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The screening principle of peptide drug screening is to utilize the specific binding between peptide molecules in the peptide library and the target molecules, to screen out peptides with specific biological activities. Various methods of peptide drug screening are described below.
Preparation Methods | Specification |
---|---|
Extraction Method | Currently, a significant portion of peptide drugs are extracted from plants and animals, such as insulin extracted from pig pancreas. The purity of peptides obtained by the extraction method is low, the content of peptides in organisms is very small, and animal pathogenic bacteria or viruses are easily introduced during the extraction process, thus limiting its application. |
Chemical Synthesis Method | Liquid-phase synthesis of peptides is mainly carried out in solution, and there are two strategies: stepwise synthesis and fragment combination. These two strategies are often used in combination. Some short peptide fragments are first synthesized by stepwise synthesis. The peptide fragments obtained in the previous step are then joined to form the target peptide by fragmentation. |
The solid phase synthesis method involves immobilizing the N-terminus of an amino acid on an insoluble resin and then sequentially condensing the amino acid on this resin. The solid-phase method has become a common technique in peptide and protein synthesis. | |
Recombinant Technology | Recombinant technology is used to form recombinant DNA expression vectors by constructing the gene sequences of polypeptides into vectors, and to express, extract, and purify the polypeptide molecules in prokaryotic or eukaryotic cells. This method is suitable for the preparation of target peptides consisting of more than 50 amino acids and is easier to obtain. |
Enzyme Degradation Method | Since organisms contain a large number of proteins, and some active peptides may be certain sequences in proteins, it can also be cost-saving if more readily available proteins can be degraded into the desired peptide molecules. Enzymatic degradation methods often require the search for enzymes that catalyze catabolic reactions at specific structures, which can efficiently function at all the same structures in the protein. |
CAT# | Product Name | CAS | Sequence |
---|---|---|---|
10-101-291 | Bradykinin 1-7 | 23815-87-4 | Arg-Pro-Pro-Gly-Phe-Ser-Pro |
10-101-293 | GLP-1(7-36) Acetate | 1119517-19-9 | HAEGTFTSDVSSYLEGQAAKEFIAWLVKGR |
10-101-295 | Neurokinin A | 86933-74-6 | H-His-Lys-Thr-Asp-Ser-Phe-Val-Gly-Leu-Met-NH2 |
10-101-317 | Galanin, human | 119418-04-1 | GWTLNSAGYLLGPHAVGNHRSFSDKNGLTS |
10-101-319 | Orexin B human | 205640-91-1 | RSGPPGLQGRLQRLLQASGNHAAGILTM |
10-101-40 | Ornipressin | 3397-23-7 | Cys-Tyr-Phe-Gln-Asn-Cys-Pro-Orn-Gly-NH2(Cys1-Cys6) |
10-101-43 | Aviptadil Acetate | 40077-57-4 | HSDAVFTDNYTRLRKQMAVKKYLNSILN |
10-101-51 | Protirelin | 24305-27-9 | {pGlu}-His-Pro-NH2 |
10-101-53 | Eledoisin | 69-25-0 | H-Pyr-Pro-Ser-Lys-Asp-Ala-Phe-Ile-Gly-Leu-Met-NH2 |
10-101-66 | Kassinin | 63968-82-1 | H-Asp-Val-Pro-Lys-Ser-Asp-Gln-Phe-Val-Gly-Leu-Met-NH2 |
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