A review of polypeptide drugs in the treatment of diseases

71 new antimicrobial peptide families discovered by Chinese researchers Researchers from Kunming Institute of zoology, Chinese Academy of Sciences identified 728 different mature antimicrobial peptides from the skin secretion of Rana odorifera These antimicrobial peptides were divided into 97 families, 71 of which were named for the first time Li Wenhui, an associate researcher of Kunming Institute of zoology, Chinese Academy of Sciences, who participated in the research project, said that the newly discovered antimicrobial peptide molecules will provide a large number of new templates for the design of new antimicrobial peptide drugs, and contribute to the development of new antimicrobial drugs According to reports, in the past two years, researchers from the Key Laboratory of animal model and human disease mechanism of Chinese Academy of Sciences "biotoxin and human disease discipline group" collected nine species of stinking frogs unique to China from Yunnan, Guizhou, Sichuan and other places By means of proteomics and genomics, 728 mature antimicrobial peptide molecules were identified from the skin secretions of these nine species of stinking frogs 662 of them are reported for the first time These antimicrobial peptides account for 30% of the known antimicrobial peptides in nature These antimicrobial peptides were divided into 97 families, 71 of which were named for the first time This study also showed that stinking frogs may be the species with the most diversity of antimicrobial peptides in nature, and proved that the same antimicrobial peptides can be widely distributed in different species of stinking frogs Discovery of amphibian cathelicidin antimicrobial peptide by lairen et al The latest research results of the researchers of Kunming Institute of zoology, Chinese Academy of sciences are published online by the internationally famous journal amino acids In this paper, the amphibian cathelicidin antimicrobial peptide was found for the first time Antimicrobial peptide is an important part of innate immunity Antimicrobial peptides have become a hot spot in the research of new anti infective drugs because they are not easy to lead to drug resistance The team led by researcher Lai Ren has done a lot of work in the exploration and utilization of antimicrobial peptides, identifying more than 500 kinds of antimicrobial peptides Cathelicidin and defensin are the two main antimicrobial peptides in vertebrates Cathelicidin has been found in fish, reptiles, birds and mammals, but has not been found in amphibians Recently, a team led by researcher Lai Ren has identified a new cathelicidin antibacterial peptide from the skin of Rana rufous, which is the first amphibian cathelicidin antibacterial peptide found in the world This discovery fills in the gap in the evolution of the cathelicidin system in vertebrates Bacteria that have evolved antimicrobial resistance may also damage the natural immune system The fight against antibiotic resistant bacteria seems to be growing every day One study aims to develop a new class of antimicrobial therapies, amps, based on small molecules that exhibit bactericidal and immunomodulatory activities But like antibiotics, bacteria can evolve amps resistance, which may lead to bacteria being able to resist the risk of the first defense weapon of the human immune system According to a new study published in the Journal of Biology Letters, scientists have confirmed for the first time that bacterial resistance to an amp evolved under selective pressure can also show cross resistance to a natural host defense peptide Gabriel Perron of Harvard University, who was not involved in the study, said the study was an "important proof of principle." Perron explained that although previous studies have indicated the existence of cross resistance to AMP, this is the first time it has been confirmed that bacteria can also cross resistance to human amps if they are resistant to a synthetic amp designed for treatment Identification of cell penetrating peptide inhibiting hepatitis C virus Researchers at UCLA's Jonsson comprehensive cancer center have identified cell penetrating peptides that inhibit hepatitis C virus proteins and block virus replication, which can lead to liver cancer and cirrhosis French and his team initially used mass spectrometry to identify cytokines involved in hepatitis C virus replication, and found that heat shock proteins (HSPs) 40 and 70 were important for virus infection Hsp70 is a previously known protein involved, but Hsp40 is the first time it has been linked to hepatitis C infection, French said They also showed that quercetin, a natural compound that inhibits the synthesis of these proteins, significantly inhibited viral infection in cultured tissues.