, an anti- NKG2A inhibitor, an anti-PVRIG / PVRL2 inhibitor, an anti-CEACAMl inhibitor, an anti- CEACAM5 inhibitor, an anti-CEACAM6 inhibitor, an focal adhesion kinase (FAK) inhibitor, a CCL2 / CCR2 inhibitor, an anti-leukemia inhibitory factor (LIF) inhibitor, an anti-CD47 / SIRPa inhibitor, an anti-colony-stimulating factor (CSF)-l inhibitor, an anti-IL-1 inhibitor, an anti-IL- 1R3 inhibitor, an anti-IL-8 inhibitor, an anti-semaphorin 4D (Sema4D) inhibitor, an angiopoietin(Ang)-2 inhibitor, a CLEVER- 1 inhibitor, Axl-targeted enapotamab vedotin (EnaV), or an anti-phosphatidylserine inhibitor including, but not limited to pembrolizumab, nivolumab, cemiplimab, dostarlimab, atezolizumab, avelumab, durvalumab, or ipilimumab.12. In one aspect disclosed herein are methods of treating, inhibiting, decreasing, reducing, ameliorating a cancer and / or metastasis (such as, for example, pancreatic cancer, colon cancer, leukemia, liver cancer, lung cancer, or melanoma) or a chronic infection in a subject in need, comprising obtaining one or more T cells (including, but not limited to autologous T cells); mixing the one or more T cells with the modified VIP-R antagonists of any preceding aspect (including, but not limited to SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39) or pharmaceutical composition of any preceding aspect. For example, disclosed herein are methods of treating a cancer or a chronic infection in a subject in need, comprising obtaining one or more T cells; mixing the one or more T cells with the modified VIP-R antagonist as set forth in SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13,SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39. In some aspect, the method further comprises mixing the one or more T cells is in combination with an anti-CD3 antibody and / or an anti-CD28 antibody. In certain embodiments, the method further comprises administering to the subject a therapeutically effective amount of a phosphatidylinositol 3-kinase (PI3K) inhibitor (including, for example, a PI3Ka inhibitor, a PI3KP inhibitor, a PI3K5 inhibitor, or a PI3Ky inhibitor including, but not limited to idelalisib, copanlisib, duvelisib, alpelisib, umbralisib, buparlisib, copanlisib, dactolisib, leniolisib, parsaclisib, paxalisib, taselisib, zandelisib, inavolisib, apitolisib, bimiralisib, eganelisib, fimepinostat, gedatolisib, linperlisib, nemiralisib, pilaralisib, samotolisib, seletalisib, serabelisib, sonolisib, tenalisib, voxtalisib, AMG 319, AZD8186, GSK2636771, SF1126, acalisib, omipalisib, AZD8835, CAL263, GSK1059615, MEN1611, PWT33597, TG100-115, or ZSTK474). In certain embodiments, the method further comprises administering to the subject a therapeutically effective amount of an immune checkpoint blockade. In some embodiments, the immune checkpoint blockade is a PD-1 inhibitor, a PD-L1 inhibitor, a CTLA-4 inhibitor, an anti-TIM3 inhibitor, an anti-LAG3 inhibitor, an anti-CD47 inhibitor, imiquimod, polyinosinic-polycytidylic acid-poly-l-lysine carboxymethylcellulose (poly-ICLC) , pexidartinib, an anti-TIGIT inhibitor, an anti-B7-H3 inhibitor, an anti-B7-H4 inhibitor, an anti-A2aR inhibitor, an anti-CD73 inhibitor, an anti- NKG2A inhibitor, an anti-PVRIG / PVRL2 inhibitor, an anti-CEACAMl inhibitor, an anti- CEACAM5 inhibitor, an anti-CEACAM6 inhibitor, an focal adhesion kinase (FAK) inhibitor, a CCL2 / CCR2 inhibitor, an anti-leukemia inhibitory factor (LIF) inhibitor, an anti-CD47 / SIRPa inhibitor, an anti-colony-stimulating factor (CSF)-l inhibitor, an anti-IL-1 inhibitor, an anti-IL- 1R3 inhibitor, an anti-IL-8 inhibitor, an anti-semaphorin 4D (Sema4D) inhibitor, an angiopoietin(Ang)-2 inhibitor, a CLEVER- 1 inhibitor, Axl-targeted enapotamab vedotin (EnaV), or an anti-phosphatidylserine inhibitor including, but not limited to pembrolizumab, nivolumab, cemiplimab, dostarlimab, atezolizumab, avelumab, durvalumab, or ipilimumab.IV. BRIEF DESCRIPTION OF THE DRAWINGS13. The accompanying drawings, which are incorporated in and constitute a part of this specification, illustrate several embodiments and together with the description illustrate the disclosed compositions and methods.14. Figure 1 shows ANT308 conjugated to the Fc domain of an immunoglobulin.15. Figure 2 shows that ANT308 conjugated to polyethylene glycol or human 1g FC fragment potently activates human T cells. Cryopreserved samples of 5 human volunteer PBMCs were thawed, resuspended in RPMI media, and rested overnight at 37 °C in a 5% C02 humidified incubator in RPMI media supplemented with 10% FBS,100U / ml Penicilin- Streptomycin, MEM nonessential amino acids, 20mM N-2-hydroxyethylpiperazine-N-2-ethane sulfonic acid (HEPES), 50mM 2-mercaptoethanol, and 50U / ml human IL-2 (RPMI culture media). The following day, the cell pellet of mononuclear cells from each donor was collected by centrifugation and then resuspended in 1ml automatics media (Miltenyi Biotec), and the cell concentration was determined. T cells were selected from each donor's mononuclear cells using the Miltenyi Biotec pan T cell isolation kit. For T cell purification, 1 mL of Pan T Cell Biotin- Antibody Cocktail consisting of biotin-conjugated monoclonal antibodies against CD14, CD15, CD16, CD19, CD34, CD36, CD56, CD123, and CD235 and 2 mL of Pan T Cell MicroBeads conjugated to monoclonal anti-biotin were added to every 109mononuclear cells. A population of enriched (>95% CD3 expression) T cells were obtained by performing magnetic absorption of cells lacking CD3 expression and decorated with the anti-Biotin microbeads according to the manufacturer’s instructions. Purified T cells from 5 donors were pooled and cultured in 200 mL RPMI culture media in individual wells of a 96 round-bottom culture plate at a cell concentration of 1 x 106cells / mL at 37 °C in a 5% CO2 humidified incubator. T cells were activated by the addition of a 1.5ul / ml soluble aCD3 / CD28 T activator (ImmunoCult) in the presence of 0.03 mM ANT308 peptide, or 0.03 mM ANT308-PEG conjugate, or 0.03 mM ANT308-Fc3 fusion polypeptide. Following 48 hours of incubation, the number of activated T cells per well was determined by flow cytometry after staining with an antibody cocktail to CD3, CD8, CD4, CD69, Granzyme B. The viable CD3+ CD4+ CD69+ T cells in each well were enumerated using live / dead gating with aqua. Each culture condition was done in triplicate or quadruplicate, with average values (+SD) shown.16. Figure 3 shows that treatment with the VIP-antagonist peptide ANT308 or ANT3O8- conjugates increases the survival of C1498 leukemic mice. C57B1 / 6 mice were given a lethal dose of the acute myeloid leukemia cell line tumor C1498 AML (1 xlO6by intravenous injection). Eight days later, when the frequency of circulating leukemic blasts in the blood was 5%-10% of the leukocytes, mice were treated with 14 daily subcutaneous injections of 9 nMoles of the ANT308 peptide dissolved in phosphate buffered saline or four twice weekly injections of 9 nMoles of ANT308-PEG or ANT3O8-Fc fusion polypeptide. Control mice received 14 subcutaneous injections of 9 moles of a 28 amino acid scrambled peptide based upon the sequence of VIP. The fraction of surviving mice in each group is shown, with log-rank teststatistical comparisons of the ANT308-PEG and ANT308-Fc fusion groups to the group receiving ANT308 and the group receiving scrambled peptide.17. Figure 4 shows that treatment with the VIP-antagonist peptide ANT308 or ANT3O8- conjugates increases the survival of P815 leukemic mice. DBA / 2 mice were given a lethal dose of the astrocytoma leukemia cell line tumor P815 (1 x 10sby subcutaneous injection). Eight days later, when the subcutaneous myeloid sarcoma tumor had grown to approximately 100-200 mm3volume, mice were treated with 14 daily subcutaneous injections of 3 nMoles of the ANT308 peptide dissolved in phosphate-buffered saline or four twice weekly injections of 3 nMoles of ANT3O8-PEG or ANT308-Fc fusion polypeptide. Control mice received 14 subcutaneous injections of 3 moles of a 28 amino acid scrambled peptide based upon the sequence of VIP. The fraction of surviving mice in each group is shown, with log-rank test statistical comparisons of the ANT308-PEG and ANT308-Fc fusion groups to the group receiving ANT308 and the group receiving scrambled peptide.18. Figure 5 shows that four doses of ANT308-Fc3 fusion were more effective than 28 doses of ANT308 in a P815 mastocytoma model.19. Figure 6 shows that the high frequency of antigen- specific CD8+ T cells induced in DBA / 2 mice with P815 after treatment with ANT308-Fc3 fusion.20. Figure 7 shows the dose-dependent survival after a single dose of ANT308-Fc fusion in mice with C 1498 leukemia.DETAILED DESCRIPTION21. Before the present compounds, compositions, articles, devices, and / or methods are disclosed and described, it is to be understood that they are not limited to specific synthetic methods or specific recombinant biotechnology methods unless otherwise specified, or to particular reagents unless otherwise specified, as such may, of course, vary. It is also to be understood that the terminology used herein is for the purpose of describing particular embodiments only and is not intended to be limiting.A. Definitions22. As used in the specification and the appended claims, the singular forms “a,” “an” and “the” include plural referents unless the context clearly dictates otherwise. Thus, for example, reference to “a pharmaceutical carrier” includes mixtures of two or more such carriers, and the like.23. Ranges can be expressed herein as from “about” one particular value, and / or to “about” another particular value. When such a range is expressed, another embodiment includesfrom the one particular value and / or to the other particular value. Similarly, when values are expressed as approximations, by use of the antecedent “about,” it will be understood that the particular value forms another embodiment. It will be further understood that the endpoints of each of the ranges are significant both in relation to the other endpoint, and independently of the other endpoint. It is also understood that there are a number of values disclosed herein, and that each value is also herein disclosed as “about” that particular value in addition to the value itself. For example, if the value “10” is disclosed, then “about 10” is also disclosed. It is also understood that when a value is disclosed that “less than or equal to” the value, “greater than or equal to the value” and possible ranges between values are also disclosed, as appropriately understood by the skilled artisan. For example, if the value “10” is disclosed the “less than or equal to 10”as well as “greater than or equal to 10” is also disclosed. It is also understood that the throughout the application, data is provided in a number of different formats, and that this data, represents endpoints and starting points, and ranges for any combination of the data points. For example, if a particular data point “10” and a particular data point 15 are disclosed, it is understood that greater than, greater than or equal to, less than, less than or equal to, and equal to 10 and 15 are considered disclosed as well as between 10 and 15. It is also understood that each unit between two particular units are also disclosed. For example, if 10 and 15 are disclosed, then 11, 12, 13, and 14 are also disclosed.24. In this specification and in the claims which follow, reference will be made to a number of terms which shall be defined to have the following meanings:25. “Optional” or “optionally” means that the subsequently described event or circumstance may or may not occur, and that the description includes instances where said event or circumstance occurs and instances where it does not.26. An "increase" can refer to any change that results in a greater amount of a symptom, disease, composition, condition or activity. An increase can be any individual, median, or average increase in a condition, symptom, activity, composition in a statistically significant amount. Thus, the increase can be a 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, or 100% increase so long as the increase is statistically significant.27. A "decrease" can refer to any change that results in a smaller amount of a symptom, disease, composition, condition, or activity. A substance is also understood to decrease the genetic output of a gene when the genetic output of the gene product with the substance is less relative to the output of the gene product without the substance. Also for example, a decrease can be a change in the symptoms of a disorder such that the symptoms are less than previously observed. A decrease can be any individual, median, or average decrease in a condition,symptom, activity, composition in a statistically significant amount. Thus, the decrease can be a 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, or 100% decrease so long as the decrease is statistically significant.28. "Inhibit," "inhibiting," and "inhibition" mean to decrease an activity, response, condition, disease, or other biological parameter. This can include but is not limited to the complete ablation of the activity, response, condition, or disease. This may also include, for example, a 10% reduction in the activity, response, condition, or disease as compared to the native or control level. Thus, the reduction can be a 10, 20, 30, 40, 50, 60, 70, 80, 90, 100%, or any amount of reduction in between as compared to native or control levels.29. By “reduce” or other forms of the word, such as “reducing” or “reduction,” is meant lowering of an event or characteristic (e.g., tumor growth). It is understood that this is typically in relation to some standard or expected value, in other words it is relative, but that it is not always necessary for the standard or relative value to be referred to. For example, “reduces tumor growth” means reducing the rate of growth of a tumor relative to a standard or a control.30. By “prevent” or other forms of the word, such as “preventing” or “prevention,” is meant to stop a particular event or characteristic, to stabilize or delay the development or progression of a particular event or characteristic, or to minimize the chances that a particular event or characteristic will occur. Prevent does not require comparison to a control as it is typically more absolute than, for example, reduce. As used herein, something could be reduced but not prevented, but something that is reduced could also be prevented. Likewise, something could be prevented but not reduced, but something that is prevented could also be reduced. It is understood that where reduce or prevent are used, unless specifically indicated otherwise, the use of the other word is also expressly disclosed.31. The term “subject” refers to any individual who is the target of administration or treatment. The subject can be a vertebrate, for example, a mammal. In one aspect, the subject can be human, non-human primate, bovine, equine, porcine, canine, or feline. The subject can also be a guinea pig, rat, hamster, rabbit, mouse, or mole. Thus, the subject can be a human or veterinary patient. The term “patient” refers to a subject under the treatment of a clinician, e.g., physician.32. The term “therapeutically effective” refers to the amount of the composition used is of sufficient quantity to ameliorate one or more causes or symptoms of a disease or disorder. Such amelioration only requires a reduction or alteration, not necessarily elimination.33. The term “treatment” refers to the medical management of a patient with the intent to cure, ameliorate, stabilize, or prevent a disease, pathological condition, or disorder. This termincludes active treatment, that is, treatment directed specifically toward the improvement of a disease, pathological condition, or disorder, and also includes causal treatment, that is, treatment directed toward removal of the cause of the associated disease, pathological condition, or disorder. In addition, this term includes palliative treatment, that is, treatment designed for the relief of symptoms rather than the curing of the disease, pathological condition, or disorder; preventative treatment, that is, treatment directed to minimizing or partially or completely inhibiting the development of the associated disease, pathological condition, or disorder; and supportive treatment, that is, treatment employed to supplement another specific therapy directed toward the improvement of the associated disease, pathological condition, or disorder.34. "Biocompatible" generally refers to a material and any metabolites or degradation products thereof that are generally non-toxic to the recipient and do not cause significant adverse effects to the subject.35. "Comprising" is intended to mean that the compositions, methods, etc. include the recited elements, but do not exclude others. "Consisting essentially of’ when used to define compositions and methods, shall mean including the recited elements, but excluding other elements of any essential significance to the combination. Thus, a composition consisting essentially of the elements as defined herein would not exclude trace contaminants from the isolation and purification method and pharmaceutically acceptable carriers, such as phosphate buffered saline, preservatives, and the like. "Consisting of" shall mean excluding more than trace elements of other ingredients and substantial method steps for administering the compositions provided and / or claimed in this disclosure. Embodiments defined by each of these transition terms are within the scope of this disclosure.36. A “control” is an alternative subject or sample used in an experiment for comparison purposes. A control can be "positive" or "negative."37. “Effective amount” of an agent refers to a sufficient amount of an agent to provide a desired effect. The amount of agent that is “effective” will vary from subject to subject, depending on many factors such as the age and general condition of the subject, the particular agent or agents, and the like. Thus, it is not always possible to specify a quantified “effective amount.” However, an appropriate “effective amount” in any subject case may be determined by one of ordinary skill in the art using routine experimentation. Also, as used herein, and unless specifically stated otherwise, an “effective amount” of an agent can also refer to an amount covering both therapeutically effective amounts and prophylactically effective amounts. An “effective amount” of an agent necessary to achieve a therapeutic effect may vary according to factors such as the age, sex, and weight of the subject. Dosage regimens can be adjusted toprovide the optimum therapeutic response. For example, several divided doses may be administered daily or the dose may be proportionally reduced as indicated by the exigencies of the therapeutic situation.38. A "pharmaceutically acceptable" component can refer to a component that is not biologically or otherwise undesirable, i.e., the component may be incorporated into a pharmaceutical formulation provided by the disclosure and administered to a subject as described herein without causing significant undesirable biological effects or interacting in a deleterious manner with any of the other components of the formulation in which it is contained. When used in reference to administration to a human, the term generally implies the component has met the required standards of toxicological and manufacturing testing or that it is included on the Inactive Ingredient Guide prepared by the U.S. Food and Drug Administration.39. "Pharmaceutically acceptable carrier" (sometimes referred to as a “carrier”) means a carrier or excipient that is useful in preparing a pharmaceutical or therapeutic composition that is generally safe and non-toxic and includes a carrier that is acceptable for veterinary and / or human pharmaceutical or therapeutic use. The terms "carrier" or "pharmaceutically acceptable carrier" can include, but are not limited to, phosphate buffered saline solution, water, emulsions (such as an oil / water or water / oil emulsion) and / or various types of wetting agents. As used herein, the term "carrier" encompasses, but is not limited to, any excipient, diluent, filler, salt, buffer, stabilizer, solubilizer, lipid, stabilizer, or other material well known in the art for use in pharmaceutical formulations and as described further herein.40. “Pharmacologically active” (or simply “active”), as in a “pharmacologically active” derivative or analog, can refer to a derivative or analog (e.g., a salt, ester, amide, conjugate, metabolite, isomer, fragment, etc.) having the same type of pharmacological activity as the parent compound and approximately equivalent in degree.41. “Therapeutic agent” refers to any composition that has a beneficial biological effect. Beneficial biological effects include both therapeutic effects, e.g., treatment of a disorder or other undesirable physiological condition, and prophylactic effects, e.g., prevention of a disorder or other undesirable physiological condition (e.g., a non-immunogenic cancer). The terms also encompass pharmaceutically acceptable, pharmacologically active derivatives of beneficial agents specifically mentioned herein, including, but not limited to, salts, esters, amides, proagents, active metabolites, isomers, fragments, analogs, and the like. When the terms “therapeutic agent” is used, then, or when a particular agent is specifically identified, it is to be understood that the term includes the agent per se as well as pharmaceutically acceptable,pharmacologically active salts, esters, amides, proagents, conjugates, active metabolites, isomers, fragments, analogs, etc.42. “Therapeutically effective amount” or “therapeutically effective dose” of a composition (e.g. a composition comprising an agent) refers to an amount that is effective to achieve a desired therapeutic result. In some embodiments, a desired therapeutic result is the control of type I diabetes. In some embodiments, a desired therapeutic result is the control of obesity. Therapeutically effective amounts of a given therapeutic agent will typically vary with respect to factors such as the type and severity of the disorder or disease being treated and the age, gender, and weight of the subject. The term can also refer to an amount of a therapeutic agent, or a rate of delivery of a therapeutic agent (e.g., amount over time), effective to facilitate a desired therapeutic effect, such as pain relief. The precise desired therapeutic effect will vary according to the condition to be treated, the tolerance of the subject, the agent and / or agent formulation to be administered (e.g., the potency of the therapeutic agent, the concentration of agent in the formulation, and the like), and a variety of other factors that are appreciated by those of ordinary skill in the art. In some instances, a desired biological or medical response is achieved following administration of multiple dosages of the composition to the subject over a period of days, weeks, or years.43. Throughout this application, various publications are referenced. The disclosures of these publications in their entireties are hereby incorporated by reference into this application in order to more fully describe the state of the art to which this pertains. The references disclosed are also individually and specifically incorporated by reference herein for the material contained in them that is discussed in the sentence in which the reference is relied upon.B. Compositions44. Disclosed are the components to be used to prepare the disclosed compositions as well as the compositions themselves to be used within the methods disclosed herein. These and other materials are disclosed herein, and it is understood that when combinations, subsets, interactions, groups, etc. of these materials are disclosed that while specific reference of each various individual and collective combinations and permutation of these compounds may not be explicitly disclosed, each is specifically contemplated and described herein. For example, if a particular VIP receptor antagonist is disclosed and discussed and a number of modifications that can be made to a number of molecules including the modified VIP receptor antagonist are discussed, specifically contemplated is each and every combination and permutation of the VIP receptor antagonist and the modifications that are possible unless specifically indicated to the contrary. Thus, if a class of molecules A, B, and C are disclosed as well as a class of moleculesD, E, and F and an example of a combination molecule, A-D is disclosed, then even if each is not individually recited each is individually and collectively contemplated meaning combinations, A-E, A-F, B-D, B-E, B-F, C-D, C-E, and C-F are considered disclosed. Likewise, any subset or combination of these is also disclosed. Thus, for example, the sub-group of A-E, B-F, and C-E would be considered disclosed. This concept applies to all aspects of this application including, but not limited to, steps in methods of making and using the disclosed compositions. Thus, if there are a variety of additional steps that can be performed it is understood that each of these additional steps can be performed with any specific embodiment or combination of embodiments of the disclosed methods.45. Vasoactive intestinal polypeptide (VIP) is a 28-residue neuropeptide (HSDAVFTDNYTRLRKQMAVKKYLNSILN (SEQ ID NO: 1)) with potent anti-inflammatory activity and immunosuppressive effects on T cells. VIP is a multifunctional endogenous polypeptide that modulates both innate and adaptive immunity at multiple levels of immune cell differentiation and activation. The VIP receptors VPAC1 and VPAC2 are widely expressed throughout the body with differential expression on the surface of immune cells. Furthermore, overexpression of VIP and its receptors is in breast, prostate, and lung cancers, wherein VIP promotes growth and metastasis in tumors.46. VIP is typically secreted by a variety of cells such as neurons (in both the central and peripheral nervous systems) B-cells, T-cells, and accessory cells. VIP and the closely related neuropeptide pituitary adenylyl cyclase-activating polypeptide (PACAP) bind to three known receptors- VPAC1, VPAC2, and PAC1. It is believed that T-cells and dendritic cells (DC) express VPAC1 and VPAC2, but not PAC1. PAC1 is mainly expressed on neuron and endocrine cells in the brain and pituitary and adrenal glands, and in most forms selectively binds PACAP.47. In adaptive immune responses, VIP polarizes CD4+T-cells to an immunosuppressive Th2 response while suppressing the Thl responses. T-cell activation and differentiation induce VPAC2 expression, while VPAC1 is down-regulated following stimulation of human blood T- cells with anti-CD3 monoclonal antibody plus PMA. VIP also acts on APC and regulates their function. Through the VPAC1 receptor, VIP leads to the development of bone marrow-derived tolerogenic DCs in vitro and in vivo. In a mouse model of bone marrow transplantation, DC that were differentiated in the presence of VIP, and then transplanted along with bone marrow cells and splenic T-cells induced the generation of regulatory T-cells and protected mice from acute graft versus host disease (GvHD). Th2 polarization is achieved partly through VIP regulation of costimulatory signals on antigen presenting cells (APC) and inhibition of IL-1, TNF-D, IL-6,and IL- 12 production. VIP suppresses expression of the pattern recognition receptors toll-like receptor (TLR) 2 and TLR4 on APC and inhibits TLR3- signaling. Conversely, binding of ligands to TLR2, TLR4, and TLR7 down-regulate VPAC2 expression on APC.48. We have recently developed a series of VIP-receptor antagonists dubbed ANT002- ANT308. These peptides possess a modified, positively charged N-terminus. The ANT peptides enhance T-cell proliferation in vitro and improve T-cell dependent anti -tumor response in murine models of acute myeloid leukemia (AML). Furthermore, treatment with ANT peptides concomitant with anti-PD-1 -combination therapy enhances both intra-tumoral T-cell proliferation as well as increases tumor-antigen-specific T cells within the tumor microenvironment (TME) of pancreatic ductal adenocarcinoma (PDAC) tumors (Figure 1). Despite the promising anti-tumor properties of these VIP antagonist derivatives, peptide therapeutics commonly suffer from poor metabolic stability and consequently exhibit short halflife and fast elimination in vivo. These limitations pose a significant barrier to the utility of therapeutic peptides as competent drug candidates.49. The term “VIP antagonist” refers to any molecule that inhibits or detracts from the ability of VIP to alter immune responses. VIP antagonists are known including VIP analogues, VIP fragments, growth hormone-releasing factor analogs and hybrid peptides. A number of VIP antagonists are disclosed in U.S. Patent Numbers 5,565,424; 7,094,755; 6,828,304, and are all hereby incorporated by reference. Some examples of VIP antagonist include VIP-hyb also known as VIPhybrid, i.e., a hybrid peptide of neurotensin and VIP consisting of an N-terminal KPRRPY (SEQ ID NO: 17), also designated neurotensin (6-11)] followed by the C-terminal 22 amino acids of VIP, i.e., TDNYTRLRKQMAVKKYLNSILN (SEQ ID NO: 18), also designated VIP (7-28); ANT005 KPRRPYTDNCTRLRKQMAVKKYLNSILN (SEQ ID NO: 4), ANT008 KPRRPYTDNYTRLRKQMAVKKYLNLILN (SREQ ID NO: 5), ANT058 KPRRPY ADNYTRLRKQMAVNKYLNLILN (SEQ ID NO: 6), ANT105KPRRPY A VNYTRLRKQIAVKKYLMSILN (SEQ ID NO: 7), ANT107 KPRRPYAVNYTRLRKQMAVNKYLMSILN (SEQ ID NO: 8), ANTI 14 KPRRPY ADNCTRLRKQIAVNKKYLNSILN (SEQ ID NO: 9), ANT195 KPRRPYTVNYTSLRKQIAVKKYLMLILN (SEQ ID NO: 10), ANT197 KPRRPYTDNCTSLRKQIAVNKYLNLILN (SEQ ID NO: 11), ANT202 KPRRPYAVNCTSLRKQIAVNKYLNSILN (SEQ ID NO: 12), ANT203 KPRRPY A VNCTSLRKQIAVKKYLMSILN (SEQ ID NO: 13), ANT219 KPRRPYTVNCTSLRKQIAVKKYLMLILN (SEQ ID NO: 14), ANT300 KPRRPYTSDYTRLRKQMAVKKYLNSILN (SEQ ID NO: 15), and ANT308KPRRPYTSDYTRLRKQMAVKKYLNLILN (SEQ ID NO: 16) . It is contemplated that any of these molecules may be modified with a chemical modification (including, but not limited to amino terminus acetylation, carboxyl terminus pegylation, or covalent staple) or conjugation of an immunoglobulin Fc domain (also referred to herein as an Fc fusion).50. Accordingly, in one aspect, disclosed herein are modified vasoactive intestinal peptide receptor (VIP-R) antagonists comprising KPRRPYX1X2X3X4TX5LRKQX6AVX7X8KYLX9X10ILN (SEQ ID NO: 3) or a fragment thereof, wherein X1is T or A; X2is D, V, or S; X3is N or D; X4is Y or C; X5is R or S; X6is M or I; X7is K or N; X8is K; X9is N or M; X10is S, or L; and provided that the peptide is not KPRRPYTDNYTRLRKQMAVKKYLNSILN (SEQ ID NO: 2) or the peptide is not the combination wherein X1is T, X2is D, X3is N; X4is Y, X5is R, X6is M, X7is K, X9is N, and X10is S (such as, for example, ANT005 KPRRPYTDNCTRLRKQMAVKKYLNSILN (SEQ ID NO: 4), ANT008 KPRRPYTDNYTRLRKQMAVKKYLNLILN (SREQ ID NO: 5), ANT058 KPRRPYADNYTRLRKQMAVNKYLNLILN (SEQ ID NO: 6), ANT105 KPRRPYAVNYTRLRKQIAVKKYLMSILN (SEQ ID NO: 7), ANT107 KPRRPYAVNYTRLRKQMAVNKYLMSILN (SEQ ID NO: 8), ANTI 14 KPRRPYADNCTRLRKQIAVNKKYLNSILN (SEQ ID NO: 9), ANT195 KPRRPYTVNYTSLRKQIAVKKYLMLILN (SEQ ID NO: 10), ANT197 KPRRPYTDNCTSLRKQIAVNKYLNLILN (SEQ ID NO: 11), ANT202 KPRRPYAVNCTSLRKQIAVNKYLNSILN (SEQ ID NO: 12), ANT203 KPRRPYAVNCTSLRKQIAVKKYLMSILN (SEQ ID NO: 13), ANT219 KPRRPYTVNCTSLRKQIAVKKYLMLILN (SEQ ID NO: 14), ANT300 KPRRPYTSDYTRLRKQMAVKKYLNSILN (SEQ ID NO: 15), or ANT308 KPRRPYTSDYTRLRKQMAVKKYLNLILN (SEQ ID NO: 16); and wherein the VIP-R antagonist comprises is conjugated to an immunoglobulin Fc domain at the carboxyl terminus of the VIP-R antagonist peptide).51. Also disclosed herein are modified vasoactive intestinal peptide receptor (VIP-R) antagonists comprising KPRRPYX1X2X3X4TX5LRKQX6AVX7KYLX8X9ILN (SEQ ID NO: 21) or a fragment thereof, wherein X1is T or A; X2is D, V, or S; X3is N or D; X4is Y or C; X5is R or S; X6is M or I; X7is K or N; X8is N or M; X9is S, or L; and provided that the peptide is not KPRRPYTDNYTRLRKQMAVKKYLNSILN (SEQ ID NO: 2) or the peptide is not the combination wherein X1is T, X2is D, X3is N; X4is Y, X5is R, X6is M, X7is K, X8is N, and X9is S (such as, for example, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO:13, SEQ ID NO: 14, SEQ ID NO: 15, and / or SEQ ID NO: 16); and wherein the V1P-R antagonist is conjugated to an immunoglobulin Fc domain at the carboxyl terminus of the VIP-R antagonist peptide).52. In one aspect disclosed herein are modified VIP-R antagonists, wherein the modification comprises an Fc domain (such as, for example, SEQ ID NO: 26) conjugated to the carboxyl terminus of the VIP-R antagonist peptide (such as, for example, ANT005 KPRRPYTDNCTRLRKQMAVKKYLNSILN (SEQ ID NO: 4), ANT008 KPRRPYTDNYTRLRKQMAVKKYLNLILN (SREQ ID NO: 5), ANT058 KPRRPYADNYTRLRKQMAVNKYLNLILN (SEQ ID NO: 6), ANT 105 KPRRPYAVNYTRLRKQIAVKKYLMSILN (SEQ ID NO: 7), ANT107 KPRRPYAVNYTRLRKQMAVNKYLMSILN (SEQ ID NO: 8), ANTI 14 KPRRPYADNCTRLRKQIAVNKKYLNSILN (SEQ ID NO: 9), ANT195 KPRRPYTVNYTSLRKQIAVKKYLMLILN (SEQ ID NO: 10), ANT197 KPRRPYTDNCTSLRKQIAVNKYLNLILN (SEQ ID NO: 11), ANT202 KPRRPYAVNCTSLRKQIAVNKYLNSILN (SEQ ID NO: 12), ANT203 KPRRPYAVNCTSLRKQIAVKKYLMSILN (SEQ ID NO: 13), ANT219 KPRRPYTVNCTSLRKQIAVKKYLMLILN (SEQ ID NO: 14), ANT300 KPRRPYTSDYTRLRKQMAVKKYLNSILN (SEQ ID NO: 15), or ANT308 KPRRPYTSDYTRLRKQMAVKKYLNLILN (SEQ ID NO: 16). In some aspects the Fc domain conjugated modified VIP-R antagonist (also referred to herein as a VIP-R antagonist Fc fusion) further comprises a linker (such as, for example a GS linker, SEQ ID NO: 22), a signal peptide (such as, for example, SEQ ID NO: 24), and a hinge domain (such as, for example, SEQ ID NO: 25). For example, disclosed herein are modified VIP-R antagonists of any preceding aspect, wherein the modification comprises an Fc domain conjugated to the carboxyl terminus of the VIP-R antagonist peptide as set forth in SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39.53. Also disclosed herein are pharmaceutical compositions comprising any of the modified VIP-R antagonist disclosed herein and a pharmaceutically acceptable carrier.54. In one aspect, disclosed herein are nucleic acids (such as, for example, GGATCCGCCGCCACCATGGGCTGGACCCTGGTGTTTCTGTTTCTCCTGAGCGTGACC GCCGGCGTGCACAGCAAGCCTAGAAGACCTTACACAAGCGACTACACAAGACTGAG AAAGCAGATGGCCGTGAAGAAGTATCTGAACTTGATACTGAACGGTAGCGAAAGTA AATATGGGCCTCCGTGCCCGCCATGTCCCGCCCCTGAGGCCGCCGGCGGCCCTAGCGTGTTCCTGTTCCCTCCTAAGCCTAAGGACACCCTGATGATCAGCAGAACCCCTGAG GTGACCTGCGTGGTGGTGGACGTGAGCCAAGAGGACCCTGAGGTGCAGTTCAACTG GTACGTGGACGGCGTGGAGGTGCACAACGCCAAGACCAAGCCTAGAGAGGAGCAG TTCAACAGCACCTACAGAGTGGTGAGCGTGCTGACCGTGCTGCACCAAGACTGGCT GAACGGCAAGGAGTACAAGTGCAAGGTGAGCAACAAGGGCCTGCCTAGCAGCATC GAGAAGACCATCAGCAAGGCCAAGGGACAGCCTAGAGAGCCTCAAGTGTACACCC TGCCTCCTAGCCAAGAGGAGATGACCAAGAACCAAGTGAGCCTGACCTGCCTGGTG AAGGGCTTCTACCCTAGCGACATCGCCGTGGAGTGGGAGAGCAACGGACAGCCTGA GAACAACTACAAGACCACCCCTCCTGTGCTGGACAGCGACGGCAGCTTCTTCCTGTA CAGCAGACTGACCGTGGACAAGAGCAGATGGCAAGAGGGCAACGTGTTCAGCTGC AGCGTGATGCACGAGGCCCTGCACAACCACTACACACAGAAGAGCCTGAGCCTGAG CCTGGGCAAGTAAATCTAGAAGCTT (SEQ ID NO: 40) encoding any of the modified VIP- R antagonists disclosed herein. Also disclosed herein are recombinant vectors comprising said nucleic acids. In one aspect, disclosed herein are expression systems or cells comprising a recombinant vector.1. Homology / identity55. It is understood that one way to define any known variants and derivatives or those that might arise, of the disclosed genes and proteins herein is through defining the variants and derivatives in terms of homology to specific known sequences. Specifically disclosed are variants of these and other genes and proteins herein disclosed which have at least, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 percent homology to the stated sequence. Those of skill in the art readily understand how to determine the homology of two proteins or nucleic acids, such as genes. For example, the homology can be calculated after aligning the two sequences so that the homology is at its highest level.56. Another way of calculating homology can be performed by published algorithms. Optimal alignment of sequences for comparison may be conducted by the local homology algorithm of Smith and Waterman Adv. Appl. Math. 2: 482 (1981), by the homology alignment algorithm of Needleman and Wunsch, J. MoL Biol. 48: 443 (1970), by the search for similarity method of Pearson and Lipman, Proc. Natl. Acad. Sci. U.S.A. 85: 2444 (1988), by computerized implementations of these algorithms (GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin Genetics Software Package, Genetics Computer Group, 575 Science Dr., Madison, WI), or by inspection.57. The same types of homology can be obtained for nucleic acids by for example the algorithms disclosed in Zuker, M. Science 244:48-52, 1989, Jaeger et al. Proc. Natl. Acad. Sei. USA 86:7706-7710, 1989, Jaeger et al. Methods Enzymol. 183:281-306, 1989 which are herein incorporated by reference for at least material related to nucleic acid alignment.2. Peptides a) Protein variants58. As discussed herein there are numerous variants of the modified VIP receptor antagonists that are known and herein contemplated. Protein variants and derivatives are well understood to those of skill in the art and in can involve amino acid sequence modifications. For example, amino acid sequence modifications typically fall into one or more of three classes: substitutional, insertional or deletional variants. Insertions include amino and / or carboxyl terminal fusions as well as intrasequence insertions of single or multiple amino acid residues. Insertions ordinarily will be smaller insertions than those of amino or carboxyl terminal fusions, for example, on the order of one to four residues. Immunogenic fusion protein derivatives, such as those described in the examples, are made by fusing a polypeptide sufficiently large to confer immunogenicity to the target sequence by cross-linking in vitro or by recombinant cell culture transformed with DNA encoding the fusion. Deletions are characterized by the removal of one or more amino acid residues from the protein sequence. Typically, no more than about from 2 to 6 residues are deleted at any one site within the protein molecule. These variants ordinarily are prepared by site specific mutagenesis of nucleotides in the DNA encoding the protein, thereby producing DNA encoding the variant, and thereafter expressing the DNA in recombinant cell culture. Techniques for making substitution mutations at predetermined sites in DNA having a known sequence are well known, for example M13 primer mutagenesis and PCR mutagenesis. Amino acid substitutions are typically of single residues, but can occur at a number of different locations at once; insertions usually will be on the order of about from 1 to 10 amino acid residues; and deletions will range about from 1 to 30 residues. Deletions or insertions preferably are made in adjacent pairs, i.e. a deletion of 2 residues or insertion of 2 residues. Substitutions, deletions, insertions or any combination thereof may be combined to arrive at a final construct. The mutations must not place the sequence out of reading frame and preferably will not create complementary regions that could produce secondary mRNA structure. Substitutional variants are those in which at least one residue has been removed and a different residue inserted in its place. Such substitutions generally are made in accordance with the following Tables 3 and 4 and are referred to as conservative substitutions.TABLE 3:Amino Acid AbbreviationsAmino Acid AbbreviationsAlanine Ala A allosoleucine AlleArginine Arg R asparagine Asn N aspartic acid Asp DCysteine Cys C glutamic acid Glu EGlutamine Gin QGlycine Gly GHistidine His HIsolelucine He ILeucine Leu LLysine Lys K phenylalanine Phe F proline Pro P pyroglutamic acid pGluSerine Ser SThreonine Thr TTyrosine Tyr YTryptophan Trp WValine Vai VTABLE 4:Amino Acid SubstitutionsOriginal Residue Exemplary Conservative Substitutions, others are known in the art.Ala Ser Arg Lys; Gin Asn Gin; His Asp Glu Cys Ser Gin Asn, Lys Glu Asp Gly Pro His Asn;Gln lie Leu; V iLeu lie; Vai Lys Arg; Gin Met Leu; He Phe Met; Leu; Tyr Ser Thr Thr Ser Trp Tyr Tyr Trp; Phe Vai He; Leu59. Substantial changes in function or immunological identity are made by selecting substitutions that are less conservative than those in Table 4, i.e., selecting residues that differ more significantly in their effect on maintaining (a) the structure of the polypeptide backbone in the area of the substitution, for example as a sheet or helical conformation, (b) the charge or hydrophobicity of the molecule at the target site or (c) the bulk of the side chain. The substitutions which in general are expected to produce the greatest changes in the protein properties will be those in which (a) a hydrophilic residue, e.g. seryl or threonyl, is substitutedfor (or by) a hydrophobic residue, e.g. leucyl, isoleucyl, phenylalanyl, valyl or alanyl; (b) a cysteine or proline is substituted for (or by) any other residue; (c) a residue having an electropositive side chain, e.g., lysyl, arginyl, or histidyl, is substituted for (or by) an electronegative residue, e.g., glutamyl or aspartyl; or (d) a residue having a bulky side chain, e.g., phenylalanine, is substituted for (or by) one not having a side chain, e.g., glycine, in this case, (e) by increasing the number of sites for sulfation and / or glycosylation.60. For example, the replacement of one amino acid residue with another that is biologically and / or chemically similar is known to those skilled in the art as a conservative substitution. For example, a conservative substitution would be replacing one hydrophobic residue for another, or one polar residue for another. The substitutions include combinations such as, for example, Gly, Ala; Vai, He, Leu; Asp, Glu; Asn, Gin; Ser, Thr; Lys, Arg; and Phe, Tyr. Such conservatively substituted variations of each explicitly disclosed sequence are included within the mosaic polypeptides provided herein.61. Substitutional or deletional mutagenesis can be employed to insert sites for N- glycosylation (Asn-X-Thr / Ser) or O-glycosylation (Ser or Thr). Deletions of cysteine or other labile residues also may be desirable. Deletions or substitutions of potential proteolysis sites, e.g. Arg, is accomplished for example by deleting one of the basic residues or substituting one by glutaminyl or histidyl residues.62. Certain post-translational derivatizations are the result of the action of recombinant host cells on the expressed polypeptide. Glutaminyl and asparaginyl residues are frequently post-translationally deamidated to the corresponding glutamyl and asparyl residues. Alternatively, these residues are deamidated under mildly acidic conditions. Other post- translational modifications include hydroxylation of proline and lysine, phosphorylation of hydroxyl groups of seryl or threonyl residues, methylation of the o-amino groups of lysine, arginine, and histidine side chains (T.E. Creighton, Proteins: Structure and Molecular Properties, W. H. Freeman & Co., San Francisco pp 79-86

[1983] ), acetylation of the N-terminal amine and, in some instances, amidation of the C-terminal carboxyl.63. It is understood that one way to define the variants and derivatives of the disclosed proteins herein is through defining the variants and derivatives in terms of homology / identity to specific known sequences. For example, SEQ ID NO: 16 sets forth a particular sequence of ANT308. Specifically disclosed are variants of these and other proteins herein disclosed which have at least, 70% or 75% or 80% or 85% or 90% or 95% homology to the stated sequence. Those of skill in the art readily understand how to determine the homology of two proteins. Forexample, the homology can be calculated after aligning the two sequences so that the homology is at its highest level.64. Another way of calculating homology can be performed by published algorithms. Optimal alignment of sequences for comparison may be conducted by the local homology algorithm of Smith and Waterman Adv. Appl. Math. 2: 482 (1981), by the homology alignment algorithm of Needleman and Wunsch, J. MoL Biol. 48: 443 (1970), by the search for similarity method of Pearson and Lipman, Proc. Natl. Acad. Sci. U.S.A. 85: 2444 (1988), by computerized implementations of these algorithms (GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin Genetics Software Package, Genetics Computer Group, 575 Science Dr., Madison, WI), or by inspection.65. The same types of homology can be obtained for nucleic acids by for example the algorithms disclosed in Zuker, M. Science 244:48-52, 1989, Jaeger et al. Proc. Natl. Acad. Sci. USA 86:7706-7710, 1989, Jaeger et al. Methods Enzymol. 183:281-306, 1989.66. It is understood that the description of conservative mutations and homology can be combined together in any combination, such as embodiments that have at least 70% homology to a particular sequence wherein the variants are conservative mutations.67. As this specification discusses various proteins and protein sequences it is understood that the nucleic acids that can encode those protein sequences are also disclosed. This would include all degenerate sequences related to a specific protein sequence, i.e. all nucleic acids having a sequence that encodes one particular protein sequence as well as all nucleic acids, including degenerate nucleic acids, encoding the disclosed variants and derivatives of the protein sequences. Thus, while each particular nucleic acid sequence may not be written out herein, it is understood that each and every sequence is in fact disclosed and described herein through the disclosed protein sequence. It is also understood that while no amino acid sequence indicates what particular DNA sequence encodes that protein within an organism, where particular variants of a disclosed protein are disclosed herein, the known nucleic acid sequence that encodes that VIP receptor antagonist is also known and herein disclosed and described.68. It is understood that there are numerous amino acid and peptide analogs which can be incorporated into the disclosed compositions. For example, there are numerous D amino acids or amino acids which have a different functional substituent then the amino acids shown in Table 3 and Table 4. The opposite stereo isomers of naturally occurring peptides are disclosed, as well as the stereo isomers of peptide analogs. These amino acids can readily be incorporated into polypeptide chains by charging tRNA molecules with the amino acid of choice andengineering genetic constructs that utilize, for example, amber codons, to insert the analog amino acid into a peptide chain in a site specific way.69. Molecules can be produced that resemble peptides, but which are not connected via a natural peptide linkage. For example, linkages for amino acids or amino acid analogs can include CH2NH-, -CH2S-, -CH2-CH2 -, -CH=CH- (cis and trans), -COCH2-, - CH(OH)CH2— , and -CHH2SO — (These and others can be found in Spatola, A. F. in Chemistry and Biochemistry of Amino Acids, Peptides, and Proteins, B. Weinstein, eds., Marcel Dekker, New York, p. 267 (1983); Spatola, A. F., Vega Data (March 1983), Vol. 1, Issue 3, Peptide Backbone Modifications (general review); Morley, Trends Pharm Sci (1980) pp. 463-468; Hudson, D. et al., Int J Pept Prot Res 14:177-185 (1979) (-CH2NH-, CH2CH2-); Spatola et al. Life Sci 38:1243-1249 (1986) (-CH H2-S); Hann J. Chem. Soc Perkin Trans. I 307-314 (1982) (— CH-CH— , cis and trans); Almquist et al. J. Med. Chem. 23:1392-1398 (1980) (-COCH2— ); Jennings-White et al. Tetrahedron Lett 23:2533 (1982) (— COCH2— ); Szelke et al. European Appln, EP 45665 CA (1982): 97:39405 (1982) (-CH(OH)CH2-); Holladay et al. Tetrahedron. Lett 24:4401-4404 (1983) (-C(OH)CH2-); and Hruby Life Sci 31:189-199 (1982) (-CH2-S-); each of which is incorporated herein by reference. A particularly preferred non-peptide linkage is -CH2NH— . It is understood that peptide analogs can have more than one atom between the bond atoms, such as b-alanine, g-aminobutyric acid, and the like.70. Amino acid analogs and analogs and peptide analogs often have enhanced or desirable properties, such as, more economical production, greater chemical stability, enhanced pharmacological properties (half-life, absorption, potency, efficacy, etc.), altered specificity (e.g., a broad-spectrum of biological activities), reduced antigenicity, and others.71. D-amino acids can be used to generate more stable peptides, because D amino acids are not recognized by peptidases and such. Systematic substitution of one or more amino acids of a consensus sequence with a D-amino acid of the same type (e.g., D-lysine in place of L- lysine) can be used to generate more stable peptides. Cysteine residues can be used to cyclize or attach two or more peptides together. This can be beneficial to constrain peptides into particular conformations.3. Pharmaceutical carriers / Delivery of pharmaceutical products72. As described above, the compositions can also be administered in vivo in a pharmaceutically acceptable carrier. By "pharmaceutically acceptable" is meant a material that is not biologically or otherwise undesirable, i.e., the material may be administered to a subject, along with the nucleic acid or vector, without causing any undesirable biological effects or interacting in a deleterious manner with any of the other components of the pharmaceuticalcomposition in which it is contained. The carrier would naturally be selected to minimize any degradation of the active ingredient and to minimize any adverse side effects in the subject, as would be well known to one of skill in the art.73 . The compositions may be administered orally, parenterally (e.g., intravenously), by intramuscular injection, by intraperitoneal injection, transdermally, extracorporeally, topically or the like, including topical intranasal administration or administration by inhalant. As used herein, "topical intranasal administration" means delivery of the compositions into the nose and nasal passages through one or both of the nares and can comprise delivery by a spraying mechanism or droplet mechanism, or through aerosolization of the nucleic acid or vector. Administration of the compositions by inhalant can be through the nose or mouth via delivery by a spraying or droplet mechanism. Delivery can also be directly to any area of the respiratory system (e.g., lungs) via intubation. The exact amount of the compositions required will vary from subject to subject, depending on the species, age, weight and general condition of the subject, the severity of the allergic disorder being treated, the particular nucleic acid or vector used, its mode of administration and the like. Thus, it is not possible to specify an exact amount for every composition. However, an appropriate amount can be determined by one of ordinary skill in the art using only routine experimentation given the teachings herein.74. Parenteral administration of the composition, if used, is generally characterized by injection. Injectables can be prepared in conventional forms, either as liquid solutions or suspensions, solid forms suitable for solution of suspension in liquid prior to injection, or as emulsions. A more recently revised approach for parenteral administration involves use of a slow release or sustained release system such that a constant dosage is maintained. See, e.g., U.S. Patent No. 3,610,795, which is incorporated by reference herein.75. The materials may be in solution, suspension (for example, incorporated into microparticles, liposomes, or cells). These may be targeted to a particular cell type via antibodies, receptors, or receptor ligands. The following references are examples of the use of this technology to target specific proteins to tumor tissue (Senter, et al., Bioconjugate Chem., 2:447-451, (1991); Bagshawe, K.D., Br. J. Cancer, 60:275-281, (1989); Bagshawe, et al., Br. J. Cancer, 58:700-703, (1988); Senter, et al., Bioconjugate Chem., 4:3-9, (1993); Battelli, et al., Cancer Immunol. Immunother., 35:421-425, (1992); Pietersz and McKenzie, Immunolog. Reviews, 129:57-80, (1992); and Roffler, et al., Biochem. Pharmacol, 42:2062-2065, (1991)). Vehicles such as "stealth" and other antibody conjugated liposomes (including lipid mediated drug targeting to colonic carcinoma), receptor mediated targeting of DNA through cell specific ligands, lymphocyte directed tumor targeting, and highly specific therapeutic retroviral targetingof murine glioma cells in vivo. The following references are examples of the use of this technology to target specific proteins to tumor tissue (Hughes et al., Cancer Research, 49:6214- 6220, (1989); and Litzinger and Huang, Biochimica et Biophysica Acta, 1104: 179-187, (1992)). In general, receptors are involved in pathways of endocytosis, either constitutive or ligand induced. These receptors cluster in clathrin-coated pits, enter the cell via clathrin-coated vesicles, pass through an acidified endosome in which the receptors are sorted, and then either recycle to the cell surface, become stored intracellularly, or are degraded in lysosomes. The internalization pathways serve a variety of functions, such as nutrient uptake, removal of activated proteins, clearance of macromolecules, opportunistic entry of viruses and toxins, dissociation and degradation of ligand, and receptor- level regulation. Many receptors follow more than one intracellular pathway, depending on the cell type, receptor concentration, type of ligand, ligand valency, and ligand concentration. Molecular and cellular mechanisms of receptor-mediated endocytosis has been reviewed (Brown and Greene, DNA and Cell Biology 10:6, 399-409 (1991)). a) Pharmaceutically Acceptable Carriers76. The compositions, including antibodies, can be used therapeutically in combination with a pharmaceutically acceptable carrier.77. Suitable carriers and their formulations are described in Remington: The Science and Practice of Pharmacy (19th ed.) ed. A.R. Gennaro, Mack Publishing Company, Easton, PA 1995. Typically, an appropriate amount of a pharmaceutically-acceptable salt is used in the formulation to render the formulation isotonic. Examples of the pharmaceutically-acceptable carrier include, but are not limited to, saline, Ringer's solution and dextrose solution. The pH of the solution is preferably from about 5 to about 8, and more preferably from about 7 to about 7.5. Further carriers include sustained release preparations such as semipermeable matrices of solid hydrophobic polymers containing the antibody, which matrices are in the form of shaped articles, e.g., films, liposomes or microparticles. It will be apparent to those persons skilled in the art that certain carriers may be more preferable depending upon, for instance, the route of administration and concentration of composition being administered.78. Pharmaceutical carriers are known to those skilled in the art. These most typically would be standard carriers for administration of drugs to humans, including solutions such as sterile water, saline, and buffered solutions at physiological pH. The compositions can be administered intramuscularly or subcutaneously. Other compounds will be administered according to standard procedures used by those skilled in the art.79. Pharmaceutical compositions may include carriers, thickeners, diluents, buffers, preservatives, surface active agents and the like in addition to the molecule of choice. Pharmaceutical compositions may also include one or more active ingredients such as antimicrobial agents, antiinflammatory agents, anesthetics, and the like.80. The pharmaceutical composition may be administered in a number of ways depending on whether local or systemic treatment is desired, and on the area to be treated. Administration may be topically (including ophthalmically, vaginally, rectally, intranasally), orally, by inhalation, or parenterally, for example by intravenous drip, subcutaneous, intraperitoneal or intramuscular injection. The disclosed antibodies can be administered intravenously, intraperitoneally, intramuscularly, subcutaneously, intracavity, or transdermally.81. Preparations for parenteral administration include sterile aqueous or non-aqueous solutions, suspensions, and emulsions. Examples of non-aqueous solvents are propylene glycol, polyethylene glycol, vegetable oils such as olive oil, and injectable organic esters such as ethyl oleate. Aqueous carriers include water, alcoholic / aqueous solutions, emulsions or suspensions, including saline and buffered media. Parenteral vehicles include sodium chloride solution, Ringer's dextrose, dextrose and sodium chloride, lactated Ringer's, or fixed oils. Intravenous vehicles include fluid and nutrient replenishers, electrolyte replenishers (such as those based on Ringer’s dextrose), and the like. Preservatives and other additives may also be present such as, for example, antimicrobials, anti-oxidants, chelating agents, and inert gases and the like.82. Formulations for topical administration may include ointments, lotions, creams, gels, drops, suppositories, sprays, liquids and powders. Conventional pharmaceutical carriers, aqueous, powder or oily bases, thickeners and the like may be necessary or desirable.83. Compositions for oral administration include powders or granules, suspensions or solutions in water or non-aqueous media, capsules, sachets, or tablets. Thickeners, flavorings, diluents, emulsifiers, dispersing aids or binders may be desirable..84. Some of the compositions may potentially be administered as a pharmaceutically acceptable acid- or base- addition salt, formed by reaction with inorganic acids such as hydrochloric acid, hydrobromic acid, perchloric acid, nitric acid, thiocyanic acid, sulfuric acid, and phosphoric acid, and organic acids such as formic acid, acetic acid, propionic acid, glycolic acid, lactic acid, pyruvic acid, oxalic acid, malonic acid, succinic acid, maleic acid, and fumaric acid, or by reaction with an inorganic base such as sodium hydroxide, ammonium hydroxide, potassium hydroxide, and organic bases such as mono-, di-, trialkyl and aryl amines and substituted ethanolamines.b) Therapeutic Uses85. Effective dosages and schedules for administering the compositions may be determined empirically, and making such determinations is within the skill in the art. The dosage ranges for the administration of the compositions are those large enough to produce the desired effect in which the symptoms of the disorder are effected. The dosage should not be so large as to cause adverse side effects, such as unwanted cross-reactions, anaphylactic reactions, and the like. Generally, the dosage will vary with the age, condition, sex and extent of the disease in the patient, route of administration, or whether other drugs are included in the regimen, and can be determined by one of skill in the art. The dosage can be adjusted by the individual physician in the event of any counterindications. Dosage can vary, and can be administered in one or more dose administrations daily, for one or several days. Guidance can be found in the literature for appropriate dosages for given classes of pharmaceutical products. For example, guidance in selecting appropriate doses for antibodies can be found in the literature on therapeutic uses of antibodies, e.g., Handbook of Monoclonal Antibodies, Ferrone et al., eds., Noges Publications, Park Ridge, N.J., (1985) ch. 22 and pp. 303-357; Smith et al., Antibodies in Human Diagnosis and Therapy, Haber et al., eds., Raven Press, New York (1977) pp. 365-389. A typical daily dosage of the antibody used alone might range from about 1 pg / kg to up to 100 mg / kg of body weight or more per day, depending on the factors mentioned above.C. Methods of Use86. In certain embodiments, the disclosure relates to expanding T cells, activating T cells, expanding or reversing senescence in T cells, or reversing exhaustion in T cells with a naturally occurring reactivity to cancer can be found infiltrated in tumors of the subject. The tumor can be harvested, and these tumor-infiltrating lymphocytes (TIL) can be isolated from the tumor and then expanded using methods discloses herein.87. In certain embodiments, this disclosure relates to compositions and methods of reversing senescence in T cells or reversing exhaustion in T cells by interrupting vasoactive intestinal peptide (VIP) signaling and / or inhibiting phosphatidy linositol-3 -kinase (PI3 kinase) inhibitor signaling and uses in managing cancer and chronic viral infections. In certain embodiments, the disclosure contemplates methods of reversing T cell senescence or reversing exhaustion in T cells by mixing T cell in vitro with any VIP-R antagonist disclosed herein (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ IDNO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39, fragment thereof, or an analog thereof).88. Also disclosed herein are methods of in vitro or ex vivo augmenting T cell activation and / or expansion, comprising mixing one or more T cells with any of the modified VIP-R antagonists disclosed herein (including, but not limited to SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39) or any of the pharmaceutical compositions disclosed herein. For example, disclosed herein are methods of ex vivo augmenting T cell activation and / or expansion, comprising mixing one or more T cells with the modified VIP-R antagonist as set forth in SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ IDNO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35,SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39.89. In certain embodiments, the disclosure contemplates methods of stimulating isolated T cells, methods of reversing senescent in T cells, methods of reversing exhaustion on T cells, method of expanding senescent T cells, and / or methods of in vitro or ex vivo augmenting T cell activation and / or expansion by the further in vitro or ex vivo exposure of T cells to antibodies that bind CD3 and / or CD28. In certain embodiments, the disclosure contemplates using anti-CD3 and anti-CD28 antibodies or binding agents optionally linked to a solid substrate such as magnetic beads.90. In some aspects, the methods of stimulating isolated T cells, methods of reversing senescent in T cells, methods of reversing exhaustion on T cells, method of expanding senescent T cells, and / or methods of in vitro or ex vivo augmenting T cell activation and / or expansion, further comprise the administration of a VIP degrading enzyme.91. In certain embodiments, the methods of stimulating isolated T cells, methods of reversing senescent in T cells, methods of reversing exhaustion on T cells, method of expanding senescent T cells, and / or methods of in vitro or ex vivo augmenting T cell activation and / or expansion contemplate that the T cells targeted by said methods that are negative for CD28 and / or CD27 using an in vitro cell culture as disclosed herein providing replicated T cells that have increased expression of CD28 and / or CD27 compared with levels prior to replication.92. In some embodiments, the methods of stimulating isolated T cells, methods of reversing senescent in T cells, methods of reversing exhaustion on T cells, method of expanding senescent T cells, and / or methods of in vitro or ex vivo augmenting T cell activation and / or expansion can further comprise the addition of a PI3K inhibitor. A PI3K inhibitor as described herein is a PI3Ka inhibitor, a PI3KP inhibitor, a PI3K6 inhibitor, or a PI3Ky inhibitor. In some embodiments, the PI3K inhibitor described herein is a Pan-PI3K inhibitor, an isoform-specific inhibitor, or a dual PI3K inhibitor. Examples of the PI3K inhibitor described herein include, but not limited to, fimepinostat, rigosertib, buparlisib, CH5132799, pilaralisib, ZSTK474, sonolisib, pictilisib, copanlisib, B591, TG-100-115, RIDR-PI-103, dactolisib, apitolisib, gedatolisib, SF1126, omipalisib, samotolisib, bimiralisib, paxalisib, voxtalisib, GSK1059615, MEN1611, ZSTK474, as well as, isoform-specific inhibitiors such as a PI3Ka inhibitor (such as, for example, inavolisib, alpelisibiAZD8835, PWT33597, taselisib, and / or serabelisib), a PI3KP inhibitor (such as, for example, AZD8186 and / or GSK2636771), a PI3K5 inhibitor (such as, for example, AZD8835, AZD8186, nemiralisib, seletalisib, acalisib, CAL263, TG100-115, duvelisib, idelalisib, tenalisib, taselisib, zandelisib, AMG319, linperlisib, parsaclisib, umbralisib, and / or leniolisib), and / or a PI3Ky inhibitor (such as, for example, eganelisib, tenalisib, taselisib, and / or duvelisib). In certain embodiments, the phosphatidy linositol-3 -kinase inhibitor is selected from idelalisib, wortmannin, demethoxyviridin, perifosine, buparlisib, duvelisib, copanlisib, and alpelisib. In certain embodiments, the phosphatidylinositol-3-kinase inhibitor is in a culture at a concentration of greater than about 0.001 nM, 0.1 nM, 1 nM, 10 nM, 100 nM or between about 10 nM and about 10 micromolar or between about 10 nM and about 500 nM, or between about lOnM and about 1 micromolar. In certain embodiments, the phosphatidylinositol- 3-kinase inhibitor is selected from idelalisib in a culture at a concentration of greater than about 0.001 nM, 0.1 nM, 1 nM, 10 nM, 100 nM or between about 10 nM and about 10 micromolar or between about 10 nM and about 500 nM, or between about 10 nM and about 1 micromolar.93. In some embodiments, the methods of stimulating isolated T cells, methods of reversing senescent in T cells, methods of reversing exhaustion on T cells, method of expanding senescent T cells, and / or methods of in vitro or ex vivo augmenting T cell activation and / or expansion further comprises administering to the subject a therapeutically effective amount of an immune checkpoint blockade. In some embodiments, the immune checkpoint blockade is a PD-1 inhibitor, a PD-L1 inhibitor, a CTLA-4 inhibitor, an anti-TIM3 inhibitor, an anti-LAG3 inhibitor, an anti-CD47 inhibitor, imiquimod, polyinosinic-polycytidylic acid-poly-l-lysine carboxymethylcellulose (poly-ICLC) , pexidartinib, an anti-TIGIT inhibitor, an anti-B7-H3 inhibitor, an anti-B7-H4 inhibitor, an anti-A2aR inhibitor, an anti-CD73 inhibitor, an anti-NKG2A inhibitor, an anti-PVR!G / PVRL2 inhibitor, an anti-CEACAMl inhibitor, an anti- CEACAM5 inhibitor, an anti-CEACAM6 inhibitor, an focal adhesion kinase (FAK) inhibitor, a CCL2 / CCR2 inhibitor, an anti-leukemia inhibitory factor (LIF) inhibitor, an anti-CD47 / SIRPa inhibitor, an anti-colony-stimulating factor (CSF)-l inhibitor, an anti-IL-1 inhibitor, an anti-IL- 1R3 inhibitor, an anti-IL-8 inhibitor, an anti-semaphorin 4D (Sema4D) inhibitor, an angiopoietin(Ang)-2 inhibitor, a CLEVER-1 inhibitor, Axl-targeted enapotamab vedotin (EnaV), or an anti-phosphatidylserine inhibitor including, but not limited to pembrolizumab, nivolumab, cemiplimab, dostarlimab, atezolizumab, avelumab, durvalumab, or ipilimumab..94. In certain embodiments, the culture comprises an enzyme that hydrolyses VIP. In certain embodiments, the culture comprises a VIP degrading enzyme such as a peptidase, serine peptidase, a tryptase, chymase, or human chymase 1 (CMA1). In certain embodiments, the culture has at least at least about 0.001 microgram per mL, about 0.01 microgram per mL, about 0.1 microgram per mL, or about 1 microgram per mL of the VIP degrading enzyme such as a mast cell chymase. In certain embodiments, the disclosure contemplates a T cells culture comprising a minimal essential medium and isolated cells that express CD3 and / or CD4 and / or CD8 and are negative for CD27 and / or CD28 and a PI3 kinase inhibitor, any modified VIP-R antagonist disclosed herein (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39, a fragment thereof, or an analog thereof). The cells may be isolated by negative or positive selection using binding agents attached to solid supports such as beads, magnetic beads, or particles of fluorescent binding agents.95. In certain embodiments, the anti-CD3 antibodies and anti-CD28 antibodies are immobilized on a bead, magnetic bead, or solid surface. In certain embodiments, more than 5.0 % or 10 % or 15 % of the total cells in the culture express CD3 and / or CD4 and / or CD8. In certain embodiments, more than 20 %, 25 % or 50 % of the total cells express CD3 and / or CD4 and / or CD8. In certain embodiments, more than 15 % or 20% or 30% of the T cells in the culture are negative for CD28 and / or CD27. In certain embodiments, more than 20 %, 25 % or 50 % of the T cells are negative for CD28 and / or CD27.96. In certain embodiments, the purified T cells are obtained from centrifuging blood under conditions such that plasma and red blood cells separate providing purified T cells in amixture of white blood cells between the plasma and red blood cells. In certain embodiments, the purified T cells are obtained by bone marrow aspirates or a bone marrow biopsy.97. In certain embodiments, the purified T cells are obtained by mixing cells with a fluorescent marker that binds CD3 and purifying cells by fluorescent activated cell sorting. In certain embodiments, the purified T cells are obtained by mixing cells with a magnetized marker that binds CD3 and purifying cells by magnetic sorting. In certain embodiments, the purified T cells are obtained by mixing cells with a fluorescent marker that binds CD3 and / or CD4 and / or CD8 and purifying cells by fluorescent activated cell sorting. In certain embodiments, the purified T cells are obtained by mixing cells with a magnetized marker that binds CD3 and / or CD4 and / or CD 8 and purifying cells by magnetic sorting.98. In certain embodiments, the disclosure contemplates a solid substrate, such as beads, with anti-CD3 and anti-CD28 antibodies and having a VIP-degrading enzyme coupled to the surface. In certain embodiments, it is contemplated that the beads are arranged in the medium and the T cells are expanded on top of the medium such that the beads are sub-cellular.99. In certain embodiments, the VIP degrading enzyme comprises human CMA1 Accession number GenBank: AAI03975.1: MLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRL MDPQACSHFRDFDHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGRSDAKPP AVFTRISHYRPWINQILQAN (SEQ ID NO: 19). In certain embodiments, the VIP-degrading enzyme is human recombinant enkephalinase (neutral endopeptidase, EC 3.4.24.11) having the sequence: DGICKSSDCIKSAARLIQNMDATTEPCTDFFKYACGGWLKRNVIPETSSRYGNFDILRDE LEVVLKDVLQEPKTEDIVAVQKAKALYRSCINESAIDSRGGEPLLKLLPDIYGWPVATE NWEQKYGASWTAEKAIAQLNSKYGKKVLINLFVGTDDKNSVNHVIHIDQPRLGLPSRD YYECTGIYKEACTAYVDFMISVARLIRQEERLPIDENQLALEMNKVMELEKEIANATAK PEDRNDPMLLYNKMTLAQIQNNFSLEINGKPFSWLNFTNEIMSTVNISITNEEDVVVYAP EYLTKLKPILTKYSARDLQNLMSWRFIMDLVSSLSRTYKESRNAFRKALYGTTSETATW RRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQTLDDLTWMDAET KKRAEEKALAIKERIGYPDDIVSNDNKLNNEYLELNYKEDEYFENIIQNLKFSQSKQLKK LREKVDKDEWISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHE ITHGFDDNGRNFNKDGDLVDWWTQQSASNFKEQSQCMVYQYGNFSWDLAGGQHLNG INTLGENIADNGGLGQAYRAYQNYIKKNGEEKLLPGLDLNHKQLFFLNFAQVWCGTYR PEYAVNSIKTDVESPGNFRIIGTLQNSAEFSEAFHCRKNSYMNPEKKCRVW (SEQ ID NO: 20).100. In certain embodiments, cell cultures and methods described herein further include IL- 12. In certain embodiments, the IL- 12 is contemplated to enhance the effect of peptide disclosed herein or nanoparticle thereof on T cell proliferation stimulated in vitro with antibodies to CD3 and CD28.101. In certain embodiments, the disclosure relates to methods of enhancing the immune response to a cell therapy comprising administering any modified VIP-R antagonist disclosed herein (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39, a fragment thereof, or an analog thereof) to a subject in combination with a cell. In certain embodiments, the subject is diagnosed with leukemia or lymphoma. In certain embodiments, the cell is a blood cell, bone marrow cell, leukocyte, T-cell, natural killer cell, a hematopoietic stem cell, a G-CSF mobilized or non-mobilized blood mononuclear cell.102. In certain embodiments, the cell is selected from the group consisting of autologous T-cells, allogeneic cells from a HLA matched donor, or allogeneic cells from a HLA mis-matched donor. In certain embodiments, the cell is a bone marrow cell. In certain embodiments, the cell is a blood mononuclear cell comprising / expressing granulocyte colonystimulating factor. The cell therapy may be conducted with non-mobilized blood mononuclear cells.103. In certain embodiments, it is contemplated that any modified VIP-R antagonist disclosed herein (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39, a fragment thereof, or an analog thereof) may be administered to subjects before, during, or after a cell-based immunotherapy including the recipient or donor. The immunotherapy may be performed in combinations with chemotherapy and / or a radiation therapy. It is contemplated that peptide may be used in combination with other immune stimulators including, but not limited to, CpG oligonucleotides, granulocyte colony stimulating factor, granulocyte-macrophage colony stimulating factor, interferon alpha, pegylated interferon, interleukin- 12, interleukin-2, and pegfilgrastim.104. In certain embodiments, this disclosure relates to methods of treating or preventing graft versus host disease in a subject comprising administering an effective amount of any modified VIP-R antagonist disclosed herein (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31 , SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39, a fragment thereof, or an analog thereof) to a subject after a hematopoietic stem cell transplant or a subject that is to receive or received transplanted allogeneic tissue or cells. In certain embodiments, the subject received transplanted allogeneic hematopoietic stem cells. In certain embodiments, the subject received transplanted allogeneic hematopoietic stem cells separated from peripheral blood. In certain embodiments, the subject received chemotherapy to radiation treatments prior to receiving transplanted allogeneic hematopoietic stem cells.D. Methods of treating infectious disease105. The disclosed VIP-R antagonists can be used in the treatment of infectious disease. Accordingly, disclosed herein are methods of treating, decreasing, inhibiting, reducing, and / or ameliorating a microbial infection in a subject infected with a microbe or at risk for a microbial infection comprising administering to the subject a therapeutically effective amount of any of the modified VIP-R antagonists disclosed herein (including, but not limited to SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39) or pharmaceutical composition of any preceding aspect. For example, disclosed herein are methods of treating, decreasing, inhibiting, reducing, and / or ameliorating a microbial in a subject infected with a microbe or at risk for a microbial infection comprising administering to the subject a therapeutically effective amount of SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39.106. In one aspect, disclosed herein are methods of treating, decreasing, inhibiting, reducing, ameliorating, and / or preventing a microbial infection, wherein the microbial infection is a viral infection, and wherein the viral infection is an infection with a virus selected from the group consisting of Herpes Simplex virus- 1, Herpes Simplex virus-2, Varicella-Zoster virus, Epstein-Barr virus, Cytomegalovirus, Human Herpes virus-6, herpes lymphotropic virus, roseolovirus, Kaposi's sarcoma-associated herpesvirus, Variola virus, Vesicular stomatitis virus, Hepatitis A virus, Hepatitis B virus, Hepatitis C virus, Hepatitis D virus, Hepatitis E virus, Rhinovirus, Coronavirus (including, but not limited to avian coronavirus (IBV), porcine coronavirus HKU15 (PorCoV HKU15), Porcine epidemic diarrhea virus (PEDV), HCoV-229E, HCoV-OC43, HCoV-HKUl, HCoV-NL63, SARS-CoV, SARS-CoV-2, or MERS-CoV), Influenza A virus (including, but not limited to H1N1), Influenza B virus, Influenza C virus, Measles virus, Polyomavirus, Human Papillomavirus (HPV) Types 16, 18, 31, 33, 35, 39, 45, 51, 52, 56, 58, 59, parvovirus B19, molluscum contagiosum virus, JC virus (JCV), BK virus, Merkel cell polyomavirus, Respiratory syncytial virus, Adenovirus, Coxsackie virus, Chikungunya virus, Dengue virus, Mumps virus, Poliovirus, Rabies virus, Rous sarcoma virus, Reovirus, Yellow fever virus, human adenovirus types (HAdV-1 to 55), norovirus, rinderpest virus, California encephalitis virus, Friend spleen focus-forming virus (SFFV) or Xenotropic MuLV-Related Virus (XMRV), Ebola virus, Marburg virus, Lassa fever virus, Eastern Equine Encephalitis virus, Japanese Encephalitis virus, St. Louis Encephalitis virus, Murray Valley fever virus, West Nile virus, Rift Valley fever virus, Rotavirus A, Rotavirus B, Rotavirus C, Rotavirus D, Rotavirus E, Sindbis virus, Simian Immunodeficiency virus, Human T-cell Leukemia virus type-1, Hantavirus, Rubella virus, Simian Immunodeficiency virus, Human Immunodeficiency virus type-1, and Human Immunodeficiency virus type-2.107. In some embodiments, the method comprises further administering to the subject a therapeutically effective amount of a phosphatidylinositol 3-kinase (PI3K) inhibitor (for example, a PI3Ka inhibitor, a PI3KP inhibitor, a PI3K5 inhibitor, or a PI3Ky inhibitor). In some embodiments, the method comprises further administering to the subject a therapeutically effective amount of an immune checkpoint blockade (e.g., a PD-1 inhibitor, a PD-L1 inhibitor, or a CTLA-4 inhibitor).108. In some embodiments, the immune checkpoint blockade comprises a PD-1 inhibitor, a PD-L1 inhibitor, a CTLA-4 inhibitor, an anti-TIM3 inhibitor, an anti-LAG3 inhibitor, an anti-CD47 inhibitor, imiquimod, polyinosinic-polycytidylic acid-poly-l-lysine carboxymethylcellulose (poly-ICLC) , pexidartinib, an anti-TIGIT inhibitor, an anti-B7-H3 inhibitor, an anti-B7-H4 inhibitor, an anti-A2aR inhibitor, an anti-CD73 inhibitor, an anti-NKG2A inhibitor, an anti-PVR!G / PVRL2 inhibitor, an anti-CEACAMl inhibitor, an anti- CEACAM5 inhibitor, an anti-CEACAM6 inhibitor, an focal adhesion kinase (FAK) inhibitor, a CCL2 / CCR2 inhibitor, an anti-leukemia inhibitory factor (LIF) inhibitor, an anti-CD47 / SIRPa inhibitor, an anti-colony-stimulating factor (CSF)-l inhibitor, an anti-IL-1 inhibitor, an anti-IL- 1R3 inhibitor, an anti-IL-8 inhibitor, an anti-semaphorin 4D (Sema4D) inhibitor, an angiopoietin(Ang)-2 inhibitor, a CLEVER-1 inhibitor, Axl-targeted enapotamab vedotin (EnaV), or an anti-phosphatidylserine inhibitor. In some embodiments, the immune checkpoint blockade comprises pembrolizumab, nivolumab, cemiplimab, dostarlimab, atezolizumab, avelumab, durvalumab, or ipilimumab.109. In some embodiments, the disclosure relates to the use of a modified VIP-R antagonist disclosed herein (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39, a fragment thereof, or an analog thereof) in the production of an anti-viral medicament for the treatment of a viral infection. In some embodiments, the anti-viral medicament further comprises a phosphatidylinositol 3 -kinase (PI3K) inhibitor (for example, a PI3Ka inhibitor, a PI3K0 inhibitor, a PI3K5 inhibitor, or a PI3Ky inhibitor). In some embodiments, the anti-viral medicament further comprises an immune checkpoint blockade (e.g., a PD-1 inhibitor, a PD-L1 inhibitor, or a CTLA-4 inhibitor). In some embodiments, the subject is diagnosed with a chronic viral infection. In certain embodiments, the subject undergoes serological monitoring. In some embodiments, the administration is under conditions such that the viral infection is no longer detected. In some embodiments, the subject is diagnosed with a RNA virus, DNA virus, or retroviruses. In some embodiments, the subject is diagnosed with a virus that is double stranded DNA virus, sense single stranded DNA virus, double stranded RNA virus, sense single stranded RNA virus, antisense single stranded RNA virus, sense single stranded RNA retrovirus or a double stranded DNA retrovirus. In some embodiments, the subject is diagnosed to have a rotavirus, an influenza virus, a herpes virus, a hepatitis virus, or a lentivirus. In some embodiments, titer of the virus in the subject is reduced after the treatment as compared to pre-treatment.110. In certain embodiments, the disclosure relates to methods of treating, decreasing, inhibiting, reducing, ameliorating, and / or preventing a viral infection comprising administering any of the modified VIP-R antagonists disclosed herein (such as, for example, SEQ ID NO: 27,SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9,SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ IDNO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31,SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ IDNO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39) to a subject at risk of, exhibiting symptoms of, or diagnosed with a viral infection. In some embodiments, the method comprises further administering to the subject a therapeutically effective amount of a phosphatidylinositol 3 -kinase (PI3K) inhibitor (for example, a PI3Ka inhibitor, a PI3KP inhibitor, a PI3K5 inhibitor, or a PI3Ky inhibitor). In some embodiments, the method comprises further administering to the subject a therapeutically effective amount of an immune checkpoint blockade (e.g., a PD-1 inhibitor, a PD-L1 inhibitor, or a CTLA-4 inhibitor). In certain embodiments, the subject is immune compromised or the subject is an allogeneic bone marrow transplant donor or recipient. In typical embodiments, the subject is an organ transplant recipient, undergoing hemodialysis, diagnosed with cancer, receiving an immunosuppressive drug, and / or diagnosed with an HIV- infection. In certain embodiments, the disclosure relates to preventing a viral infection in an immunocompromised subject at risk of infection by administering any of the VIP-R antagonists disclosed herein and optionally one or more antiviral agents.111. In some embodiments, the immune checkpoint blockade comprises a PD-1 inhibitor, a PD-L1 inhibitor, a CTLA-4 inhibitor, an anti-TIM3 inhibitor, an anti-LAG3 inhibitor, an anti-CD47 inhibitor, imiquimod, polyinosinic-polycytidylic acid-poly-l-lysine carboxymethylcellulose (poly-ICLC) , pexidartinib, an anti-TIGIT inhibitor, an anti-B7-H3 inhibitor, an anti-B7-H4 inhibitor, an anti-A2aR inhibitor, an anti-CD73 inhibitor, an anti- NKG2A inhibitor, an anti-PVRIG / PVRL2 inhibitor, an anti-CEACAM 1 inhibitor, an anti- CEACAM5 inhibitor, an anti-CEACAM6 inhibitor, an focal adhesion kinase (FAK) inhibitor, a CCL2 / CCR2 inhibitor, an anti-leukemia inhibitory factor (LIF) inhibitor, an anti-CD47 / SIRPa inhibitor, an anti-colony-stimulating factor (CSF)-l inhibitor, an anti-IL-1 inhibitor, an anti-IL- 1R3 inhibitor, an anti-IL-8 inhibitor, an anti-semaphorin 4D (Sema4D) inhibitor, an angiopoietin(Ang)-2 inhibitor, a CLEVER- 1 inhibitor, Axl-targeted enapotamab vedotin (EnaV), or an anti-phosphatidylserine inhibitor. In some embodiments, the immune checkpoint blockade comprises pembrolizumab, nivolumab, cemiplimab, dostarlimab, atezolizumab, avelumab, durvalumab, or ipilimumab.112. The disclosed modified VIP-R antagonists (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ IDNO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39) are not limited to the treatment of viral infections, but are also useful in the treatment of other microbial infections, including, but not limited to bacterial, fungal, and parasitic infections. Accordingly, also disclosed herein are methods of treating, decreasing, inhibiting, reducing, ameliorating, and / or preventing a microbial infection, wherein the microbial infection is a bacterial infection, and wherein the bacterial infection is an infection with a bacteria selected from the group consisting of Mycobacterium tuberculosis, Mycobacterium bovis, Mycobacterium bovis strain BCG, BCG substrains, Mycobacterium avium, Mycobacterium intracellular, Mycobacterium africanum, Mycobacterium kansasii, Mycobacterium marinum, Mycobacterium ulcerans, Mycobacterium avium subspecies paratuberculosis, Nocardia asteroides, other Nocardia species, Legionella pneumophila, other Legionella species, Acetinobacter baumanii, Salmonella typhi, Salmonella enterica, other Salmonella species, Shigella boydii, Shigella dysenteriae, Shigella sonnei, Shigella flexneri, other Shigella species, Yersinia pestis, Pasteurella haemolytica, Pasteurella multocida, other Pasteurella species, Actinobacillus pleuropneumoniae, Listeria monocytogenes, Listeria ivanovii, Brucella abortus, other Brucella species, Cowdria ruminantium, Borrelia burgdorferi, Bordetella avium, Bordetella pertussis, Bordetella bronchiseptica, Bordetella trematum, Bordetella hinzii, Bordetella pteri, Bordetella parapertussis, Bordetella ansorpii other Bordetella species, Burkholderia mallei, Burkholderia psuedomallei, Burkholderia cepacian, Chlamydia pneumoniae, Chlamydia trachomatis, Chlamydia psittaci, Coxiella burnetii, Rickettsial species, Ehrlichia species, Staphylococcus aureus, Staphylococcus epidermidis, Streptococcus pneumoniae, Streptococcus pyogenes, Streptococcus agalactiae, Escherichia coli, Vibrio cholerae, Campylobacter species, Neiserria meningitidis, Neiserria gonorrhea, Pseudomonas aeruginosa, other Pseudomonas species, Haemophilus influenzae, Haemophilus ducreyi, other Hemophilus species, Clostridium tetani, other Clostridium species, Yersinia enterolitica, and other Yersinia species.113. In one aspect, disclosed herein are methods of treating, decreasing, inhibiting, reducing, ameliorating, and / or preventing a microbial infection, wherein the microbial infection is a fungal infection, and wherein the fungal infection is an infection with a fungus selected from the group consisting of Candida albicans, Cryptococcus neoformans, Histoplasma capsulatum, Aspergillus fumigatus, Coccidiodes immitis, Paracoccidiodes brasiliensis, Blastomyces dermitidis, Pneumocystis carnii, Penicillium marneffi, and Altemaria alternata.217. Also disclosed herein are methods of treating, decreasing, inhibiting, reducing, ameliorating, and / or preventing a microbial infection, wherein the microbial infection is a parasitic infection, and wherein the parasitic infection is an infection with a parasite selected from the group consisting of Toxoplasma gondii, Plasmodium falciparum, Plasmodium vivax, Plasmodium malariae, other Plasmodium species, Entamoeba histolytica, Naegleria fowleri, Rhinosporidium seeberi, Giardia lamblia, Enterobius vermicularis, Enterobius gregorii, Ascaris lumbricoides, Ancylostoma duodenale, Necator americanus, Cryptosporidium spp., Trypanosoma brucei, Trypanosoma cruzi, Leishmania major, other Leishmania species, Diphyllobothrium latum, Hymenolepis nana, Hymenolepis diminuta, Echinococcus granulosus, Echinococcus multilocularis, Echinococcus vogeli, Echinococcus oligarthrus, Diphyllobothrium latum, Clonorchis sinensis; Clonorchis viverrini, Fasciola hepatica, Fasciola gigantica, Dicrocoelium dendriticum, Fasciolopsis buski, Metagonimus yokogawai, Opisthorchis viverrini, Opisthorchis felineus, Clonorchis sinensis, Trichomonas vaginalis, Acanthamoeba species, Schistosoma intercalatum, Schistosoma haematobium, Schistosoma japonicum, Schistosoma mansoni, other Schistosoma species, Trichobilharzia regenti, Trichinella spiralis, Trichinella britovi, Trichinella nelsoni, Trichinella nativa, and Entamoeba histolytica.lt is understood and herein contemplated that despite the ability of the disclosed modified VIP-R antagonists (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39, a fragment thereof, or an analog thereof) to inhibit microbial virulence and effectuate microbial clearance in tissue without the addition of an anti-microbial agent, there can be instances where the addition (either in the composition itself or as a separate administration) of an anti-microbial is desired. Accordingly, disclosed herein are methods of treating, decreasing, inhibiting, reducing, ameliorating, and / or preventing a microbial infection, autoimmune disease, autoinflammatory disease, or cancer, further comprising administering to the subject an anti-microbial agent. Antimicrobial agents can comprise any antibiotics, antibodies, small molecules, and functional nucleic acids (siRNA, RNAi, anti-sense oligonucleotides), that directly attack the infecting microbe or alter host conditions rendering the host system inhospitable to the microbe. Such agents include, but are not limited to Abacavir, Acyclovir, Adefovir, Amantadine, Amprenavir, Ampligen, Arbidol, Atazanavir, Atripla, Balavir, Beta-D-N4-hydroxycitidine (NHC, EIDD- 1931), Cidofovir, Combivir, Dolutegravir, Darunavir, Delavirdine, Didanosine, Docosanol,Edoxudine, Efavirenz, Emtricitabine, Enfuvirtide, Entecavir, Ecoliever, Famciclovir, Fomivirsen, Fosamprenavir, Foscamet, Fosfonet, Ganciclovir, Hydroxy-chloroquine, Ibacitabine, Imunovir, Idoxuridine, Imiquimod, Indinavir, Inosine, Lamivudine, Lopinavir, Loviride, Maraviroc, Moroxydine, Methisazone, Nelfinavir, Nevirapine, Nexavir, Nitazoxanide, Norvir, Oseltamivir, Peginterferon alfa-2a, Penciclovir, Peramivir, Pleconaril, Podophyllotoxin, Raltegravir, Remdecivir, Ribavirin, Rimantadine, Ritonavir, Pyramidine, Saquinavir, Sofosbuvir, Stavudine, Telaprevir, Tenofovir, Tenofovir disoproxil, Tipranavir, Trifluridine, Trizivir, Tromantadine, Truvada, Valaciclovir, Valganciclovir, Vicriviroc, Vidarabine, Viramidine, Zalcitabine, Zanamivir, Zidovudine, Clofazimine; Dapsone; Capreomycin; Cycloserine; Ethambutol(Bs); Ethionamide; Isoniazid; Pyrazinamide; Rifampicin; Rifabutin; Rifapentine; Streptomycin; Arsphenamine; Chloramphenicol (Bs); Fosfomycin; Fusidic acid; Metronidazole; Mupirocin; Platensimycin; Quinupristin / Dalfopristin; Thiamphenicol; Tigecycline(Bs); Tinidazole; Trimethoprim(Bs); aminoglycosides such as, for example, Amikacin, Gentamicin, Kanamycin, Meropenem, Neomycin, Netilmicin, Tobramycin, Paromomycin, Streptomycin, Spectinomycin, Nitazoxanide, Melarsoprol Eflomithine, Metronidazole, Tinidazole, Miltefosine, Mebendazole, Pyrantel pamoate , Thiabendazole, Diethylcarbamazine, Ivermectin, Niclosamide, Praziquantel, Albendazole, Praziquantel, Rifampin, Amphotericin B, Fumagillin, Amphotericin B, Candicidin, Filipin, Hamycin, Natamycin, Nystatin, Rimocidin, Bifonazole, Butoconazole, Clotrimazole, Econazole, Fenticonazole, Isoconazole, Ketoconazole, Luliconazole, Miconazole, Omoconazole, Oxiconazole, Sertaconazole, Sulconazole, Tioconazole, Albaconazole, Efinaconazole, Epoxiconazole, Fluconazole, Isavuconazole, Itraconazole, Posaconazole, Propiconazole, Ravuconazole, Terconazole, Voriconazole, Abafungin, Anidulafungin, Caspofungin, Micafungin, Aurones, Benzoic acid, Ciclopirox, Flucytosine, Griseofulvin, Haloprogin, Tolnaftate, Undecylenic acid, Crystal violet, Balsam of Peru, Orotomide, Miltefosine, ; ansamycins, such as, for example, geldanamycin, rifaximin, herbimycin; Carbapenems, such as, for example, Ertapenem, Doripenem, Imipenem / Cilastatin, and Meropenem; Cephalosporins, such as, for example, Cefadroxil, Cefazolin, Cephradine, Cephapirin, Cephalothin, Cefalexin, Cefaclor, Cefoxitin, Cefotetan, Cefamandole, Cefmetazole, Cefonicid, Loracarbef, Cefprozil, Cefuroxime, Cefixime, Cefdinir, Cefditoren, Cefoperazone, Cefotaxime, Cefpodoxime, Ceftazidime, Ceftibuten, Ceftizoxime, Moxalactam, Ceftriaxone, Cefepime, Ceftaroline fosamil, and Ceftobiprole; Glycopeptides, such as, for example Teicoplanin, Vancomycin, Telavancin, Dalbavancin, and Oritavancin; Lincosamides(Bs), such as, for example, Clindamycin and Lincomycin; Lipopeptides, such as, for example, Daptomycin; Macrolides (Bs), such as, forexample, Azithromycin, Clarithromycin, Erythromycin, Roxithromycin, Telithromycin, and Spiramycin; Monobactams, such as, for example, Aztreonam; Nitrofurans, such as, for example, Furazolidone and Nitrofurantoin(Bs); Oxazolidinones(Bs), such as, for example, Linezolid, Posizolid, Radezolid, and Torezolid; Penicillins, such as, for example, Amoxicillin, Ampicillin, Azlocillin, Dicloxacillin, Flucloxacillin, Mezlocillin, Methicillin, Nafcillin, Oxacillin, Penicillin G, Penicillin V, Piperacillin, Penicillin G, Temocillin, and Ticarcillin; Polypeptides, such as, for example, Bacitracin, Colistin, and Polymyxin B; Quinolones / Fluoroquinolones, such as, for example, Ciprofloxacin, Enoxacin, Gatifloxacin, Gemifloxacin, Levofloxacin, Lomefloxacin, Moxifloxacin, Nadifloxacin, Nalidixic acid, Norfloxacin, Ofloxacin, Trovafloxacin, Grepafloxacin, Sparfloxacin, and Temafloxacin; Sulfonamides(Bs), such as, for example, Mafenide, Sulfacetamide, Sulfadiazine, Silver sulfadiazine, Sulfadimethoxine, Sulfamethizole, Sulfamethoxazole, Sulfanilamide (archaic), Sulfasalazine, Sulfisoxazole, Trimethoprim- Sulfamethoxazole (Co-trimoxazole) (TMP-SMX), and Sulfonamidochrysoidine (archaic); Tetracyclines(Bs), such as, for example, Demeclocycline, Doxycycline, Metacycline, Minocycline, Oxytetracycline, and Tetracycline; monoclonal antibodies such as, for example, Actoxumab, Atidortoxumab, Berlimatoxumab,’ Bezlotoxumab, Cosfroviximab, Edobacomab, Felvizumab, Firivumab, Foravirumab, Larcaviximab, Motavizumab, Navivumab, Panobacumab, Palivizumab, Porgaviximab, CR6261, Rafivirumab, Pagibaximab, Obiltoxaximab, Ibalizumab, Regavirumab, Rmab, Sevirumab, Rivabazumab pegol, Tefibazumab, Suvratoxumab, and Tuvirumab; and checkpoint inhibitors; Pembrolizumab, Nivolumab, Atezolizumab, Avelumab, Durvalumab, pidilizumab, AMP-224, AMP-514, PDR001, cemiplimab, and Ipilimumab. In certain embodiments, the subject is administered a pharmaceutical composition comprising a modified VIP-R antagonist disclosed herein (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39, a fragment thereof, or an analog thereof) and a second antiviral agent.218. In certain embodiments, the disclosure relates to treating a subject with a viral infection after infection by administering a modified VIP-R antagonist disclosed herein (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39, a fragment thereof, or an analog thereof) and an immunoglobulin.219. In certain embodiments, the disclosure relates to treating or preventing a viral infection by administering a modified VIP-R antagonist disclosed herein (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39) and a viral vaccine or in the absence of a viral vaccine.220. In certain embodiments, the disclosure relates to enhancing the immune response to a vaccine comprising administering a modified VIP-R antagonist disclosed herein (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39) to a subject in need thereof. Typically, the vaccine is selected from the group of vaccines consisting of herpes zoster vaccine, smallpox vaccine, polio vaccine, pertussis vaccine, influenza vaccine, diphtheria vaccine, tetanus vaccine, meningococcal vaccine, influenza A vaccine including subtype H1N1 vaccine, influenza B vaccine, influenza C vaccine, rotavirus A vaccine, rotavirus B vaccine, rotavirus C vaccine, rotavirus D vaccine, rotavirus E vaccine, SARS coronavirus vaccine, human adenovirus types (HAdV-1 to 55) vaccine, human papillomavirus (HPV) vaccine, parvovirus B19 vaccine, molluscum contagiosum vaccine, JC vaccine, BK vaccine, Merkel cell polyomavirus vaccine, coxsackie A vaccine, norovirus vaccine, Rubella vaccine, lymphocytic choriomeningitis vaccine, yellow fever vaccine, measles vaccine, mumps vaccine, respiratory syncytial vaccine, rinderpest vaccine, California encephalitis vaccine, hantavirus vaccine, rabies vaccine, Ebola vaccine, marburg vaccine, herpes simplex virus-1 (HSV-1) vaccine, herpes simplex virus-2 (HSV-2) vaccine, varicella zoster vaccine, Epstein-Barr virus (EBV) vaccine, cytomegalovirus (CMV) vaccine, herpes lymphotropic vaccine, roseolovirus vaccine, Kaposi's sarcoma-associated herpesvirus vaccine, hepatitis A (HAV) vaccine, hepatitis B (HBV) vaccine, hepatitis C (HCV) vaccine, hepatitis D (HDV) vaccine, hepatitis E (HEV) vaccine, human immunodeficiency virus (HIV) vaccine, The Human T-lymphotropic virus Type I (HTLV-1)vaccine, Friend spleen focus-forming virus (SFFV) vaccine, and Xenotropic MuLV-Related Virus (XMRV) vaccine. In certain embodiments, the vaccine for a subject diagnosed with a chronic viral infection.221. In certain embodiments, the vaccine comprises a protein or peptide, carbohydrate, sugar, polysaccharide, or nucleic acid. Typically, the vaccine is an attenuated replication competent virus or an inactivated virus. Tn certain embodiments, the vaccine comprises a live or a killed or inactivated prokaryotic or eukaryotic cell.222. In certain embodiments, the human T cells are activated in vitro by co-incubation with viral antigens. In certain embodiments, the viral antigens are presented on microvesicles. In certain embodiments, the viral antigens are presented on dendritic cells.223. Nucleic acid vaccines, typically a DNA plasmid or RNA vaccine, are genetically engineered to encode and / or produce one or more antigens from a pathogen. The nucleic acid transfects or infects host cells, where the inner machinery of the cells expresses the proteins. Because these proteins are recognized as foreign, when they are processed by the host cells and displayed on their surface immune response is triggered. Cytotoxic T lymphocytes responses can also be enhanced by co-inoculation with co-stimulatory molecules such as GM-CSF, B7-1, or B7-2. In certain embodiments, a modified VIP-R antagonist disclosed herein (such as, for example SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39, a fragment thereof, or an analog thereof) may be administered in combination with nucleic acid vaccines or other co-stimulatory molecules.224. In certain embodiments, the disclosure relates to vaccine compositions comprising a modified VIP-R antagonist disclosed herein (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39) and methods of administering a modified VIP-R antagonist disclosed herein in combination with a vaccine. In certain embodiments, the vaccine contains an antigen from a pathogen and is presented to the immune system from weakened or killed forms of the microbe or its toxins. The antigen stimulates the immunesystem. Vaccines may be prophylactic (e.g. to prevent or ameliorate the effects of a future infection by any pathogen), or therapeutic by being administered after infection or diagnosis of the disease.225. Some vaccines contain killed, but previously virulent, microorganisms that have been destroyed with chemicals or heat. The influenza vaccine, cholera vaccine, bubonic plague vaccine, polio vaccine, hepatitis A vaccine, and rabies vaccine are examples of a killed vaccine that are contemplated by this disclosure.226. Some vaccines contain live, attenuated microorganisms. Typically, these are live viruses that have been cultivated under conditions that disable certain virulent properties, or which use closely related but less dangerous organisms to produce a broad immune response; however, some are bacterial in nature.227. In certain embodiments, the vaccine is a protein subunit. Rather than introducing an inactivated or attenuated microorganism to an immune system, a fragment of it can be used to create an immune response. Examples include the subunit vaccine against Hepatitis B virus that is composed of only the surface proteins of the virus, the virus-like particle (VLP) vaccine against human papillomavirus (HPV) that is composed of the viral major capsid protein, and the hemagglutinin and neuraminidase subunits of the influenza virus.228. In certain embodiments, the vaccine comprises a polysaccharide. Certain bacteria have polysaccharide outer coats that are typically immunogenic. By linking these polysaccharides to proteins (e.g. toxins), the immune system can be led to recognize the polysaccharide as if it were a protein antigen.229. Toxoid vaccines are made from inactivated toxic compounds. Examples of toxoid-based vaccines include diphtheria and tetanus toxoid. In certain embodiments, a VIP-R antagonist disclosed herein (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39) is administered in combination with DPT. DPT (also DTP and DTwP) refers to a class of combination vaccines against three infectious diseases in humans: diphtheria, pertussis (whooping cough) and tetanus. The vaccine components include diphtheria, tetanus toxoids, and killed whole cells of the organism that causes pertussis (wP). DTaP (also known as Tdap, DTPa, and TDaP) refers to similar combination vaccines in which the pertussiscomponent is acellular. Also contemplated is the DT or TD vaccine, which lacks the pertussis component.230. Other specific vaccines contemplated by the disclosure include the anthrax vaccine, e.g., culture filtrates of an avirulent, nonencapsulated strain known as V770-NP1-R, Bacille Calmette-Guerin (BCG), e.g., a strain of the attenuated live bovine tuberculosis bacillus, haemophilus influenzae type B vaccine, e.g., Hib polysaccharide-protein conjugate vaccine, hepatitis A vaccine, e.g., inactivated Hepatitis A virus, hepatitis B vaccine, e.g., hepatitis B surface antigen, human papillomavirus (HPV) vaccine, e.g., non- infectious virus-like particles assembled from the LI proteins of HPV types 6, 11, 16 and 18, meningococcal vaccine, e.g., capsular polysaccharide antigens of Neisseria meningitides serogroups A, C, Y, and W-135 strains individually conjugated to diphtheria toxoid protein.231. In certain embodiments, this disclosure relates to methods of treating an active cytomegalovirus infection comprising administering an effective amount of a vasoactive intestinal peptide antagonist disclosed herein to a subject diagnosed with and exhibiting signs or symptoms of an active cytomegalovirus infection, wherein the vasoactive intestinal peptide antagonist comprises a peptide having a C-terminal amide and is optionally modified with hydrocarbon or polyethylene glycol groups. In some embodiments, the method comprises further administering to the subject a therapeutically effective amount of a phosphatidylinositol 3-kinase (PI3K) inhibitor (for example, a PI3Ka inhibitor, a PI3KP inhibitor, a PI3K5 inhibitor, or a PI3Ky inhibitor). In some embodiments, the method comprises further administering to the subject a therapeutically effective amount of an immune checkpoint blockade (e.g., a PD-1 inhibitor, a PD-L1 inhibitor, or a CTLA-4 inhibitor).232. In certain embodiments, this disclosure relates to methods of reducing an active cytomegalovirus infection comprising administering an effective amount of a vasoactive intestinal peptide antagonist disclosed herein to a subject suffering from an active cytomegalovirus infection, wherein the vasoactive intestinal peptide antagonist comprises a peptide having a C-terminal amide and is optionally modified with hydrocarbon or polyethylene glycol groups. In some embodiments, the method comprises further administering to the subject a therapeutically effective amount of a phosphatidylinositol 3-kinase (PI3K) inhibitor (for example, a PI3Ka inhibitor, a PI3KP inhibitor, a PI3K5 inhibitor, or a PI3Ky inhibitor). In some embodiments, the method comprises further administering to the subject a therapeutically effective amount of an immune checkpoint blockade (e.g., a PD-1 inhibitor, a PD-L1 inhibitor, or a CTLA-4 inhibitor). In certain embodiments, a titer of cytomegalovirus in the subject isreduced after administering the vasoactive intestinal peptide antagonist as compared to pretreatment.233. In some embodiments, the immune checkpoint blockade comprises a PD-1 inhibitor, a PD-L1 inhibitor, a CTLA-4 inhibitor, an anti-TIM3 inhibitor, an anti-LAG3 inhibitor, an anti-CD47 inhibitor, imiquimod, polyinosinic-polycytidylic acid-poly-l-lysine carboxymethylcellulose (poly-ICLC) , pexidartinib, an anti-TIGTT inhibitor, an anti-B7-H3 inhibitor, an anti-B7-H4 inhibitor, an anti-A2aR inhibitor, an anti-CD73 inhibitor, an anti- NKG2A inhibitor, an anti-PVRIG / PVRL2 inhibitor, an anti-CEACAMl inhibitor, an anti- CEACAM5 inhibitor, an anti-CEACAM6 inhibitor, an focal adhesion kinase (FAK) inhibitor, a CCL2 / CCR2 inhibitor, an anti-leukemia inhibitory factor (LIF) inhibitor, an anti-CD47 / SIRPa inhibitor, an anti-colony-stimulating factor (CSF)-l inhibitor, an anti-IL-1 inhibitor, an anti-IL- 1R3 inhibitor, an anti-IL-8 inhibitor, an anti-semaphorin 4D (Sema4D) inhibitor, an angiopoietin(Ang)-2 inhibitor, a CLEVER- 1 inhibitor, Axl-targeted enapotamab vedotin (EnaV), or an anti-phosphatidylserine inhibitor. In some embodiments, the immune checkpoint blockade comprises pembrolizumab, nivolumab, cemiplimab, dostarlimab, atezolizumab, avelumab, durvalumab, or ipilimumab.E. Method of treating cancer234. The disclosed VIP antagonists can be used to treat any disease where uncontrolled cellular proliferation occurs such as cancers. A representative but non- limiting list of cancers that the disclosed compositions can be used to treat is the following: malignancies located in the colon, abdomen, bone, breast, digestive system, liver, pancreas, peritoneum, endocrine glands (adrenal, parathyroid, hypophysis, testicles, ovaries, thymus, thyroid), eye, head and neck, nervous system (central and peripheral), lymphatic system, pelvis, skin, soft tissue, spleen, thorax and genitourinary apparatus and, more particularly, childhood acute lymphoblastic leukemia, acute lymphoblastic leukemia, acute lymphocytic leukemia, acute myeloid leukemia, adrenocortical carcinoma, adult (primary) hepatocellular cancer, adult (primary) liver cancer, adult acute lymphocytic leukemia, adult acute myeloid leukemia, adult Hodgkin's disease, adult Hodgkin's lymphoma, adult lymphocytic leukemia, adult nonHodgkin's lymphoma, adult primary liver cancer, adult soft tissue sarcoma, AIDS-related lymphoma, AIDS-related malignant tumors, anal cancer, astrocytoma, cancer of the biliary tract, cancer of the bladder, bone cancer, brain stem glioma, brain tumors, breast cancer, cancer of the renal pelvis and ureter, primary central nervous system lymphoma, central nervous system lymphoma, cerebellar astrocytoma, brain astrocytoma, cancer of the cervix, childhood (primary) hepatocellular cancer, childhood (primary) liver cancer, childhood acute lymphoblasticleukemia, childhood acute myeloid leukemia, childhood brain stem glioma, childhood cerebellar astrocytoma, childhood brain astrocytoma, childhood extracranial germ cell tumors, childhood Hodgkin's disease, childhood Hodgkin's lymphoma, childhood visual pathway and hypothalamic glioma, childhood lymphoblastic leukemia, childhood medulloblastoma, childhood nonHodgkin’s lymphoma, childhood supratentorial primitive neuroectodermal and pineal tumors, childhood primary liver cancer, childhood rhabdomyosarcoma, childhood soft tissue sarcoma, childhood visual pathway and hypothalamic glioma, chronic lymphocytic leukemia, chronic myeloid leukemia, cancer of the colon, cutaneous T-cell lymphoma, endocrine pancreatic islet cells carcinoma, endometrial cancer, ependymoma, epithelial cancer, cancer of the esophagus, Ewing's sarcoma and related tumors, cancer of the exocrine pancreas, extracranial germ cell tumor, extragonadal germ cell tumor, extrahepatic biliary tract cancer, cancer of the eye, breast cancer in women, Gaucher's disease, cancer of the gallbladder, gastric cancer, gastrointestinal carcinoid tumor, gastrointestinal tumors, germ cell tumors, gestational trophoblastic tumor, head and neck cancer, hepatocellular cancer, Hodgkin's disease, Hodgkin's lymphoma, hypergammaglobulinemia, hypopharyngeal cancer, intestinal cancers, intraocular melanoma, islet cell carcinoma, islet cell pancreatic cancer, Kaposi’s sarcoma, cancer of kidney, cancer of the larynx, cancer of the lip and mouth, cancer of the liver, cancer of the lung, lymphoproliferative disorders, macroglobulinemia, breast cancer in men, malignant mesothelioma, malignant thymoma, medulloblastoma, melanoma, mesothelioma, Merkel cell carcinoma, occult primary metastatic squamous neck cancer, primary metastatic squamous neck cancer, metastatic squamous neck cancer, multiple myeloma, multiple myeloma / plasmatic cell neoplasia, myelodysplastic syndrome, myelogenous leukemia, myeloid leukemia, myeloproliferative disorders, paranasal sinus and nasal cavity cancer, nasopharyngeal cancer, neuroblastoma, non-Hodgkin's lymphoma during pregnancy, non-melanoma skin cancer, nonsmall cell lung cancer, metastatic squamous neck cancer with occult primary, buccopharyngeal cancer, malignant fibrous histiocytoma, malignant fibrous osteosarcoma / histiocytoma of the bone, epithelial ovarian cancer, ovarian germ cell tumor, ovarian low malignant potential tumor, pancreatic cancer, paraproteinemias, purpura, parathyroid cancer, cancer of the penis, pheochromocytoma, hypophysis tumor, neoplasia of plasmatic cells / multiple myeloma, primary central nervous system lymphoma, primary liver cancer, prostate cancer, rectal cancer, renal cell cancer, cancer of the renal pelvis and ureter, retinoblastoma, rhabdomyosarcoma, cancer of the salivary glands, sarcoidosis, sarcomas, skin cancer, small cell lung cancer, small intestine cancer, soft tissue sarcoma, squamous neck cancer, stomach cancer, pineal and supratentorial primitive neuroectodermal tumors, T-cell lymphoma, testicular cancer, thymoma, thyroidcancer, transitional cell cancer of the renal pelvis and ureter, transitional renal pelvis and ureter cancer, trophoblastic tumors, cell cancer of the renal pelvis and ureter, cancer of the urethra, cancer of the uterus, uterine sarcoma, vaginal cancer, optic pathway and hypothalamic glioma, cancer of the vulva, Waldenstrom’s macroglobulinemia, Wilms’ tumor and any other hyperproliferative disease, as well as neoplasia, located in the system of a previously mentioned organ.235. In certain embodiments, it is contemplated that any VIP-R antagonist disclosed herein (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39) is used in certain cellular immunotherapies that are effective for treating cancer such as lymphocyte infusions or allogeneic bone marrow transplantations. Accordingly, disclosed herein are methods of treating, decreasing, inhibiting, reducing, ameliorating, and / or preventing a cancer and / or metastasis (such as, for example, pancreatic cancer, colon cancer, leukemia, liver cancer, lung cancer, or melanoma) in a subject or enhancing the immune response to cancer and / or metastasis (such as, for example, pancreatic cancer, colon cancer, leukemia, liver cancer, lung cancer, or melanoma) in a subject comprising administering to the subject a therapeutically effective amount of any of the modified VIP-R antagonists disclosed herein (including, but not limited to SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39) or pharmaceutical composition as disclosed herein. For example, disclosed herein are methods of treating, decreasing, inhibiting, reducing, ameliorating, and / or preventing a cancer and / or metastasis (such as, for example, pancreatic cancer, colon cancer, leukemia, liver cancer, lung cancer, or melanoma) in a subject or enhancing the immune response to cancer and / or metastasis (such as, for example, pancreatic cancer, colon cancer, leukemia, liver cancer, lung cancer, or melanoma) in a subject comprising administering to the subject a therapeutically effective amount of SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ IDNO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39.236. In one aspect disclosed herein are methods of treating, inhibiting, decreasing, reducing, ameliorating a cancer and / or metastasis (such as, for example, pancreatic cancer, colon cancer, leukemia, liver cancer, lung cancer, or melanoma) or a chronic infection in a subject in need, comprising obtaining one or more T cells (including, but not limited to autologous T cells); mixing the one or more T cells with the modified VIP-R antagonists disclosed herein (including, but not limited to SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39) or pharmaceutical composition as disclosed herein. For example, disclosed herein are methods of treating a cancer or a chronic infection in a subject in need, comprising obtaining one or more T cells; mixing the one or more T cells with the modified VIP-R antagonist as set forth in SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39.237. Donor immune cells, particularly NK cells and T-cells, cells have anti-cancer cytotoxic activity. VIP antagonism of the peptide enhances cellular immune responses in vivo. VIP antagonism increases the cytotoxic activity of antigen-specific T-cells and NK cells. VIP antagonism is predicted to increase the anti-cancer activity of NK cells or antigen-specific T- cells. VIP antagonism in conjunction with cellular immunotherapy is predicted to increase the efficacy of said therapy. It is believed that the absence of VIP does not increase the "off-target" graft versus host disease activity of donor lymphocytes in recipients of allogeneic bone marrow transplantation. Thus, administration of modified VIP-R antagonists to subjects with cancer receiving cellular therapies, e.g., donor lymphocyte infusions or allogeneic bone marrow transplantation, will increase the anti-cancer activity of said therapy.238. In some embodiments, the method comprises further administering to the subject a therapeutically effective amount of a phosphatidylinositol 3-kinase (PI3K) inhibitor (including, for example, a PI3Ka inhibitor, a PI3KP inhibitor, a PI3K5 inhibitor, or a PI3Ky inhibitor including, but not limited to idelalisib, copanlisib, duvelisib, alpelisib, umbralisib, buparlisib,copanlisib, dactolisib, leniolisib, parsaclisib, paxalisib, taselisib, zandelisib, inavolisib, apitolisib, bimiralisib, eganelisib, fimepinostat, gedatolisib, linperlisib, nemiralisib, pilaralisib, samotolisib, seletalisib, serabelisib, sonolisib, tenalisib, voxtalisib, AMG 319, AZD8186, GSK2636771, SF1126, acalisib, omipalisib, AZD8835, CAL263, GSK1059615, MEN1611, PWT33597, TG100-115, or ZSTK474).239. In some embodiments, the method comprises further administering to the subject a therapeutically effective amount of an immune checkpoint blockade (e.g., a PD-1 inhibitor, a PD-L1 inhibitor, or a CTLA-4 inhibitor). In some embodiments, the immune checkpoint blockade comprises a PD-1 inhibitor, a PD-L1 inhibitor, a CTLA-4 inhibitor, an anti-TIM3 inhibitor, an anti-LAG3 inhibitor, an anti-CD47 inhibitor, imiquimod, polyinosinic-polycytidylic acid-poly-l-lysine carboxymethylcellulose (poly-ICLC) , pexidartinib, an anti-TIGIT inhibitor, an anti-B7-H3 inhibitor, an anti-B7-H4 inhibitor, an anti-A2aR inhibitor, an anti-CD73 inhibitor, an anti-NKG2A inhibitor, an anti-PVRIG / PVRL2 inhibitor, an anti-CEACAMl inhibitor, an anti-CEACAM5 inhibitor, an anti-CEACAM6 inhibitor, an focal adhesion kinase (FAK) inhibitor, a CCL2 / CCR2 inhibitor, an anti-leukemia inhibitory factor (LIF) inhibitor, an anti- CD47 / SIRPa inhibitor, an anti-colony-stimulating factor (CSF)-l inhibitor, an anti-IL-1 inhibitor, an anti-IL-lR3 inhibitor, an anti-IL-8 inhibitor, an anti-semaphorin 4D (Sema4D) inhibitor, an angiopoietin(Ang)-2 inhibitor, a CLEVER- 1 inhibitor, Axl-targeted enapotamab vedotin (EnaV), or an anti-phosphatidylserine inhibitor. In some embodiments, the immune checkpoint blockade comprises pembrolizumab, nivolumab, cemiplimab, dostarlimab, atezolizumab, avelumab, durvalumab, or ipilimumab.240. It is understood and herein contemplated that the disclosed VIP receptor antagonists can be used alone or in combination with any anti-cancer therapy known in the art including, but not limited to Abemaciclib, Abiraterone Acetate, ABITREXATE® (Methotrexate), ABRAXANE® (Paclitaxel Albumin-stabilized Nanoparticle Formulation), ABVD, ABVE, ABVE-PC, AC, AC-T, ADCETRIS® (Brentuximab Vedotin), ADE, Ado- Trastuzumab Emtansine, ADRIAMYCIN® (Doxorubicin Hydrochloride), Afatinib Dimaleate, AFINITOR® (Everolimus), AKYNZEO® (Netupitant and Palonosetron Hydrochloride), ALDARA® (Imiquimod), Aldesleukin, ALECENSA® (Alectinib), Alectinib, Alemtuzumab, ALIMTA® (Pemetrexed Disodium), ALIQOPA® (Copanlisib Hydrochloride), ALKERAN™ for Injection (Melphalan Hydrochloride), ALKERAN™ Tablets (Melphalan), ALOXI® (Palonosetron Hydrochloride), ALUNBRIG® (Brigatinib), AMBOCHLORIN® (Chlorambucil), AMBOCLORIN® (Chlorambucil), Amifostine, Aminolevulinic Acid, Anastrozole, Aprepitant, AREDIA® (Pamidronate Disodium), ARIMIDEX® (Anastrozole), AROMASIN®(Exemestane),ARRANON® (Nelarabine), Arsenic Trioxide, ARZERRA® (Ofatumumab), Asparaginase Erwinia chrysanthemi, Atezolizumab, AVASTIN® (Bevacizumab), Avelumab, Axitinib, Azacitidine, BAVENCIO® (Avelumab), BEACOPP, BECENUM® (Carmustine), BELEODAQ® (Belinostat), Belinostat, Bendamustine Hydrochloride, BEP, BESPONSA® (Inotuzumab Ozogamicin) , Bevacizumab, Bexarotene, BEXXAR® (Tositumomab and Iodine I 131 Tositumomab), Bicalutamide, BICNU® (Carmustine), Bleomycin, Blinatumomab, BLINCYTO® (Blinatumomab), Bortezomib, BOSULIF® (Bosutinib), Bosutinib, Brentuximab Vedotin, Brigatinib, BuMel, Busulfan, BUSULFEX® (Busulfan), Cabazitaxel, CABOMETYX® (Cabozantinib-S-Malate), Cabozantinib-S-Malate, CAF, CAMPATH® (Alemtuzumab), CAMPTOSAR® (Irinotecan Hydrochloride), Capecitabine, CAPOX, CARAC® (Fluorouracil— Topical), Carboplatin, CARBOPLATIN-TAXOL, Carfilzomib, CARMUBRIS® (Carmustine), Carmustine, Carmustine Implant, CASODEX® (Bicalutamide), CEM, Ceritinib, CERUBIDINE® (Daunorubicin Hydrochloride), CERVARIX® (Recombinant HPV Bivalent Vaccine), Cetuximab, CEV, Chlorambucil, CHLORAMBUCIL-PREDNISONE, CHOP, Cisplatin, Cladribine, CLAFEN® (Cyclophosphamide), Clofarabine, CLOFAREX® (Clof arabine), CLOLAR® (Clofarabine), CMF, Cobimetinib, COMETRIQ® (Cabozantinib-S- Malate), Copanlisib Hydrochloride, COPDAC, COPP, COPP-ABV, COSMEGEN® (Dactinomycin), COTELLIC® (Cobimetinib), Crizotinib, CVP, Cyclophosphamide, CYFOS® (Ifosfamide), CYRAMZA® (Ramucirumab), Cytarabine, Cytarabine Liposome, CYTOSAR- U® (Cytarabine), CYTOXAN® (Cyclophosphamide), Dabrafenib, Dacarbazine, DACOGEN® (Decitabine), Dactinomycin, Daratumumab, DARZALEX® (Daratumumab), Dasatinib, Daunorubicin Hydrochloride, Daunorubicin Hydrochloride and Cytarabine Liposome, Decitabine, Defibrotide Sodium, DEFITELIO® (Defibrotide Sodium), Degarelix, Denileukin Diftitox, Denosumab, DEPOCYT® (Cytarabine Liposome), Dexamethasone, Dexrazoxane Hydrochloride, Dinutuximab, Docetaxel, DOXIL® (Doxorubicin Hydrochloride Liposome), Doxorubicin Hydrochloride, Doxorubicin Hydrochloride Liposome, DOX-SL® (Doxorubicin Hydrochloride Liposome), DTIC-DOME® (Dacarbazine), Durvalumab, EFUDEX® (Fluorouracil— Topical), ELITEK® (Rasburicase), ELLENCE® (Epirubicin Hydrochloride), Elotuzumab, ELOXATIN® (Oxaliplatin), Eltrombopag Olamine, EMEND® (Aprepitant), EMPLICITI® (Elotuzumab), Enasidenib Mesylate, Enzalutamide, Epirubicin Hydrochloride , EPOCH, ERBITUX® (Cetuximab), Eribulin Mesylate, ERIVEDGE® (Vismodegib), Erlotinib Hydrochloride, ERWINAZE® (Asparaginase Erwinia chrysanthemi), ETHYOL® (Amifostine), Etopophos ETOPOPHOS® (Etoposide Phosphate), Etoposide, Etoposide Phosphate, EV ACET® (Doxorubicin Hydrochloride Liposome), Everolimus, EVISTA® (RaloxifeneHydrochloride), EVOMELA® (Melphalan Hydrochloride), Exemestane, 5-FU® (Fluorouracil Injection), 5-FU® (Fluorouracil— Topical), FARESTON® (Toremifene), FARYDAK® (Panobinostat), FASLODEX® (Fulvestrant), FEC, FEMARA® (Letrozole), Filgrastim, FLUDARA® (Fludarabine Phosphate), Fludarabine Phosphate, FLUOROPLEX® (Fluorouracil- -Topical), Fluorouracil Injection, Fluorouracil— Topical, Flutamide, FOLEX® (Methotrexate), FOLEX PFS® (Methotrexate), FOLFIRI, FOLFIRI-BEVACIZUMAB, FOLFIRI- CETUXIMAB, FOLFIRINOX, FOLFOX, FOLOTYN® (Pralatrexate), FU-LV, Fulvestrant, GARDASIL® (Recombinant HPV Quadrivalent Vaccine), GARDASIL 9® (Recombinant HPV Nonavalent Vaccine), GAZYVA® (Obinutuzumab), Gefitinib, Gemcitabine Hydrochloride, GEMCITABINE-CISPLATIN, GEMCITABINE- OXALIPLATIN, Gemtuzumab Ozogamicin, GEMZAR® (Gemcitabine Hydrochloride), GILOTRIF® (Afatinib Dimaleate), GLEEVEC® (Imatinib Mesylate), GLIADEL® (Carmustine Implant), GLIADEL WAFER® (Carmustine Implant), Glucarpidase, Goserelin Acetate, HALAVEN® (Eribulin Mesylate), HEMANGEOL® (Propranolol Hydrochloride), HERCEPTIN® (Trastuzumab), HPV Bivalent Vaccine, Recombinant, HPV Nonavalent Vaccine, Recombinant, HPV Quadrivalent Vaccine, Recombinant, HYCAMTIN® (Topotecan Hydrochloride), HYDREA® (Hydroxyurea), Hydroxyurea, Hyper-CVAD, IBRANCE® (Palbociclib), Ibritumomab Tiuxetan, Ibrutinib, ICE, ICLUSIG® (Ponatinib Hydrochloride), IDAMYCIN® (Idarubicin Hydrochloride), Idarubicin Hydrochloride, Idelalisib, IDHIFA® (Enasidenib Mesylate), IFEX® (Ifosfamide), Ifosfamide, IFOSFAMIDUM® (Ifosfamide), IL-2 (Aldesleukin), Imatinib Mesylate, IMBRUVICA® (Ibrutinib), IMFINZI® (Durvalumab), Imiquimod, IMLYGIC® (Talimogene Laherparepvec), INLYTA® (Axitinib), Inotuzumab Ozogamicin, Interferon Alfa-2b, Recombinant, Interleukin-2 (Aldesleukin), INTRON A® (Recombinant Interferon Alfa-2b), Iodine 1 131 Tositumomab and Tositumomab, Ipilimumab, IRESSA® (Gefitinib), Irinotecan Hydrochloride, Irinotecan Hydrochloride Liposome, ISTODAX® (Romidepsin), Ixabepilone, Ixazomib Citrate, IXEMPRA® (Ixabepilone), IAKAFI® (Ruxolitinib Phosphate), JEB, JEVTANA® (Cabazitaxel), KADCYLA® (Ado-Trastuzumab Emtansine), KEOXIFENE® (Raloxifene Hydrochloride), KEPIVANCE® (Palifermin), KEYTRUDA® (Pembrolizumab), KISQALI® (Ribociclib), KYMRIAH® (Tisagenlecleucel), KYPROLIS® (Carfilzomib), Lanreotide Acetate, Lapatinib Ditosylate, LARTRUVO® (Olaratumab), Lenalidomide, Lenvatinib Mesylate, LENVIMA® (Lenvatinib Mesylate), Letrozole, Leucovorin Calcium, LEUKERAN® (Chlorambucil), Leuprolide Acetate, LEUSTATIN® (Cladribine), LEVULAN® (Aminolevulinic Acid), LINFOLIZIN® (Chlorambucil), LIPODOX® (DoxorubicinHydrochloride Liposome), Lomustine, LONSURF® (Trifluridine and Tipiracil Hydrochloride),LUPRON® (Leuprolide Acetate), LUPRON DEPOT® (Leuprolide Acetate), LUPRON DEPOT-PED® (Leuprolide Acetate), LYNPARZA® (Olaparib), MARQIBO® (Vincristine Sulfate Liposome), MATULANE® (Procarbazine Hydrochloride), Mechlorethamine Hydrochloride, Megestrol Acetate, MEKINIST® (Trametinib), Melphalan, Melphalan Hydrochloride, Mercaptopurine, Mesna, MESNEX® (Mesna), METHAZOLASTONE® (Temozolomide), Methotrexate, METHOTREXATE LPF® (Methotrexate), Methylnaltrexone Bromide, MEXATE® (Methotrexate), MEXATE-AQ® (Methotrexate), Midostaurin, Mitomycin C, Mitoxantrone Hydrochloride, MITOZYTREX® (Mitomycin C), MOPP, MOZOBIL® (Plerixafor), MUSTARGEN® (Mechlorethamine Hydrochloride) , MUTAMYCIN® (Mitomycin C), MYLERAN® (Busulfan), MYLOSAR® (Azacitidine), MYLOTARG® (Gemtuzumab Ozogamicin), NANOPARTICLE PACLITAXEL® (Paclitaxel Albumin-stabilized Nanoparticle Formulation), NAVELBINE® (Vinorelbine Tartrate), Necitumumab, Nelarabine, NEOSAR® (Cyclophosphamide), Neratinib Maleate, NERLYNX® (Neratinib Maleate), Netupitant and Palonosetron Hydrochloride, NEULASTA® (Pegfilgrastim), NEUPOGEN® (Filgrastim), NEXAVAR® (Sorafenib Tosylate), NILANDRON® (Nilutamide), Nilotinib, Nilutamide, NINLARO® (Ixazomib Citrate), Niraparib Tosylate Monohydrate, Nivolumab, NOLVADEX® (Tamoxifen Citrate), NPLATE® (Romiplostim), Obinutuzumab, ODOMZO® (Sonidegib), OEPA, Ofatumumab, OFF, Olaparib, Olaratumab, Omacetaxine Mepesuccinate, ONCASPAR® (Pegaspargase), Ondansetron Hydrochloride, ONIVYDE® (Irinotecan Hydrochloride Liposome), ONTAK® (Denileukin Diftitox), OPDIVO® (Nivolumab), OPPA, Osimertinib, Oxaliplatin, Paclitaxel, Paclitaxel Albumin-stabilized Nanoparticle Formulation, PAD, Palbociclib, Palifermin, Palonosetron Hydrochloride, Palonosetron Hydrochloride and Netupitant, Pamidronate Disodium, Panitumumab, Panobinostat, PARAPLAT® (Carboplatin), PARAPLATIN® (Carboplatin), Pazopanib Hydrochloride, PCV, PEB, Pegaspargase, Pegfilgrastim, Peginterferon Alfa-2b, PEG-INTRON® (Peginterferon Alfa-2b), Pembrolizumab, Pemetrexed Disodium, PERJETA® (Pertuzumab), Pertuzumab, PLATINOL® (Cisplatin), PLATINOL-AQ® (Cisplatin), Plerixafor, Pomalidomide, POMALYST® (Pomalidomide), Ponatinib Hydrochloride, PORTRAZZA® (Necitumumab), Pralatrexate, Prednisone, Procarbazine Hydrochloride, PROLEUKIN® (Aldesleukin), PROLIA® (Denosumab), PROMACTA® (Eltrombopag Olamine), Propranolol Hydrochloride, PROVENGE® (Sipuleucel-T), PURINETHOL® (Mercaptopurine), PURIXAN® (Mercaptopurine), Radium 223 Dichloride, Raloxifene Hydrochloride, Ramucirumab, Rasburicase, R-CHOP, R-CVP, Recombinant Human Papillomavirus (HPV) Bivalent Vaccine, Recombinant Human Papillomavirus (HPV)Nonavalent Vaccine, Recombinant Human Papillomavirus (HPV) Quadrivalent Vaccine, Recombinant Interferon Alfa- 2b, Regorafenib, RELISTOR® (Methylnaltrexone Bromide), R- EPOCH, REVLIMID® (Lenalidomide), RHEUMATREX® (Methotrexate), Ribociclib, R-ICE, RITUXAN® (Rituximab), RITUXAN HYCELA® (Rituximab and Hyaluronidase Human), Rituximab, Rituximab and , Hyaluronidase Human, ,Rolapitant Hydrochloride, Romidepsin, Romiplostim, RUBIDOMYCIN® (Daunorubicin Hydrochloride), RUBRACA® (Rucaparib Camsylate), Rucaparib Camsylate, Ruxolitinib Phosphate, RYDAPT® (Midostaurin), Sclerosol Intrapleural Aerosol (Talc), Siltuximab, Sipuleucel-T, SOMATULINE DEPOT® (Lanreotide Acetate), Sonidegib, Sorafenib Tosylate, SPRYCEL® (Dasatinib), STANFORD V, Sterile Talc Powder (Talc), STERITALC® (Talc), STIVARGA® (Regorafenib), Sunitinib Malate, SUTENT® (Sunitinib Malate), SYLATRON® (Peginterferon Alfa-2b), SYLVANT® (Siltuximab), Synribo SYNRIBO® (Omacetaxine Mepesuccinate), TABLOID® (Thioguanine), TAC, TAFINLAR® (Dabrafenib), TAGRISSO® (Osimertinib), Talc, Talimogene Laherparepvec, Tamoxifen Citrate, TARABINE PFS® (Cytarabine), TARCEVA® (Erlotinib Hydrochloride), TARGRETIN® (Bexarotene), TASIGNA® (Nilotinib), TAXOL® (Paclitaxel), TAXOTERE® (Docetaxel), TECENTRIQ® (Atezolizumab), TEMODAR® (Temozolomide), Temozolomide, Temsirolimus, Thalidomide, THALOMID® (Thalidomide), Thioguanine, Thiotepa, Tisagenlecleucel, TOLAK® (Fluorouracil-Topical), Topotecan Hydrochloride, Toremifene, TORISEL® (Temsirolimus), Tositumomab and Iodine 1 131 Tositumomab, TOTECT® (Dexrazoxane Hydrochloride), TPF, Trabectedin, Trametinib, Trastuzumab, TREANDA® (Bendamustine Hydrochloride), Trifluridine and Tipiracil Hydrochloride, TRISENOX® (Arsenic Trioxide), TYKERB® (Lapatinib Ditosylate) , UNITUXIN® (Dinutuximab), Uridine Triacetate, VAC, Vandetanib, VAMP, VARUBI® (Rolapitant Hydrochloride), VECTIBIX® (Panitumumab), VelP, VELBAN® (Vinblastine Sulfate), VELCADE® (Bortezomib), VELSAR® (Vinblastine Sulfate), Vemurafenib, VENCLEXTA® (Venetoclax), Venetoclax, VERZENIO® (Abemaciclib), VIADUR® (Leuprolide Acetate), VIDAZA® (Azacitidine), Vinblastine Sulfate, VINCASAR PFS® (Vincristine Sulfate), Vincristine Sulfate, Vincristine Sulfate Liposome, Vinorelbine Tartrate, VIP, Vismodegib, VISTOGARD® (Uridine Triacetate), VORAXAZE® (Glucarpidase), Vorinostat, VOTRIENT® (Pazopanib Hydrochloride), VYXEOS® (Daunorubicin Hydrochloride and Cytarabine Liposome), WELLCOVORIN® (Leucovorin Calcium), XALKORI® (Crizotinib), XELODA® (Capecitabine), XELIRI, XELOX, XGEVA® (Denosumab), XOFIGO® (Radium 223 Dichloride), XTANDI® (Enzalutamide), YERVOY® (Ipilimumab), YONDELIS® (Trabectedin), ZALTRAP® (Ziv-Aflibercept), ZARXIO® (Filgrastim), ZEJULA® (NiraparibTosylate Monohydrate), ZELBORAF® (Vemurafenib), ZEVAL1N® (Ibritumomab Tiuxetan), ZINECARD® (Dexrazoxane Hydrochloride), Ziv-Aflibercept, ZOFRAN® (Ondansetron Hydrochloride), ZOLADEX® (Goserelin Acetate), Zoledronic Acid, ZOLINZA® (Vorinostat), ZOMETA® (Zoledronic Acid), ZYDELIG® (Idelalisib), ZYKADIA® (Ceritinib), and / or ZYTIGA® (Abiraterone Acetate). The treatment methods can include or further include checkpoint inhibitors including, but are not limited to antibodies that block PD-1 (such as, for example, Nivolumab (BMS-936558 or MDX1106), pembrolizumab, cemiplimab , CT-011, MK- 3475), PD-L1 (such as, for example, atezolizumab, avelumab, durvalumab, MDX-1105 (BMS- 936559), MPDL3280A, or MSB0010718C), PD-L2 (such as, for example, rHIgM12B7), CTLA- 4 (such as, for example, Ipilimumab (MDX-010), Tremelimumab (CP-675,206)), IDO, B7-H3 (such as, for example, MGA271, MGD009, omburtamab), B7-H4, B7-H3, T cell inmiunoreceptor with Ig and ITIM domains (TIGIT)(such as, for example BMS-986207, OMP- 313M32, MK-7684, AB- 154, ASP-8374, MTIG7192A, or PVSRIPO), CD96, B- and T- lyinphocyte attenuator (BTLA), V-doraain Ig suppressor of T cell activation (VISTA)(such as, for example, JNJ-61610588, CA-170), TIM3 (such as, for example, TSR-022, MBG453, Sym023, INCAGN2390, LY3321367, BMS-986258, SHR-1702, RO7121661), LAG-3 (such as, for example, BMS-986016, LAG525, MK-4280, REGN3767, TSR-033, BI754111, Sym022, FS 118, MGD013, and Immutep).241. In certain embodiments, the method of administration is in a subject with a lymphodepleted environment. In certain embodiments, lymphodepleting agents are cyclophosphamide and fludarabine.242. As used herein the term “idelalisib” refers to the compound (S)-2-(l-(9H-purin-6- ylamino)propyl)-5-fluoro-3-phenylquinazolin-4(3H)-one or alternative salts thereof.243. The disclosed VIP-R antagonists can further be combined with radiotherapy and / or adoptive cell transfer therapies including but not limited to the administration of expanded, modified, or cultured tumor infiltrating lymphocytes (TILs); expanded, modified, or cultured marrow infiltrating lymphocytes (MILs); expanded, modified, or cultured Tumor infiltrating Natural killer cells (TINKs); chimeric antigen receptor (CAR) T cells; TCR Modified T Cells, and / or CAR NK cells. In certain embodiments, this disclosure relates to methods of treating a subject diagnosed with cancer comprising administering a cell in combination with any of the VIP-R antagonists disclosed herein to a subject in need thereof. In certain embodiments, the subject is diagnosed with leukemia. In certain embodiments, the subject is diagnosed with lymphoma. In certain embodiments, the cell is a blood mononuclear cell. In certain embodiments, the cell is a bone marrow cell. In certain embodiments, the cell is aleukocyte. In certain embodiments, the cell is a T-cell. In certain embodiments, the cell is a natural killer cell. In certain embodiments, the cell is a hematopoietic stem cell. In certain embodiments, the cell is a G-CSF mobilized blood mononuclear cell. In certain embodiments, the cell is an HLA matched or mis-matched allogeneic cell. In certain embodiments, the cell is syngeneic cell. In certain embodiments, the cell is an autologous cell. In certain embodiments, the peptide has a C-terminal amide and / or is optionally modified with hydrocarbon or polyethylene glycol groups. In one aspect, disclosed herein are methods of treating, inhibiting, reducing, decreasing, ameliorating, and / or preventing leukemia comprising administering any of the VIP-R antagonists disclosed herein (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39) to a subject in combination with transplanting hematopoietic stem cells. In certain embodiments, this disclosure relates to methods comprising expanding lymphocytes in vitro providing expanded cells and exposing the expanded cells with any of the VIP-R antagonists disclosed herein.244. In certain embodiments, the disclosure relates to methods of treating cancer by performing a stem cell transplantation comprising administering any VIP-R antagonist disclosed herein (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39) to the subject in combination with transplanting a multipotent hematopoietic stem cell derived from the subject (self) or a donor. The stem cells may be collected from peripheral blood such as cord blood or placenta-derived stem cells or from the bone marrow. To limit the risks of transplanted stem cell rejection or of severe graft- versus-host disease, the donor will typically have the substantially the same human leukocyte antigens (HLA) as the recipient; however, the donor may have mis-matches for certain antigens. In some embodiments, the method comprises further administering to the subject a therapeutically effective amount of a phosphatidylinositol 3-kinase (PI3K) inhibitor (for example, a PI3Ka inhibitor, a PI3KP inhibitor, a PI3K5 inhibitor, or a PI3Ky inhibitor). In some embodiments, the method comprises further administering to thesubject a therapeutically effective amount of an immune checkpoint blockade (e.g., a PD-1 inhibitor, a PD-L1 inhibitor, or a CTLA-4 inhibitor).245. In certain embodiments, the disclosure relates to methods of providing lymphocyte infusions after a hematopoietic progenitor cell transplant to treat a hematologic malignancy (e.g., cancer of the blood or bone marrow, such as leukemia or lymphoma). A transplant recipient is typically infused with lymphocytes obtained in a leukapheresis procedure from the original allogeneic stem cell (hematopoietic progenitor cell) donor.246. In certain embodiments, the disclosure relates to extraction of lymphocytes from the blood and expanding in vitro against tumor antigen(s) and optionally exposing the cells with an appropriate stimulatory cytokine and / or any modified VIP-R antagonist disclosed herein (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39).247. In certain embodiments, the disclosure relates to methods of enhancing topical immunotherapies comprising administering any of the modified VIP-R antagonists disclosed herein (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39) in combination with providing an immune enhancement cream, such as imiquimod, comprising an interferon-producing drug that causes the activation of T-cells. In some embodiments, the method comprises further administering to the subject a therapeutically effective amount of a phosphatidylinositol 3-kinase (PI3K) inhibitor (for example, a PI3Ka inhibitor, a PI3KP inhibitor, a PI3K5 inhibitor, or a PI3Ky inhibitor). In some embodiments, the method comprises further administering to the subject a therapeutically effective amount of an immune checkpoint blockade (e.g., a PD-1 inhibitor, a PD-L1 inhibitor, or a CTLA-4 inhibitor).248. In certain embodiments, it is contemplated that peptides disclosed herein can be used in combination with adoptive cell therapies. For example, T cells with a naturally occurring reactivity to cancer can be found infiltrated in tumors of the subject. The tumor can be harvested, and these tumor-infiltrating lymphocytes (TIL) can be expanded, or made more effective, in vitro using interleukin-2 (IL-2), anti-CD3 and allo-reactive feeders. These T cells can then betransferred back into the subject along with administration of a VIP-R antagonist. Before reinfusion, lymphodepletion of the recipient is typically done to eliminate regulatory T cells as well as normal endogenous lymphocytes that compete with the transferred cells. It is also contemplated that the adoptive cell transfer of lymphocytes may be transduced with a vector encoding T cell receptors (TCRs) that recognize a cancer antigen. In some embodiments, the method comprises further administering to the subject a therapeutically effective amount of a phosphatidylinositol 3-kinase (PI3K) inhibitor (for example, a PI3Ka inhibitor, a PI3KP inhibitor, a PI3K5 inhibitor, or a PI3Ky inhibitor). In some embodiments, the method comprises further administering to the subject a therapeutically effective amount of an immune checkpoint blockade (e.g., a PD-1 inhibitor, a PD-L1 inhibitor, or a CTLA-4 inhibitor).249. In certain embodiments, this disclosure relates to methods of augmenting T-cell activation and ex vivo expansion by co-incubation of human T cells with a nanoparticle containing a small molecule antagonist of VIP signaling. In certain embodiments, the human T cells are activated with anti-CD3 antibody bound to a plate. In certain embodiments, the human T cells are activated in a mixed lymphocyte reaction. In certain embodiments, the human T cells are activated in vitro by co-incubation with tumor-associated antigens. In certain embodiments, the tumor associate antigens are presented on tumor micro vesicles. In certain embodiments, the activated human T cells are infused into a human patient with cancer.250. In certain embodiments, the activated human T cells are infused into a human patient with cancer. In certain embodiments, the human patient with cancer has leukemia. In certain embodiments, the human patient with cancer has lymphoma. In certain embodiments, the human patient with cancer has multiple myeloma. In certain embodiments, the human patient with cancer has an epithelial cancer. In certain embodiments, the human patient has lung cancer. In certain embodiments, the human patient has breast cancer. In certain embodiments, the human patient has colon cancer. In certain embodiments, the human patient has prostate cancer. In certain embodiments, the human patient has malignant melanoma. In certain embodiments, the human patient has brain cancer.251. In certain embodiments, this disclosure relates to methods of augmenting anticancer immune responses by infusion of any of the modified VIP-R antagonists disclosed herein (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39). Incertain embodiments, the activated T-cells are infused into a patient with chronic CMV infection. In certain embodiments, the activated T-cells are infused into a patient with chronic EBV infection. In certain embodiments, the activated T-cells are infused into a patient with chronic BK virus infection. In certain embodiments, the activated T-cells are infused into a patient with chronic adenovirus infection.252. It is believed that cancer cells arise and are destroyed by the immune system, and that cancer forms when the immune system fails to destroy them. One approach to cancer vaccination is to separate proteins from cancer cells and immunize cancer patients against those proteins, stimulating an immune reaction that kills the cancer cells. Cancer vaccines are contemplated for the treatment of acute myeloid leukemia, multiple myeloma, lymphoma, breast, lung, colon, skin, kidney, prostate, and other cancers.253. In certain embodiments, the disclosure relates to treating cancers by administering any vasoactive intestinal peptide receptor (VIP-R) antagonist disclosed herein (such as, for example, SEQ ID NO: 27, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, and / or SEQ ID NO: 39) in combination with cancer antigens. Other VIP-R antagonists or VIP antagonists are also reported in U.S. Patent Nos. 6,630,124 and 5,217,953, which are incorporated herein by reference in their entireties.254. Prevention of the action of microorganisms may be controlled by addition of any of various antibacterial and antifungal agents, for example, parabens, chlorobutanol, phenol, sorbic acid, and the like. It may also be desirable to include isotonic agents, for example sugars, sodium chloride, and the like. Prolonged absorption of the injectable pharmaceutical form can be brought about by the use of agents delaying absorption, for example, aluminum monostearate and gelatin.F. Examples255. The following examples are put forth so as to provide those of ordinary skill in the art with a complete disclosure and description of how the compounds, compositions, articles, devices and / or methods claimed herein are made and evaluated, and are intended to be purely exemplary and are not intended to limit the disclosure. Efforts have been made to ensure accuracy with respect to numbers (e.g., amounts, temperature, etc.), but some errors anddeviations should be accounted for. Unless indicated otherwise, parts are parts by weight, temperature is in °C or is at ambient temperature, and pressure is at or near atmospheric.1. Example 1: ANT308 Fusion256. The emergence of site-selective peptide modifications has enabled the enhancement of therapeutic peptide drug properties. Such chemical modifications have facilitated the introduction of several peptide drugs in active clinical development and preclinical studies. Because peptide therapeutics can possess desirable physiochemical properties of both small molecule and biologies, the ability to access druggable peptides is of intrinsic value. We aimed to utilize Fc fusions to enhance the drug properties of the lead VIP antagonist ANT3O8. For the design of our ANT3O8 derivatives (Figure 1), we linked an IgG4 Fc domain to ANT308Materials and Methods a) Results257. A fusion of ANT308 and the Fc domain of a human immunoglobulin was made by cloning a signal sequence (e.g., MGWTLVFLFLLSVTAGVHS (SEQ ID NO: 24)) to the amino terminal end of ANT308 and cloning an immunoglobulin hinge (e.g., ESKYGPPCPPCPAPEAA (SEQ ID NO: 25)) and Fc domain (e.g., GGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPRE EQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLP PSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLT VDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGK (SEQ ID NO: 26)) to the carboxyl end of ANT308 using a GS linker to join the hinge and Fc domain to ANT308 ending with the construct as follows:MGWTLVFLFLLSVTAGVHSKPRRPYTSDYTRLRKQMAVKKYLNLILNGSESKYGPPCP PCPAPEAAGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHN AKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPRE PQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSF FLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGK (SEQ ID NO: 27)258. Next, we assessed ANT308-PEG and ANT308-Fc for in vitro human T cell activation (Figure 2). Here, we showed at 0.03 pM single dose, both ANT308-Fc and ANT308- PEG better enhanced CD69 expressions in CD4+ and CD8+ T cells and resulted in also Perforin, Granzyme B in CD8+ T cells compared to ANT308. Thus, PEGylation and Fc fusion improved ANT308 peptide functions in vitro.259. The Fc fusion and PEGylated ANT308 derivatives were administered to C1498 (Figure 3) or P805( Figure 4) AML and T-cell leukemia-bearing mice to evaluate theirimmunotherapeutic potential. The survival rate and tumor size of mice treated with ANT308 or its pegylated or Fc fusion derivatives over a 60-day period were measured (Figures 3 and 4). Mice treated with ANT308 or its pegylated or Fc fusion derivatives show significantly higher survival rates relative to the scramble control. Additionally, in the C1498 model, in the ANT308-Fc fusion showed significantly increased survival relative to ANT308 or ANT3O8-Peg.260. Next we compared the efficacy of a dose of ANT3O8 Fc3 fusion (i.e., Fc-Fusion ANT308) relative to ANT308 alone in a P815 mastcytoma model (Figure 5). We found that 4 doses of 6 nmol of ANT308 Fc3 fusion provided superior efficacy to 28 doses of 6nmol of AN308. Moreover, we found that the ANT308 Fc3 fusion also provided more effective protection to ANT308-Peg. Next using a Pl A tetramer, we measured the kinetics of antigen specific T cells. We observed a high frequency of antigen- specific CD8+ T cells induced in DBA / 2 mice with P815 after treatment with ANT308-Fc3 fusion (Figure 6).261. Lastly, we wanted to determine the dose-dependent survival after a single dose of ANT308-Fc fusion in mice with C 1498 leukemia. We showed that survival increased above control in a dose dependent manner at 0.3nmol and above.(1) Materials262. Canonical N-a-Fmoc-L-amino acids were obtained from Oakwood Chemical, Estill, USA. Fmoc-Lys(N3)-OH was purchased from Aapptec, Louisville, USA and Fmoc- Asp(OMpe)-OH was purchased from Combi-Blocks, San Diego, USA. NovaS yn® TGR resin was obtained from Novabiochem, Merck Biosciences, Darmstadt, Germany. All peptides were prepared by solid-phase automated synthesis (CEM Liberty Blue) using standard Fmoc protocol. Asparagine (N), cysteine (C), and glutamine (Q) were incorporated with Trt protected side chains. Aspartic acid (D) was incorporated with OMpe protected side chain. Arginine (R) was incorporated with Pbf protected side chain. Lysine (K) was incorporated with Boc protected side chain. Serine (S), threonine (T), and tyrosine (Y) were incorporated with 'Bu protected side chains. DBCO-mPEG, 20 kDa was purchased from Click Chemistry Tools, Scottsdale, USA. Synthetic reagents and solvent were purchased from MilliporeSigma, Darmstadt, Germany of the highest grade and used without further purification. Gel-electrophoresis materials were purchased from BioRad, Hercules, USA.(2) Linear Peptide Synthesis263. All peptides were prepared as carboxamides at the C-terminus on NovaSyn® TGR resin (0.24 mmol / g). 0.2 M amino acid stock solutions were used, along with 1.0 M Oxyma Pure and 1.0 M DIC. All stock solutions were prepared using HPLC-grade DMF. ForFmoc-deprotection, 20% (v / v) piperidine solution in DMF was prepared. For N-terminus acetylation, 20% (v / v) acetic anhydride in DMF was used. Syntheses were carried out under 0.1 mmol scale. All amino acids were singly coupled at 90°C for 2 minutes except for arginine, which was doubly coupled. The instrument was set to deliver 6 equivalents of amino acid, etc. N-terminus acetylation was performed using 4 iterative couplings at 60°C.(3) Cleavage and Purification of Crude Peptides264. Crude peptides without methionine or cysteine were cleaved under air using a cocktail of TFA. For peptides containing methionine or cysteine, cleavage was performed under nitrogen using a cocktail of 94% HPLC-grade TFA, 2.5% H2O, 2.5% EDT, 1% TIPS for 2 hours. For peptides containing azidolysine, cleavage was performed under nitrogen using a cocktail of 92.5:2.5:2.5:2.5 (w / w / w / w) TFA:H2O:TIPS:DTT for 2 hours. The crude peptide solution was triturated with 10 CV of cold Et2O. The white solid was centrifuged at 4000 rpm for 10 min to form a pellet. After removal of Et2O, the solid was resuspended twice with Et2O then dried under a stream of nitrogen. The crude material was reconstituted in 20% MeCN in H2O (0.1% TFA) and filtered via 0.45 pm syringe filter (PTFE). The crude solution was purified on an Agilent 1260 preparatory RP-HPLC using a Pursuit C18 column (21.2 x 250 mm, 5 pm) at 20 mL / min. The peptides were purified using H2O (solvent A) and MeCN (solvent B) with 0.1% TFA co-solvent under the following gradient. (Table 1). Peptide elution was monitored via UV absorption at 220 nm. The desired fractions were collected and lyophilized to yield purified product as a white powder, stored at -20°C.Table 1: Gradient used to purify ANT308 peptides on RP-HPLCTime (min) Solvent A (%) Solvent B (%)0 79 215 74 2619 67 3324 25 75(4) In vitro T cell studies265. Leukapheresis product containing peripheral blood mononuclear cells (PBMC) from multiple healthy donors were obtained from Stem Cell Technologies. T cells were isolated from PBMC using human pan-T cell isolation kit according to manufacturer’s protocol (Miltenyi Biotec, Catalog No. 130-096-535). Isolated T cells from 4-5 donors were pooled and seeded at a density of lxl06 / mL in a 96-well plate, activated with 1.5 pL / mL CD3 / CD28 T cell activator (ImmunoCult) in the presence of 30 IU interleukin 2 (IL2). Pooled T-cells were activated in the presence or absence of peptides (scrambled, ANT308 or modified ANT308) and cultured for 48hours. Leukocyte Activation Cocktail with Golgi Plug (BD) was added 4 hours prior to cell harvesting to assess Granzyme B expression in CD4+ and CD8+ T cells. Briefly, cells were stained with Fixable Aqua live / dead viability stain for 5 minutes at room temperature (RT). Surface antibodies (Table 2) were added to the cells at the desired concentration and left to stain for 30 minutes at 4°C. Following surface staining, cells were subsequently fixed and permeabilized for intracellular Granzyme B detection. Antibody targeting Granzyme B (Cat. 515408, BioLegend) was added and left to stain for 45 minutes at RT. Stained samples were run on five-laser Cytek Aurora cytometer for subsequent analysis.Table 2: List of antibodies used for flow cytometryTarget Fluorochrome Vendor Catalog No.CD3 PE / Cyanine 5 BioLegend 300410CD4 APC-Cy7 BD 557871CD8 Alexa Fluor 700 BD 557945CD69 Brilliant Violet 650 BioLegend 3109344- IBB Brilliant Violet 650 BioLegend 309828(5) In vivo AML studies266. P815-mastocytoma / myeloid leukemia cell line was obtained from ATCC.DBA / 2j (H-2Kd) mice were purchased from Jackson Laboratory (Bar Harbor, Maine). The mice were maintained by Emory University facilities. Both male and female mice were 8-10 weeks old. On day 0, DBA / 2j mice were injected subcutaneously with IxlO5C1498 or P815 cells. The treatments were injected subcutaneously and started from day 7 for a total of 28 (ANT308) or 4 total doses (Fc Fusion ANT3O8, Fc Fusion Scrambled, and VIP-fully scramble, and Pegylated (PEG) ANT3O8) for 10 days or 14 days. Lymphocyte kinetics were analyzed weekly through pterygoid venous plexus blood collection from the recipients. DBA mice were measured with tumor size by caliper, twice weekly. 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SequencesSEQ ID NO: 28 Fc-fusion-ANT005MGWTLVFLFLLSVTAGVHSKPRRPYTDNCTRLRKQMAVKKYLNSILNGSESKYGPPCP PCPAPEAAGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHN AKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPRE PQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSF FLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGKSEQ ID NO: 29 Fc-fusion-ANT008MGWTLVFLFLLSVTAGVHSKPRRPYTDNYTRLRKQMAVKKYLNLILNGSESKYGPPCP PCPAPEAAGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSF FLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGKSEQ ID NO: 30 Fc-fusion-ANT058MGWTLVFLFLLSVTAGVHSKPRRPYADNYTRLRKQMAVNKYLNLILNGSESKYGPPCPPCPAPEAAGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSF FLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGKSEQ ID NO: 31 Fc-fusion-ANT105MGWTLVFLFLLSVTAGVHSKPRRPYAVNYTRLRKQIAVKKYLMSILNGSESKYGPPCPPCPAPEAAGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSF FLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGKSEQ ID NO: 32 Fc-fusion-ANT107MGWTLVFLFLLSVTAGVHSKPRRPYAVNYTRLRKQMAVNKYLMSILNGSESKYGPPCPPCPAPEAAGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSF FLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGKSEQ ID NO: 33 Fc-fusion-ANT114MGWTLVFLFLLSVTAGVHSKPRRPYADNCTRLRKQIAVNKKYLNSILNGSESKYGPPCPPCPAPEAAGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSF FLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGKSEQ ID NO: 34 Fc-fusion-ANT195MGWTLVFLFLLSVTAGVHSKPRRPYTVNYTSLRKQ1AVKKYLMLILNGSESKYGPPCPPCPAPEAAGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGKSEQ ID NO: 35 Fc-fusion-ANT197MGWTLVFLFLLSVTAGVHSKPRRPYTDNCTSLRKQIAVNKYLNLILNGSESKYGPPCPPCPAPEAAGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGKSEQ ID NO: 36 Fc-fusion-ANT202MGWTLVFLFLLSVTAGVHSKPRRPYAVNCTSLRKQIAVNKYLNSILNGSESKYGPPCPPCPAPEAAGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGKSEQ ID NO: 37 Fc-fusion-ANT203MGWTLVFLFLLSVTAGVHSKPRRPYAVNCTSLRKQIAVKKYLMSILNGSESKYGPPCPPCPAPEAAGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGKSEQ ID NO: 38 Fc-fusion-ANT219MGWTLVFLFLLSVTAGVHSKPRRPYTVNCTSLRKQIAVKKYLMLILNGSESKYGPPCPPCPAPEAAGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGKSEQ ID NO: 39 Fc-fusion-ANT300MGWTLVFLFLLSVTAGVHSKPRRPYTSDYTRLRKQMAVKKYLNSILNGSESKYGPPCPPCPAPEAAGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSQEDPEVQFNWYVDGVEVHNAKTKPREEQFNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKGLPSSIEKTISKAKGQPRE PQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGK

Claims

V. CLAIMSWhat is claimed is:

1. A modified vasoactive intestinal peptide receptor (VIP-R) antagonist comprising KPRRPYX1X2X3X4TX5LRKQX6AVX7X8KYLX9X10ILN (SEQ ID NO: 3) or a fragment thereof, whereinX1is T or A;X2is D, V, or S;X3is N or D;X4is Y or C;X5is R or S;X6is M or I;X7is K or N;X8is K;X9is N or M;X10is S, or L; and provided that the peptide is not KPRRPYTDNYTRLRKQMAVKKYLNSILN (SEQ ID NO: 2) or the peptide is not the combination wherein X1is T, X2is D, X3is N; X4is Y, X5is R, X6is M, X7is K, X9is N, and X10is S; and wherein the VIP-R antagonist is conjugated to an immunoglobulin Fc domain.

2. A modified vasoactive intestinal peptide receptor (VIP-R) antagonist comprising KPRRPYX1X2X3X4TX5LRKQX6AVX7KYLX8X9ILN (SEQ ID NO: 21) or a fragment thereof, whereinX1is T or A;X2is D, V, or S;X3is N or D;X4is Y or C;X5is R or S;X6is M or I;X7is K or N;X8is N or M;X9is S, or L; and provided that the peptide is not KPRRPYTDNYTRLRKQMAVKKYLNSILN (SEQ ID NO: 2)or the peptide is not the combination wherein X1is T, X2is D, X3is N; X4is Y, X5is R, X6is M, X7is K, X8is N, and X9is S; and wherein the VIP-R antagonist is conjugated to an immunoglobulin Fc domain.

3. The modified VIP-R antagonist of claim 1 or 2, wherein the VIP-R antagonist comprises the amino acid sequence:KPRRPYADNYTRLRKQMAVNKYLNLILN (SEQ ID NO: 6), KPRRPYAVNYTRLRKQIAVKKYLMSILN (SEQ ID NO: 7), KPRRPYAVNYTRLRKQMAVNKYLMSILN (SEQ ID NO: 8), KPRRPYADNCTRLRKQIAVNKKYLNSILN (SEQ ID NO: 9), KPRRPYTVNYTSLRKQIAVKKYLMLILN (SEQ ID NO: 10), KPRRPYTDNCTSLRKQIAVNKYLNLILN (SEQ ID NO: 11), KPRRPYAVNCTSLRKQIAVNKYLNSILN (SEQ ID NO: 12), KPRRPYAVNCTSLRKQIAVKKYLMSILN (SEQ ID NO: 13), KPRRPYTVNCTSLRKQIAVKKYLMLILN (SEQ ID NO: 14), KPRRPYTSDYTRLRKQMAVKKYLNSILN (SEQ ID NO: 15), KPRRPYTSDYTRLRKQMAVKKYLNLILN (SEQ ID NO: 16), or a fragment thereof.

4. The modified VIP-R antagonist of any of Claims 1-3, wherein the Fc domain is conjugated to the amino terminus of the VIP-R antagonist peptide.

5. The modified VIP-R antagonist of any of Claims 1-3, wherein the Fc domain is conjugated to the carboxyl terminus of the VIP-R antagonist peptide.

6. The modified VIP-R antagonist of any of Claims 4 or 5, wherein the Fc domain comprises the sequence as set forth in SEQ ID NO: 26.

7. The modified VIP-R antagonist of any of Claims 1-6, wherein the modified VIP-R antagonist comprises SEQ ID NO: 27, SEQ ID NO: 28, SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 32, SEQ ID NO: 33, SEQ ID NO: 34, SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, or SEQ ID NO:

398. A pharmaceutical composition comprising the vasoactive intestinal peptide receptor (VIP-R) antagonist of any of Claims 1-7 and a pharmaceutically acceptable carrier.

9. A nucleic acid encoding the amino acid sequence of a vasoactive intestinal peptide receptor (VIP-R) antagonist of any of Claims 1-7.

10. An expression vector comprising the nucleic acid of Claim 9.

11. A cell comprising the expression vector of Claim 10.

12. A method of ex vivo augmenting T cell activation and / or expansion, comprising mixing one or more T cells with the vasoactive intestinal peptide receptor (VIP-R) antagonist of any of Claims 1-7 or the pharmaceutical composition of claim 8.

13. The method of Claim 12, wherein mixing the one or more T cells is in combination with an anti-CD3 antibody and / or an anti-CD28 antibody.

14. The method of Claim 12 or 13, wherein mixing the one or more T cells is in combination with a phosphatidylinositol 3-kinase (PI3K) inhibitor.

15. The method of Claim 14, wherein the PI3K inhibitor is a PI3Ka inhibitor, a PI3KP inhibitor, a PI3K5 inhibitor, or a PI3Ky inhibitor.

16. The method of Claim 14 or 15, wherein the PI3K inhibitor comprises idelalisib, copanlisib, duvelisib, alpelisib, umbralisib, buparlisib, copanlisib, dactolisib, leniolisib, parsaclisib, paxalisib, taselisib, zandelisib, inavolisib, apitolisib, bimiralisib, eganelisib, fimepinostat, gedatolisib, linperlisib, nemiralisib, pilaralisib, samotolisib, seletalisib, serabelisib, sonolisib, tenalisib, voxtalisib, AMG 319, AZD8186, GSK2636771, SF1126, acalisib, omipalisib, AZD8835, CAL263, GSK1059615, MEN1611, PWT33597, TG100-115, or ZSTK474.

17. The method of any of Claims 12-16, wherein mixing the one or more T cells is in combination with an immune checkpoint blockade.

18. The method of Claim 17, wherein the immune checkpoint blockade comprises a PD-1 inhibitor, a PD-L1 inhibitor, a CTLA-4 inhibitor, an anti-TIM3 inhibitor, an anti-LAG3inhibitor, an anti-CD47 inhibitor, imiquimod, polyinosinic-polycytidylic acid-poly-l-lysine carboxymethylcellulose (poly-ICLC) , pexidartinib, an anti-TIGIT inhibitor, an anti-B7-H3 inhibitor, an anti-B7-H4 inhibitor, an anti-A2aR inhibitor, an anti-CD73 inhibitor, an anti- NKG2A inhibitor, an anti-PVRIG / PVRL2 inhibitor, an anti-CEACAMl inhibitor, an anti- CEACAM5 inhibitor, an anti-CEACAM6 inhibitor, an focal adhesion kinase (FAK) inhibitor, a CCL2 / CCR2 inhibitor, an anti-leukemia inhibitory factor (LTF) inhibitor, an anti-CD47 / STRPa inhibitor, an anti-colony-stimulating factor (CSF)-l inhibitor, an anti-IL-1 inhibitor, an anti-IL- 1R3 inhibitor, an anti-IL-8 inhibitor, an anti-semaphorin 4D (Sema4D) inhibitor, an angiopoietin(Ang)-2 inhibitor, a CLEVER- 1 inhibitor, Axl-targeted enapotamab vedotin (EnaV), or an anti-phosphatidylserine inhibitor.

19. The method of Claim 18, wherein the immune checkpoint blockade comprises a PD-1 inhibitor, a PD-L1 inhibitor, or a CTLA-4 inhibitor.

20. The method of Claim 19, the immune checkpoint blockade comprises pembrolizumab, nivolumab, cemiplimab, dostarlimab, atezolizumab, avelumab, durvalumab, or ipilimumab.

21. A method of treating a microbial infection in a subject in need, comprising administering to the subject infected with a microbe or at risk for a microbial infection a therapeutically effective amount of the vasoactive intestinal peptide receptor (VIP-R) antagonist of any of Claims 1-7 or the pharmaceutical composition of claim 8.

22. The method of claim 21 wherein the microbial infection is a viral infection, a bacterial infection, a fungal infection, and / or a parasitic infection.

23. The method of Claim 21 or 22, further comprising administering to the subject a therapeutically effective amount of a phosphatidylinositol 3-kinase (PI3K) inhibitor.

24. The method of claim 23, wherein the PI3K inhibitor is a PI3Ka inhibitor, a PI3KP inhibitor, a PI3K5 inhibitor, or a PI3Ky inhibitor.

25. The method of claim 23 or 24, wherein the PI3K inhibitor comprises idelalisib, copanlisib, duvelisib, alpelisib, umbralisib, buparlisib, copanlisib, dactolisib, leniolisib,parsaclisib, paxalisib, taselisib, zandelisib, inavolisib, apitolisib, bimiralisib, eganelisib, fimepinostat, gedatolisib, linperlisib, nemiralisib, pilaralisib, samotolisib, seletalisib, serabelisib, sonolisib, tenalisib, voxtalisib, AMG 319, AZD8186, GSK2636771, SF1126, acalisib, omipalisib, AZD8835, CAL263, GSK1059615, MEN1611, PWT33597, TG100-U5, or ZSTK474.

26. The method of any one of Claims 21-25, further comprising administering to the subject a therapeutically effective amount of an immune checkpoint blockade.

27. The method of Claim 26, wherein the immune checkpoint blockade comprises a PD-1 inhibitor, a PD-L1 inhibitor, a CTLA-4 inhibitor, an anti-TlM3 inhibitor, an anti-LAG3 inhibitor, an anti-CD47 inhibitor, imiquimod, polyinosinic-polycytidylic acid-poly-l-lysine carboxymethylcellulose (poly-ICLC) , pexidartinib, an anti-TIGIT inhibitor, an anti-B7-H3 inhibitor, an anti-B7-H4 inhibitor, an anti-A2aR inhibitor, an anti-CD73 inhibitor, an anti- NKG2A inhibitor, an anti-PVRIG / PVRL2 inhibitor, an anti-CEACAM 1 inhibitor, an anti- CEACAM5 inhibitor, an anti-CEACAM6 inhibitor, an focal adhesion kinase (FAK) inhibitor, a CCL2 / CCR2 inhibitor, an anti-leukemia inhibitory factor (LIF) inhibitor, an anti-CD47 / SIRPa inhibitor, an anti-colony-stimulating factor (CSF)-l inhibitor, an anti-IL-1 inhibitor, an anti-IL- 1R3 inhibitor, an anti-IL-8 inhibitor, an anti-semaphorin 4D (Sema4D) inhibitor, an angiopoietin(Ang)-2 inhibitor, a CLEVER- 1 inhibitor, Axl-targeted enapotamab vedotin (EnaV), or an anti-phosphatidylserine inhibitor.

28. The method of Claim 26 or 27, wherein the immune checkpoint blockade comprises a PD-1 inhibitor, a PD-L1 inhibitor, or a CTLA-4 inhibitor.

29. The method of claim 28, wherein the immune checkpoint blockade comprises pembrolizumab, nivolumab, cemiplimab, dostarlimab, atezolizumab, avelumab, durvalumab, or ipilimumab.

30. A method of treating a cancer and / or metastasis in a subject in need, comprising administering to the subject a therapeutically effective amount of the vasoactive intestinal peptide receptor (VIP-R) antagonist of any of Claims 1-9 or the pharmaceutical composition of Claim 10.

31. The method of Claim 30, wherein the cancer comprises pancreatic cancer, colon cancer, leukemia, liver cancer, lung cancer, or melanoma.

32. The method of Claim 30 or 31 , further comprising administering to the subject a therapeutically effective amount of a phosphatidylinositol 3-kinase (PI3K) inhibitor.

33. The method of Claim 32, wherein the PI3K inhibitor is a PI3Ka inhibitor, a PI3K0 inhibitor, a PI3K8 inhibitor, or a PI3Ky inhibitor.

34. The method of Claim 32 or 33, wherein the PI3K inhibitor comprises idelalisib, copanlisib, duvelisib, alpelisib, umbralisib, buparlisib, copanlisib, dactolisib, leniolisib, parsaclisib, paxalisib, taselisib, zandelisib, inavolisib, apitolisib, bimiralisib, eganelisib, fimepinostat, gedatolisib, linperlisib, nemiralisib, pilaralisib, samotolisib, seletalisib, serabelisib, sonolisib, tenalisib, voxtalisib, AMG 319, AZD8186, GSK2636771, SF1126, acalisib, omipalisib, AZD8835, CAL263, GSK1059615, MEN1611, PWT33597, TG100-115, or ZSTK474.

35. The method of any one of Claims 30-34, further comprising administering to the subject a therapeutically effective amount of an immune checkpoint blockade.

36. The method of Claim 35 wherein the immune checkpoint blockade comprises a PD-1 inhibitor, a PD-L1 inhibitor, a CTLA-4 inhibitor, an anti-TIM3 inhibitor, an anti-LAG3 inhibitor, an anti-CD47 inhibitor, imiquimod, polyinosinic-polycytidylic acid-poly-l-lysine carboxymethylcellulose (poly-ICLC) , pexidartinib, an anti-TIGIT inhibitor, an anti-B7-H3 inhibitor, an anti-B7-H4 inhibitor, an anti-A2aR inhibitor, an anti-CD73 inhibitor, an anti- NKG2A inhibitor, an anti-PVRIG / PVRL2 inhibitor, an anti-CEACAMl inhibitor, an anti- CEACAM5 inhibitor, an anti-CEACAM6 inhibitor, an focal adhesion kinase (FAK) inhibitor, a CCL2 / CCR2 inhibitor, an anti-leukemia inhibitory factor (LIF) inhibitor, an anti-CD47 / SIRPa inhibitor, an anti-colony-stimulating factor (CSF)-l inhibitor, an anti-IL-1 inhibitor, an anti-IL- 1R3 inhibitor, an anti-IL-8 inhibitor, an anti-semaphorin 4D (Sema4D) inhibitor, an angiopoietin(Ang)-2 inhibitor, a CLEVER- 1 inhibitor, Axl-targeted enapotamab vedotin (EnaV), or an anti-phosphatidylserine inhibitor.

37. The method of Claim 35 or 36, wherein the immune checkpoint blockade comprises a PD-1 inhibitor, a PD-L1 inhibitor, or a CTLA-4 inhibitor.

38. The method of claim 37, wherein the immune checkpoint blockade comprises pembrolizumab, nivolumab, cemiplimab, dostarlimab, atezolizumab, avelumab, durvalumab, or ipilimumab.

39. A method of enhancing an immune response to a cancer and / or metastasis in a subject, comprising administering to the subject a therapeutically effective amount of the vasoactive intestinal peptide receptor (VIP-R) antagonist of any of Claims 1-7 or the pharmaceutical composition of claim 8.

40. The method of Claim 39, wherein the cancer comprises pancreatic cancer, colon cancer, leukemia, liver cancer, lung cancer, or melanoma.

41. The method of Claim 39 or 40, further comprising administering to the subject a therapeutically effective amount of a phosphatidylinositol 3-kinase (PI3K) inhibitor.

42. The method of claim 41, wherein the PI3K inhibitor is a PI3Ka inhibitor, a PI3KP inhibitor, a PI3K5 inhibitor, or a PI3Ky inhibitor.

43. The method of claim 41 or 42, wherein the the PI3K inhibitor comprises idelalisib, copanlisib, duvelisib, alpelisib, umbralisib, buparlisib, copanlisib, dactolisib, leniolisib, parsaclisib, paxalisib, taselisib, zandelisib, inavolisib, apitolisib, bimiralisib, eganelisib, fimepinostat, gedatolisib, linperlisib, nemiralisib, pilaralisib, samotolisib, seletalisib, serabelisib, sonolisib, tenalisib, voxtalisib, AMG 319, AZD8186, GSK2636771, SF1126, acalisib, omipalisib, AZD8835, CAL263, GSK1059615, MEN1611, PWT33597, TG100-115, or ZSTK474.

44. The method of any one of Claims 39-43, further comprising administering to the subject a therapeutically effective amount of an immune checkpoint blockade.

45. The method of Claim 44, wherein the immune checkpoint blockade comprises a PD- 1 inhibitor, a PD-L1 inhibitor, a CTLA-4 inhibitor, an anti-TIM3 inhibitor, an anti-LAG3 inhibitor, an anti-CD47 inhibitor, imiquimod, polyinosinic-polycytidylic acid-poly-l-lysine carboxymethylcellulose (poly-ICLC) , pexidartinib, an anti-TIGIT inhibitor, an anti-B7-H3 inhibitor, an anti-B7-H4 inhibitor, an anti-A2aR inhibitor, an anti-CD73 inhibitor, an anti- NKG2A inhibitor, an anti-PVRTG / PVRL2 inhibitor, an anti-CEAC AM 1 inhibitor, an anti- CEACAM5 inhibitor, an anti-CEACAM6 inhibitor, an focal adhesion kinase (FAK) inhibitor, a CCL2 / CCR2 inhibitor, an anti-leukemia inhibitory factor (LIF) inhibitor, an anti-CD47 / SIRPa inhibitor, an anti-colony-stimulating factor (CSF)-l inhibitor, an anti-IL-1 inhibitor, an anti-IL- 1R3 inhibitor, an anti-IL-8 inhibitor, an anti-semaphorin 4D (Sema4D) inhibitor, an angiopoietin(Ang)-2 inhibitor, a CLEVER- 1 inhibitor, Axl-targeted enapotamab vedotin (EnaV), or an anti-phosphatidylserine inhibitor.

46. The method of Claim 44 or 45, wherein the immune checkpoint blockade comprises a PD-1 inhibitor, a PD-L1 inhibitor, or a CTLA-4 inhibitor.

47. The method of claim 46, wherein the immune checkpoint blockade comprises pembrolizumab, nivolumab, cemiplimab, dostarlimab, atezolizumab, avelumab, durvalumab, or ipilimumab.

48. A method of treating a cancer or a chronic infection in a subject in need, comprising obtaining one or more T cells; mixing the one or more T cells with the vasoactive intestinal peptide receptor (VIP-R) antagonist of any of Claims 1-7 or the pharmaceutical composition of claim 8 thereby expanding the one or more T cells; and administering a therapeutically effective amount of the expanded T cells to the subject.

49. The method of claim 48, wherein mixing the one or more T cells is in combination with an anti-CD3 antibody and / or an anti-CD28 antibody.

50. The method of claim 48 or 49, wherein mixing the one or more T cells is in combination with a phosphatidylinositol 3-kinase (PI3K) inhibitor.

51. The method of claim 50, wherein the P13K inhibitor is a P13Ka inhibitor, a P13KP inhibitor, a PI3K5 inhibitor, or a PI3Ky inhibitor.

52. The method of any one of claims 48-51, wherein mixing the one or more T cells is in combination with an immune checkpoint blockade.

53. The method of any one of claims 48-52, wherein the one or more T cells are derived from the subject.

54. The method of any one of claims 48-53, wherein the one or more T cells comprises a chimeric antigen receptor.

55. The method of any one of claims 48-54, wherein the expanded T cells have increased levels of CD28 and / or CD27 compared with levels prior to expansion.

56. The method of any one of claims 48-55, wherein expanded T cells have decreased levels of PD-1, TIM-3, and / or Lag3 compared with levels prior to expansion.

57. The method of any one of claims 48-56, further comprising administering to the subject a PI3 kinase inhibitor or a VIP receptor antagonist, or an immune checkpoint blockade, or a combination thereof before, during, or after administering the expanded T cells.

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