30 results about "Melanocyte-stimulating hormone" patented technology

The presence of the ancient anti-inflammatory peptide α-melanocyte stimulating hormone (α-MSH [1-13], SYSMEHFRWGKPV) in barrier organs such as gut and skin suggests a role in the nonspecific (innate) host defense system. α-MSH and other amino acid sequences derived from α-MSH were determined to have antimicrobial influences, including against two major and representative cutaneous and mucosal pathogens: Staphylococcus aureus and Candida albicans. C-MSH peptides had antimicrobial effects against S. aureus and significantly reversed the enhancing effect of urokinase on S. aureus colony formation. α-MSH and other amino acid sequences reduced C. albicans viability and germination. α-MSH peptides also enhanced C. albicans killing by human neutrophils. The antimicrobial agent is selected from the group consisting of one or more peptides including the amino acid sequence KPV, one or more peptides including the amino acid sequence MEHFRWG, or a biologically functional equivalent of any of the foregoing. The most effective of the peptides were those bearing the C-terminal amino acid sequence of α-MSH, i.e., α-MSH (1-13), (6-13), and (11-13). The α-MSH “core” sequence (4-10), important for melanotropic effects, was also effective but significantly less potent. Antimicrobial influences of α-MSH peptides could be mediated by their well-known capacity to increase cellular cAMP; this messenger was significantly augmented in peptide-treated yeast. α-MSH has potent anti-inflammatory effects and is expected to be useful for treatment of inflammation in human and veterinary disorders. Reduced killing of pathogens is a detrimental consequence of therapy with corticosteroids and nonsteroidal anti-inflammatory drugs during infection. Therefore, anti-inflammatory agents based on α-MSH peptides that do not reduce microbial killing, but rather enhance it, would be very useful. The antimicrobial effects of these α-MSH peptides occurred over a broad range of concentrations including the physiological (picomolar) range.

The present invention relates to methods of using GPR101 G protein-coupled receptor (GPCR) to screen candidate compounds as modulators of hypothalamic proopiomelanocortin (POMC)-derived biologically active peptide secretion. Modulators of GPR101 receptor modulate hypothalamic POMC-derived biologically active peptide secretion and are useful in the treatment of POMC-derived biologically active peptide-related disorders. POMC-derived biologically active peptides include, but are not limited to, α-melanocyte stimulating hormone (α-MSH), β-melanocyte stimulating hormone (β-MSH) and γ-melanocyte stimulating hormone (γ-MSH). Agonists and partial agonists of GPR101 receptor stimulate hypothalamic α-MSH, β-MSH and γ-MSH secretion and are useful, for example, in the treatment and prevention of obesity and conditions related thereto (including but not limited to Type 2 diabetes, insulin resistance, and metabolic syndrome), inflammation-associated disorders, and pyrexia. Inverse agonists and antagonists of GPR101 receptor inhibit α-MSH, β-MSH and γ-MSH secretion and are useful, for example, in the treatment and prevention of disorders such as cachexia.

The invention discloses recombinant diphtheria toxin and its preparation method and application. A connecting peptide composed of (Gly4Ser)2 is added between diphtheria toxin DAB389 and α-melanocytostimulating hormone. For the convenience of recombinant toxin purification, add Prefix body, amplify the prefix body + DAB389(Gly4Ser) 2-αMSH gene fragment, construct the pET28a / prefix body + DAB389(Gly4Ser) 2-αMSH expression plasmid, transform it into E. coli for expression, induce with IPTG, and obtain the prefix body + The expression protein of DAB389(Gly4Ser)2-αMSH is purified, digested with factor Xa, and separated to obtain the fusion protein of DAB389(Gly4Ser)2-αMSH. The present invention proves through experiments that the recombinant diphtheria toxin has the advantages of convenient purification and reduced cost , high yield, and the advantages of improving the activity of the recombinant toxin; at the same time, it has the characteristics of specific attack and killing on malignant melanoma, but has no damage to normal cells, and achieves the purpose of effectively treating malignant melanoma.

A method for inducing melanogenesis in a human subject having a melanocortin 1 receptor (MC1R) variant allele associated with loss of or diminished receptor function comprises administering to said subject an amount of an α-melanocyte stimulating hormone (α-MSH) analogue effective to induce melanogenesis by the melanocytes in the skin or other epidermal tissue of the subject.

Alpha-melanocyte stimulating hormone (α-MSH) or an equivalent is used, in conjunction with erythropoietin (EPO) or equivalent, to prevent or treat ischemic conditions.

The invention discloses α - Application of melanocyte-stimulating hormone in preparing medicine for treating elevated white blood cells and preventing radiation damage. The prevention of radiation damage refers to: melanocyte-stimulating hormone promotes the proliferation of bone marrow and spleen cells. The elevated leukocytes refers to leukopenia caused after chemotherapy. The prophylactic administration of the present invention can effectively improve the 30-day survival rate of mice irradiated with a lethal dose. Simultaneous prophylactic administration has obvious protective effect on chemotherapy-induced leukopenia and thrombocytopenia without obvious toxic and side effects.

The invention discloses a method of applying a class of functional peptide to regulate golden yellow body color of large yellow croaker, and relates to large yellow croaker. The method is injecting the functional peptide, soaking the functional peptide, or taking the peptide orally; the method of injecting the functional peptide comprises the steps that alpha-melanocyte stimulating hormone is dissolved in normal saline with the sodium chloride concentration of 0.65-0.90 g / mL, intraperitoneal injection is conducted, the body color of the large yellow croaker turns to golden yellow from silver white, and the golden yellow color keeps 24 hours or longer; the method of soaking the functional peptide comprises the steps that a whole large yellow croaker fish is soaked in seawater containing thefunctional peptide with the concentration larger than or equal to 0.5 mM, after soaking, the body color of the large yellow croaker fish turns to golden yellow from silver white, and the golden yellow color keeps 24 hours or longer; the method of taking the functional peptide orally comprises the steps that the functional peptide solution is poured into the stomach of the large yellow croaker, the dosage is larger than or equal to 0.3 nmol per gram of weight, after gastric perfusion, the body color of the large yellow croaker turns to golden yellow from silver white, and the golden yellow color keeps 12 hours or longer.

The invention belongs to the field of genetic engineering pharmaceutics, and particularly relates to a fusion protein of alpha-melanophore stimulating hormone. The fusion protein comprises a PTD (protein transduction domain), an HSA (albumin human) and an alpha-MSH (alpha-melanocyte stimulating hormone). The fusion protein has the advantages that by adding a flexible connecting peptide between the alpha-MSH and the HSA, the high-level stable expression of the fusion protein in a host is guaranteed; while the biological activity of the alpha-MSH is maintained, a blood brain barrier can be effectively crossed, and the medicine effect is improved; the effect of delaying a half-life period is realized. The invention also provides a preparation method of the fusion protein, and application of the fusion protein in inhibiting or treating central nervous system inflammation.

Disclosed is a fusion protein for α-Melanocyte stimulating hormone, the fusion protein containing a protein transduction domain (PTD), a human serum albumin (HSA) and an α-Melanocyte stimulating hormone (α-MSH). Also disclosed are a method for preparing the fusion protein and a use thereof for inhibiting or treating central nervous system inflammations.