103424-73-3

Basic information

• Product Name: tyr-ala-gly-ala-val-val-asn-asp-leu
• CAS NO: 103424-73-3
• Molecular Formula: C₄₁H₆₄N₁₀O₁₄
• Molecular Weight: 921.01
• Mol File: 103424-73-3.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: tyr-ala-gly-ala-val-val-asn-asp-leu(CAS DataBase Reference)
• NIST Chemistry Reference: tyr-ala-gly-ala-val-val-asn-asp-leu(103424-73-3)
• EPA Substance Registry System: tyr-ala-gly-ala-val-val-asn-asp-leu(103424-73-3)

Safety Data

• Hazardous Substances Data: 103424-73-3(Hazardous Substances Data)

Upstream product

• 4530-20-5 BOC-glycine 
• 13734-41-3 t-Boc-L-valine 
• 15761-38-3 L-N-Boc-Ala 
• 47689-67-8 (S)-3-[4-(2-Bromo-benzyloxycarbonyloxy)-phenyl]-2-tert-butoxycarbonylamino-propionic acid 

Relevant articles and documents

Synthesis and Inhibitory Potency of Peptides Corresponding to the Subunit 2 C-Terminal Region of Herpes Virus Ribonucleotide Reductases

H-Tyr239-Ala330-Gly331-Ala332-Val333-Val334-Asn335-Asp336-Leu337-OH, the C-terminal end of herpes simplex virus ribonucleotide reductase subunit 2 (HSV R2), specifically inhibits viral enzyme activity by interacting with subunit 1 (HSV R1).In a previous structure-activity study, we identified four sites on the nonapeptide where the inhibitory potency could be modulated: a minimum active core 333-337, a spacer segment 330-332, and the N- and C-termini.To further explore the structural features of HSV R2-(329-337) that are required to obtain a potent inhibition, a series of analogues comprising modifications in these four regions were synthesized by solid-phase methodology.Changes in the segment 333-337 of the molecule decreased the inhibitory potency by more than 2-fold, except for the Ile334 substitution, which resulted in a 1.5-fold increase in potency.Replecement of Tyr329 by other aromatic or aliphatic amino acids diminished the nonapeptide activity from 1.4-fold to 5.9-fold.The spacer segment contributed to enhance potency.Modification with amino acids that could induce conformational changes, such as Pro or D-Ala, generated compounds with a similar or lower activity, respectively.Amidation or amino acyl addition at the carboxylic end was detrimental while acylation of the N-terminus was generally beneficial for the inhibitory potency.Disubstitution in position 332 and 334 by Thr and Ile, which are present in the C-terminal portion of varicella-zoster virus ribonucleotide reductase subunit 2, resulted in a peptide that is 4.0 times more potent than HSV R2-(329-337), while each monosubstitution alone generated peptides with 150percent of the activity of HSV R2-(329-337) nonapeptide.These results indicate a synergistic effect of the disubstitution which confers to this analogue physicochemical properties enhancing its ability to interact with its R1 binding site.