50 results about "Lytic peptide" patented technology

Amphipathic lytic peptides are ideally suited to use in a ligand/cytotoxin combination to specifically inhibit cells that are driven by or are dependent upon a specific ligand interaction; for example, to induce sterility or long-term contraception, or to attack tumor cells, or to selectively lyse virally-infected cells, or to attack lymphocytes responsible for autoimmune diseases. The peptides act directly on cell membranes, and need not be internalized. Administering a combination of gonadotropin-releasing hormone (GnRH) (or a GnRH agonist) and a membrane-active lytic peptide produces long-term contraception or sterilization in animals in vivo. Administering in vivo a combination of a ligand and a membrane-active lytic peptide kills cells with a receptor for the ligand. The compounds are relatively small, and are not antigenic. Lysis of gonadotropes has been observed to be very rapid (on the order of ten minutes.) Lysis of tumor cells is rapid. The two components-the ligand and the lytic peptide-may optionally be administered as a fusion peptide, or they may be administered separately, with the ligand administered slightly before the lytic peptide, to activate cells with receptors for the ligand, and thereby make those cells susceptible to lysis by the lytic peptide. The compounds may be used in gene therapy to treat malignant or non-malignant tumors, and other diseases caused by clones or populations of "normal" host cells bearing specific receptors (such as lymphocytes), because genes encoding a lytic peptide or encoding a lytic peptide/peptide hormone fusion may readily be inserted into hematopoietic stem cells or myeloid precursor cells.

The invention is directed to peptides having antimicrobial activity (antimicrobial peptides). The antimicrobial peptides of the present invention are analogs of the Lentivirus Lytic Peptide 1 (LLP1) amino acid sequence. The invention is further directed to peptides referred to as the Lytic Base Unit (LBU) peptides derived from the LLP1 analogs, also having antimicrobial activity. In addition, the present invention is also directed to methods of using the peptides in a variety of contexts, including the treatment or prevention of infectious diseases. The antimicrobial LLP1 analog peptides and the LBU peptides (collectively eLLPs) may be highly active under high salt conditions and in biologic fluids. In addition, the eLLPs are effective when presented either in soluble form, or when attached to a solid surface. Furthermore, the peptides of the present invention are selectively active against a wide variety of bacterial pathogens and exhibit minimal toxicity to eukaryotic cells in vitro and in vivo.

Chimeric proteins are expressed, secreted or released by a bacterium to immunize against or treat a parasite, infectious disease or malignancy. The delivery vector may also be attenuated, non-pathogenic, low pathogenic, or a probiotic bacterium. The chimeric proteins include chimeras of, e.g., phage coat and/or colicin proteins, bacterial toxins and/or enzymes, autotransporter peptides, lytic peptides, multimerization domains, and/or membrane transducing (ferry) peptides. The active portion of the immunogenic chimeric proteins can include antigens against a wide range of parasites and infectious agents, cancers, Alzheimer's and Huntington's diseases, and have enhanced activity when secreted or released by the bacteria, and/or have direct anti-parasite or infectious agent activity. The activity of the secreted proteins is further increased by co-expression of a protease inhibitor that prevents degradation of the effector peptides. Addition of an antibody binding or antibody-degrading protein further prevents the premature elimination of the vector and enhances the immune response.

Non-naturally occurring lytic peptides which contain a phenylalanine residue and one or more alanine, valine and lysine residues, and optionally contain chemically masked cysteine or serine residues possess an amphipathic structure which allows them to promote cell lysis in certain pathologic organisms, and particularly in prokaryotes. Peptides having a beta-pleated sheet secondary structure and lacking cysteine residues form one embodiment of these lytic peptides.

This invention relates to novel synthetic lytic peptide fragments of full-length peptides with the capacity to modulate angiogenic activity in mammals. The invention also relates to the use of such peptides in pharmaceutical compositions and in methods for treating diseases or disorders that are associated with angiogenic activity.

Nanoparticle compositions and methods are disclosed for the sustained release of small molecules, such as pharmaceutical compounds in vivo, for example ligand-lytic peptide conjugates. The construction of the nanoparticles helps to prevent self-aggregation of the molecules, and the consequent loss of effectiveness. The system employs layer-by-layer self-assembly of biocompatible polyelectrolyte layers, and layers of charged small molecules such as drug molecules, to form a multilayer nanoparticle in which the drug or other small molecule itself acts as one of the alternating charged layers in the multilayer assembly. The small molecules can then be released over time in a sustained manner. The LbL nano-assemblies can specifically target cancers, metastases, or other diseased tissues, while minimizing side effects.

Amphipathic lytic peptides are ideally suited to use in a ligand/cytotoxin combination to induce sterility or long-term contraception in mammals. The peptides act directly on cell membranes, and need not be internalized. Administering a combination of gonadotropin-releasing hormone (GnRH) (or a GnRH agonist) and a membrane-active lytic peptide produces long-term contraception or sterilization in mammals in vivo. The compounds are relatively small, and are not antigenic. Lysis of gonadotropes has been observed to be very rapid (on the order of ten minutes.) The two components-the ligand and the lytic peptide-may optionally be administered as a fusion peptide, or they may be administered separately, with the ligand administered slightly before the lytic peptide, to activate cells with receptors for the ligand, and thereby make those cells susceptible to lysis by the lytic peptide.

A cytotoxin can be rendered non-toxic by charge neutralizing the amino acids salient to pore assembly and/or sterically inhibiting formation of the peptide's active conformation. In the presence of specific proteases, the inactive peptide or procytotoxin can be activated to assemble into its lytic conformation and selectively destroy a target cell.

This invention relates to novel lytic peptides which are effective in treating citrus plant diseases including canker and greening. The invention also relates to antimicrobial compositions comprising lytic peptides and the use of such compositions in methods for treating diseases of citrus plants.

An acid-resistant peptide solubility tag (an “inclusion body tag”) is provided that is effective in producing peptides of interest in an insoluble form. Fusion peptide constructs comprising the inclusion body tag fused to a peptide of interest are provided. An acid cleavable peptide moiety separates the inclusion body tag from the peptide of interest so that acid hydrolysis can be used during subsequent processing steps to separate the tag from the desired peptide of interest. The present inclusion body tag's resistance to acid hydrolysis facilitates easier and cleaner separation of the peptide of interest after acid hydrolysis. Specifically, a ketosteroid isomerase-derived inclusion body tag is provided that has been engineered to be more resistant to acid hydrolysis.

This invention relates to novel synthetic lytic peptide fragments of full-length peptides with the capacity to modulate angiogenic activity in mammals. The invention also relates to the use of such peptides in pharmaceutical compositions and in methods for treating diseases or disorders that are associated with angiogenic activity.

The invention relates to nucleolin binding peptides, nucleolin binding peptides and anti-nucleolin antibody conjugates with cytotoxic activity, fusion constructs, methods of using nucleolin binding peptides and antibodies and fusion constructs thereof, and methods of treating various disorders, undesirable conditions and diseases treatable with nucleolin binding peptides and fusion constructs, such as undesirable or aberrant cell proliferation (hyperproliferation) or hyperproliferative disorders, including tumors, cancers, neoplasia and malignancies, angiogenesis related or dependent diseases, and inflammatory diseases and inflammation.

It is an object of the present invention to provide a substance usable as an anticancer agent or DDS, which has intracellular stability, which is capable of evading side effects from functional disorder with respect to normal cells, or which has instantaneous effect. The inventors developed a novel chimeric peptide targeting cancer cells which overexpress EGFR or the like using a binding peptide such as a peptide sequence binding to EGFR, and a lytic peptide sequence, thereby solving such an object. Particularly, by using a chimeric peptide including an EGF receptor-binding peptide or the like and a cytotoxic peptide, this object was solved.

The present invention provides a composition and a method for cleaving a peptide from a solid support resin. Hydrochloric acid in an organic water miscible solvent is used to cleave the peptide-resin attachment. Optionally, trifluoroethanol or hexafluoroisopropanol may be added to the cleavage composition to improve results. When using the present cleavage composition, an evaporation or other step to remove carboxylic byproducts is not necessary following the cleavage reaction. After the resin is filtered out of the cleavage mixture, the peptide may be immediately precipitated with water.

The invention relates to conjugates that bind to Her2/neu, methods of using conjugates that bind to Her2/neu and methods of treating undesirable or aberrant cell proliferation or hyperproliferative disorders, such as tumors, cancers, neoplasia and malignancies that express Her2/neu.

The invention relates to a method for preparing polypeptide or pharmaceutically acceptable salts. The method comprises the following steps of 1, synthesizing a full-protection peptide sequence on a solid phase carrier, and obtaining peptide resin; 2, adopting a lysate for pyrolyzing the peptide resin, and obtaining crude peptide; 3, adopting an iodine oxidation method for directly performing a disulfide bond cyclization reaction on the crude peptide. The preparation method is applicable to preparing the polypeptide in large scale, and the preparation scale can reach the hectogram scale to thekilogram scale.

The invention relates to a polygene element realizing equivalent expression of two genes based on 2A lytic peptide, an expression vector and application. The gene element is formed by Ck and the 2A lytic peptide, wherein a nucleotide sequence of the 2A lytic peptide is as shown in SEQ ID NO.38, and a nucleotide sequence of the Ck is as shown in SEQ ID NO.39. The vector containing the element can be used for equivalently performing recombination expression on the genes located on two ends of 2A so as to have significance on realizing silkworm poly-gene expression.

The invention belongs to the technical field of biological medicines, and particularly relates to a compound polypeptide molecule for targeted killing of cancer cells and a preparation method thereof. The compound polypeptide molecule comprises gallic acid, a cracking peptide and a polypeptide substrate which is connected between the gallic acid and the cracking peptide and is used for MMP-2 specific recognition degradation. In the composite polypeptide molecule, the electronegative gallic acid small molecule can effectively neutralize the electropositivity and the split membrane activity of the split peptide, so that the damage of the split peptide to normal cells in the in-vivo circulation process can be effectively prevented, and after the composite polypeptide molecule enters cancer tissues, the cancer cells secrete a large amount of MMP-2 protein, the MMP-2 protein can recognize and degrade a polypeptide substrate connected between gallic acid and lytic peptide, so that free lytic peptide is released, and the effect of killing cancer cells in a targeted manner can be achieved.