Selected article for: "cleavage site and similar site"
Author: Chew, Miaw-Fang; Poh, Keat-Seong; Poh, Chit-Laa
Title: Peptides as Therapeutic Agents for Dengue Virus
  • Document date: 2017_10_15
    • ID: u1opdwmd_34
    Snippet: In a recent study, several cyclic peptides were designed based on the binding loop of aprotinin which is highly similar to the sequence of the native NS2B-NS3 cleavage site and extends from the P3 to P4' position at the active site of the NS2B-NS3 protease [164] . Results indicated that a peptide, CP7, was able to show good inhibitory property (Ki value of 2.9 µM) against the DENV-3 protease. Similar with the binding of aprotinin to the protease.....
    Document: In a recent study, several cyclic peptides were designed based on the binding loop of aprotinin which is highly similar to the sequence of the native NS2B-NS3 cleavage site and extends from the P3 to P4' position at the active site of the NS2B-NS3 protease [164] . Results indicated that a peptide, CP7, was able to show good inhibitory property (Ki value of 2.9 µM) against the DENV-3 protease. Similar with the binding of aprotinin to the protease, strong hydrogen bonds contributed by the P1 and P2' positions were observed but the inhibitory constant value was not as strong as aprotinin (Ki of 0.026 µM). This might be due to the flexibility of the cyclic peptide which resulted in the decreased affinity against the protease. Nevertheless, this study proved the feasibility of designing inhibitors against both prime and non-prime regions of the protease, and CP7 could act as an alternative candidate for developing a therapeutic against the NS2B-NS3 protease.

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