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Isolation and structure of a novel peptide inhibitor of HIV-1 integrase from marine polychaetes

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Abstract

A homogeneous peptide with a mass of 683 Da which inhibits HIV-1 integrase with IC50 3 × 10−5 M was separated from aqueous extracts of a marine worm Eunicidae sp. by multistage chromatography purification. The Asp-Leu-Hse-His-Ala-Gln structure was proposed for this peptide according to amino acid analysis, automated amino acid Edman sequences, and TLC with witness homoserine and MS/MS fragmentation. The proposed structure is the first example of a natural peptide containing an amino acid homoserine residue.

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Abbreviations

IA:

inhibitory activity

IN:

integrase of HIV-1

RT:

reverse transcriptase of HIV-1

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Correspondence to L. A. Elyakova.

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Original Russian Text © L.A. Elyakova, B.V. Vaskovsky, N.I. Khoroshilova, S.I. Vantseva, Yu.Yu. Agapkina, 2011, published in Bioorganicheskaya Khimiya, 2011, Vol. 37, No. 2, pp. 233–243.

The material of the present article was presented in a brief at the International Scientific Conference on Bioorganic Chemistry, in memoriam of academician Yu.A. Ovchinnikov [1].

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Elyakova, L.A., Vaskovsky, B.V., Khoroshilova, N.I. et al. Isolation and structure of a novel peptide inhibitor of HIV-1 integrase from marine polychaetes. Russ J Bioorg Chem 37, 207–216 (2011). https://doi.org/10.1134/S1068162010061019

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  • DOI: https://doi.org/10.1134/S1068162010061019

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