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Ts-Phe-Gly, also known as Tosyl-Phe-Gly, is a tripeptide consisting of three amino acids: phenylalanine (Phe), glycine (Gly), and a tosyl group (Ts) attached to the N-terminus of phenylalanine. This specific arrangement of amino acids forms a short chain that can be found in various biological processes, such as protein synthesis and peptide signaling. The tosyl group serves as a protecting group for the N-terminus, which is crucial in peptide synthesis to prevent unwanted side reactions. Ts-Phe-Gly is often used as a building block in the synthesis of larger peptides and proteins, and its study contributes to understanding peptide structure, function, and the development of new therapeutic agents.

74075-20-0

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74075-20-0 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 74075-20-0 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 7,4,0,7 and 5 respectively; the second part has 2 digits, 2 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 74075-20:
(7*7)+(6*4)+(5*0)+(4*7)+(3*5)+(2*2)+(1*0)=120
120 % 10 = 0
So 74075-20-0 is a valid CAS Registry Number.

74075-20-0Relevant academic research and scientific papers

Studies on the Alkylation of Dipeptide Substrates

Ager, David J.,Froen, Diane E.,Klix, Russell C.,Zhi, Benxin,McIntosh, John M.,Thangarasa, Rasiah

, p. 1975 - 1982 (2007/10/02)

Alkylation of anions derived from dipeptides with a glycine at the C-terminus have been investigated.A hydrocarbon sedition in the N-terminal residue does impart some asymmetric induction.The use of a chiral ester derivative provides the potential for double asymmetric induction and good selectivity.With an aspartyl residue at the N-terminus, problems were encountered due to competing side reactions.The use of an azetidione could circumvent some of these, but the observed induction was not high.

Synthesis and biological activity of a ketomethylene analogue of a tripeptide inhibitor of angiotensin converting enzyme

Almquist,Chao,Ellis,Johnson

, p. 1392 - 1398 (2007/10/02)

An analogue of a tripeptide inhibitor of angiotensin converting enzyme, Bz-Phe-Gly-Pro, has been synthesized in which the amide bond connecting phenylalanine and glycine has been replaced by a ketomethylene group. This nonpeptide analogue, 20, shows more potent converting enzyme inhibiting activity, I50=0.07 μM, than Bz-Phe-Gly-Pro, I50=9.4 μM, or than the orally active D-3-mercapto-2-methylpropanoyl-L-proline (captopril, 1)I50=0.30 μM. Compound 20 has a K(i)of 1.06 x 10-7 and either competitive or noncompetitive enzyme kinetics depending on what substrate is used in the converting enzyme assay. In tests for inhibition of angiotensin I induced contractions in the guinea pig ileum, 20 has one-tenth the activity of 1.

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