CAS 116939-85-6
:Boc-Met-Pro-OH
Description:
Boc-Met-Pro-OH, also known as N-Boc-L-methionyl-L-proline, is a protected amino acid derivative commonly used in peptide synthesis. The "Boc" (tert-butyloxycarbonyl) group serves as a protective group for the amino functionality, allowing for selective reactions without interfering with other functional groups. This compound features a methionine residue followed by a proline residue, which contributes to its unique structural and steric properties. The presence of the sulfur atom in methionine can influence the peptide's folding and stability, while proline's cyclic structure introduces rigidity. Boc-Met-Pro-OH is typically utilized in the synthesis of peptides and proteins, particularly in solid-phase peptide synthesis, where the protection and deprotection of amino acids are crucial steps. Its solubility in organic solvents and stability under various reaction conditions make it a valuable intermediate in the field of medicinal chemistry and drug development. Proper handling and storage are essential, as with many chemical substances, to maintain its integrity and reactivity.
Formula:C15H26N2O5S
Synonyms:- BOC-MET-PRO-OH
- BOC-L-METHIONYL PROLINE
- (2S)-1-[(2S)-2-[(2-methylpropan-2-yl)oxycarbonylamino]-4-methylsulfanylbutanoyl]pyrrolidine-2-carboxylic acid
- L-Proline, N-[(1,1-dimethylethoxy)carbonyl]-L-methionyl-
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Boc-Met-Pro-OH
CAS:<p>Boc-Met-Pro-OH is a peptide that can be synthesized by condensation of the amino acid methanol with the carboxylic acid proline. This reaction yields Boc-Met-Pro-OH, which can be monitored via thin layer chromatography. The side chain on Boc-Met-Pro-OH is analogous to that of cholecystokinin and this class of peptides are derived from the amide bond. Condensation reactions catalyzed by papain or methyl esters result in the formation of an amide bond between two amino acids. These reactions also produce Boc-Met-Pro-OH because it has an amide bond.</p>Formula:C15H26N2O5SPurity:Min. 95%Molecular weight:346.44 g/mol
