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Gastric Pentadecapeptide BPC-157 (also known as PL 14736, Body Protection Compound 157, or Bepecin) is a fifteen amino acid long oligopeptide that was discovered during research on human gastric juice. [1]
Rational Numbers Excel Add-In Proprietary: De novo identification tool for small molecules that works with Microsoft Excel (2010, 2013, 2016 and 2019). This software treats small molecules as mathematical partitions of the molecular mass and generates subfragment formulas with atoms that are sets of partitions comprising the molecular formula.
Examorelin (developmental code names EP-23905, MF-6003), also known as hexarelin, is a potent, synthetic, peptidic, orally-active, centrally-penetrant, and highly selective agonist of the ghrelin/growth hormone secretagogue receptor (GHSR) and a growth hormone secretagogue which was developed by Mediolanum Farmaceutici.
Radiolabeled peptides containing RGD show high affinity and selectivity for integrin αVβ3 and are being investigated as tools to monitor treatment response of tumors via PET imaging. [24] These include 18 F-Galacto-RGD, 18 F-Fluciclatide-RGD, 18 F-RGD-K5, 68 Ga-NOTA-RGD, 68 Ga-NOTA-PRGD2, 18 F-Alfatide, 18 F-Alfatide II, and 18 F-FPPRGD2.
In organic chemistry, peptide synthesis is the production of peptides, compounds where multiple amino acids are linked via amide bonds, also known as peptide bonds. Peptides are chemically synthesized by the condensation reaction of the carboxyl group of one amino acid to the amino group of another.
The Bergmann azlactone peptide synthesis is a classic organic synthesis process for the preparation of dipeptides. In the presence of a base, peptides are formed by aminolysis of N-carboxyanhydrides of amino acids with amino acid esters ( 1 ).
Constituent amino-acids can be analyzed to predict secondary, tertiary and quaternary protein structure. This list of protein structure prediction software summarizes notable used software tools in protein structure prediction, including homology modeling, protein threading, ab initio methods, secondary structure prediction, and transmembrane helix and signal peptide prediction.
The peptide backbone dihedral angles (φ, ψ) are about (–140°, 135°) in antiparallel sheets. In this case, if two atoms C α i and C α j are adjacent in two hydrogen-bonded β-strands, then they form two mutual backbone hydrogen bonds to each other's flanking peptide groups; this is known as a close pair of hydrogen bonds.