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Bioorg Med Chem Lett. 2012 Apr 1;22(7):2393-5. doi: 10.1016/j.bmcl.2012.02.037. Epub 2012 Feb 22.

Short cyclic peptides derived from the C-terminal sequence of α1-antitrypsin exhibit significant anti-HIV-1 activity.

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Beijing Institute of Pharmacology & Toxicology, Pharmaceutical Chemistry, 27 Taiping Road, Beijing 100850, China.


Serpin A1 (α1-AT), the largest subgroup of serpins, presents in human plasma at high concentration and plays important regulatory roles in physiological and pathological processes. Accumulated evidence suggests that α1-AT may play a role in controlling HIV-1 infection. In this study, we designed and synthesized a set of short linear peptides derived from the C-terminal sequence of α1-AT. Since none of them showed significant anti-HIV-1 activity, we proceeded to synthesize four short cyclic peptides having 7 amino acids, and we found that three of them exhibited significant anti-HIV-1 activity. One of these cyclic peptides, designated CPM, inhibited HIV-1 entry and infection at low μM level, indicating that these short cyclic peptides could serve as leads for the development of novel anti-HIV-1 therapeutics.

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