Definition-and-Characteristics-of-Active-Peptides-Derived-From-Protein

Definition and Characteristics of Active Peptides Derived From Protein Peptides are chain compounds formed by α-amino acids linked together by peptide bonds, and most biologically active peptides are intermediate products of protein hydrolysis. Some proteins synthesized in the body have no physiological activity or very low activity. After a series of hydrolysis, polypeptide fragments of different lengths are produced, including peptide hormones or biologically active small molecule peptides. These peptides have small molecular weight, wide distribution, diverse biological effects, rapid synthesis and metabolism, and far lower immunogenicity than macromolecular substances, and play an important role in regulating cardiovascular homeostasis. Active peptides include different groups of polypeptide molecules. After genome transcription and translation, pre-pro polypeptides are produced, including secretion-related domains and receptor-binding domains. Pre-pro polypeptides are biologically active through secretion and proteolysis of peptides. Most of the peptides found so far are widely distributed, and the local tissue level is significantly higher than that in plasma, and has tissue distribution specificity, suggesting that most biologically active peptides exert their physiological effects in an autocrine and paracrine manner. In the local tissue, it mainly binds to its corresponding receptor in the form of ligand to mediate intracellular signals and functions. Cardiovascular Active Peptide There are many kinds of cardiovascular active peptides, which play an important role in the occurrence and development of cardiovascular diseases. Among them, some active peptides

were discovered earlier. On the basis of systematic research, scientists also have new physiological functions and their functions as The possibility of drug targets was further explored. Cardiovascular active peptide is an important biologically active peptide. Studies have found that a series of active peptides play a very important role in regulating the homeostasis of the cardiovascular system, including intermediary hormone (IMD), Apelin, ghrelin ( Ghrelin), glucagon-like peptide (GLP1), fibroblast growth factor (FGF21), etc. These active peptides are widely distributed in tissues, have small molecular weight, low immunogenicity, rapid synthesis and metabolism, and after secretion, they interact with ligands and receptors to regulate cardiovascular physiological and pathophysiological processes through various intracellular signaling pathways, for example, Vasomotor and newborn, glycolipid metabolism and myocardial remodeling process after cardiac ischemic injury. Since Robert synthesized the first biologically active peptide in 1953, the research and development trend of peptide drugs has gradually increased. Peptide drugs are mainly derived from natural peptides or endogenous peptides. Their activity is close to that of protein drugs, and their quality control level is close to that of small molecule chemical drugs. It combines the advantages of protein drugs and traditional chemical drugs, and has strong specificity and high purity, small dosage, strong biological activity and low toxicity and side effects, it has a significant curative effect on cardiovascular diseases. The Institute for Biohealth Innovation, currently from George Mason University, has in-depth research on cardiovascular peptides. 1. Intermediary factor (IMD) Adrenomedullin 2 (ADM2), also known as intermedin (IMD), is a secreted polypeptide discovered by Roh in 2004. The IMD gene is located on human chromosome 22, and the full- length gene encodes a secreted peptide precursor containing 148 amino acid residues through transcription and translation. Through gene polymorphism analysis, it was found that intermediate was a new member of calcitonin/CGRP superfamily. Intermediaries are widely expressed in the body and can be artificially synthesized by peptide synthesis biology laboratories such as Omizzur ltd. 2. Glucagon-like peptide (GLP-1) GLP-1 belongs to the incretin family and is encoded by the glucagon gene (GCG), which produces long-chain polypeptide precursors, which can produce a variety of active polypeptides through tissue-specific proteolysis, including GCG, GLP1 and GLP-2. The C-terminal of GLP-1 contains 36 amino acids, has high sequence homology with glucagon, is widely expressed in different species, and can stimulate islet β cells to secrete insulin in a glucose-dependent manner. 3. Ghrelin Ghrelin is an active polypeptide containing 28 acylated amino acids, which was first isolated from the stomach of rats in 1999 and is the endogenous source of the G protein-coupled receptor growth hormone secretagogue receptor (GHSR). Sex ligand, mainly activates

GHSR1a, stimulates the release of growth hormone. In addition to the protective effect of ghrelin on myocardial ischemia, clinical experiments also suggest that it may have a certain therapeutic effect on heart failure. Giving a certain dose of ghrelin to healthy volunteers can reduce systemic vascular resistance and reduce the estimated risk of heart failure and stroke. 4. Apelin Angiotensin-1 receptor-related protein (APJ, also named AGTRL1) is a transmembrane protein in the G protein-coupled family discovered by Canadian scholar O'Dowd et al. in 1993. In 1998, Japanese scholar Tatemoto et al. extracted and purified the natural ligand of APJ from bovine gastric secretion and named it Apelin. The Apelin/APJ system is widely distributed in various tissues in the body, among which higher concentrations are detected in the lung, cardiovascular system and spleen, and the local content in cardiovascular tissue is dozens of times that in plasma, indicating that its distribution has certain tissue specificity , and may be produced by a certain cardiovascular tissue, which has an important physiological effect on the cardiovascular system. Research Limitations and Prospects of Vasoactive Peptides At present, the research on vasoactive polypeptides is mainly found through genome analysis. The research on protein structure and function is progressing slowly, and there is no clear classification and elaboration of vasoactive peptides. It is only a vague concept based on function, which needs further research. For the study of neuropeptides, the concept of peptidomics has been established. In addition to the study of genomics, proteomics and peptidomics can be combined with mass spectrometry to identify the structure of peptides, which can be used for reference in the study of vasoactive peptides. In addition, the metabolic process of peptides in the body after secretion is a rapid dynamic equilibrium process. The half-life of peptides is very short, and they are quickly hydrolyzed by proteolysis. It is difficult to detect the active form in sufficient concentration, and the detected form is not necessarily its active form. For the monitoring and functional detection of polypeptide molecular metabolic processes, it is a difficult problem in the study of peptides at present, and more further research is needed.