Amino Acids (AA)

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H-Gly-Met-Gly-OH is an amide containing a sulfoxide group. It is synthesized from the amino acid glycine and the tripeptide Met-Gly-Gly. The synthesis of HMG was first reported by Sato in 1907, although it was not used as a drug until 1983. This drug has potential antitumor activity and inhibits the growth of certain tumor cells. HMG is metabolized by peptidases, which hydrolyze the peptide bond between glycine and Met-Gly-Gly. Hydrolysis of HMG yields glyoxylic acid (H2O2) and the amino acids glycine and methanol. HMG also inhibits the uptake of glucose into cells, which may be related to its antitumor effect. X-ray diffraction studies have shown that HMG has a carboxylate group at C6 that binds to three oxygen atoms, which are present in two

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(S)-9,10-Difluoro-2,3-dihydro-3-methyl-7-oxo-7H-pyrido[1,2,3-de]-1,4-benzoxazine-6-carboxylic acid ethyl ester is an acidic substance that can be produced by the amination of piperazine with chloroacetic acid. The reaction solution is heated to a temperature of about 120°C for about 30 minutes and then cooled to room temperature. The product precipitates as a white solid. This compound has been shown to have antibacterial activity against methicillin resistant Staphylococcus aureus (MRSA) in plates.

Hirullin H-Ser-Asp-Phe-Glu-Glu-Phe-Ser-Leu-Asp-Asp-Ile-Glu-Gln is a peptide with a carboxy terminal and carbonyl group. It has minimal inhibitory concentrations of about 100 nM for most bacteria and is active against the majority of Gram positive bacteria. Hirullin H is composed of amino acid sequences that are similar to the sequences of active substances in other compounds, such as hirulog, an anticoagulant, and heparin, an antithrombotic drug. Hirullin H has been shown to have bifunctional properties by inhibiting thrombin, which is responsible for blood clotting, while also inhibiting platelet activation.

Amylin (mouse, rat) trifluoroacetate is a synthetic peptide, which is a derivative of the islet amyloid polypeptide (IAPP) found in rodent species. It is sourced from the pancreatic beta cells of mice and rats, where it is co-secreted with insulin. The mode of action involves regulation of glucose metabolism through its effects on gastric emptying, glucagon secretion, and satiety. These actions are crucial in managing postprandial blood glucose levels and provide insights into the pathophysiology of diabetes.Amylin (mouse, rat) trifluoroacetate is primarily used in research applications to study the mechanisms of amylin aggregation and its implications in type 2 diabetes. It also serves as a model for understanding the differences in amyloid fibril formation between human and rodent amylin, making it invaluable for the development of therapeutic strategies aimed at mitigating amyloid-related cellular toxicity. Researchers utilize this peptide to explore the potential compensatory roles of amylin analogs in diabetic models, advancing our understanding of diabetes progression and treatment options.

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H-Lys(Boc)-OH is an ε-amino-protected lysine that plays a pivotal role in solution phase peptide synthesis. Strategically protected at the ε-amino group, it allows controlled peptide assembly, and it serves as intermediate for synthesizing β-peptides. The bulky Boc (tert-butyloxycarbonyl) group shields its epsilon amine (NH2) group, acting as a protective measure to prevent unwanted side reactions.

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MeOSuc-Ala-Ala-Pro-Val-chloromethylketone is a serine protease inhibitor that has been shown to be effective against influenza virus and HIV. It was found to be active against a number of serine proteases, such as trypsin, chymotrypsin, and elastase. MeOSuc-Ala-Ala-Pro-Val-chloromethylketone also has chemotactic activity in thp1 cells and lung fibroblasts. It is activated by the addition of water and has been shown to inhibit the growth of soybean trypsin. However, it does not have any effect on human trypsin.

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Ac-Ala-Ala-Pro-Ala-AMC is a substrate for acetylcholinesterase and its structural analogues, including Ac-Ala-Glu-Phe. It has been found to be an isomerase that catalyzes the conversion of L-serine to D-serine in human cells. The enzyme displays a high resolution crystal structure with water molecules bound at the active site. The enzyme is a dimer composed of two identical monomers. The enzyme binds two substrates through hydrogen bonding interactions and then undergoes a conformational change, which releases the products as water molecules are released from the active site.

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