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Z-D-Ala-gPhe-Gly-COH is a synthetic pentapeptide, a chain of five amino acids, with the sequence Z-D-alanine, gamma-phenylalanine, glycine, and a terminal carboxylic acid group. This specific sequence is of interest in the field of chemistry and pharmacology due to its potential applications. The "Z" group is a protecting group used in peptide synthesis to prevent unwanted reactions until the desired peptide bond formation occurs. The D-alanine indicates that the alanine amino acid is in its D-configuration, which is the non-natural isomer and is often used in the synthesis of certain antibiotics. The gamma-phenylalanine is a non-natural amino acid with a cyclized structure, which can confer unique properties to the peptide. The glycine is a simple amino acid that often provides flexibility in peptide structures. The terminal carboxylic acid group is essential for further reactions or for the peptide to interact with biological targets. This particular sequence may be studied for its ability to mimic or modulate the activity of natural peptides, potentially leading to therapeutic applications.

95617-55-3

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95617-55-3 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 95617-55-3 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 9,5,6,1 and 7 respectively; the second part has 2 digits, 5 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 95617-55:
(7*9)+(6*5)+(5*6)+(4*1)+(3*7)+(2*5)+(1*5)=163
163 % 10 = 3
So 95617-55-3 is a valid CAS Registry Number.

95617-55-3Downstream Products

95617-55-3Relevant academic research and scientific papers

Synthesis and Pharmacological Activity of Partially Modified Retro-Inverso Dermorphin Tetrapeptides

Salvadori, Severo,Marastoni, Mauro,Balboni, Gianfranco,Sarto, Gian Pietro,Tomatis, Roberto

, p. 769 - 774 (2007/10/02)

We studied the effect of partial retro-inverso modification of selected peptide bonds of N-terminal tetrapeptide analogues of dermorphin (H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2).Among the 14 compounds synthesized and tested for opioid activity, some tetrapeptides have the C-terminus carrying different amide moieties; retromodifications concern the Phe-Gly bond (Ia-f) and/or the C-terminal carboxamide function (IIIa-d, IIa-d).All pseudotetrapeptide derivatives showed opioid activity in vitro and in vivo.The most potent compounds (II) have a biological potency comparable with that of the original tetrapeptides in the guinea pig ileum preparation and in the mouse tail-flick test after intracerebral or subcutaneous administration.

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