A comparative study of the solution structures of tachyplesin I and a novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), determined by nuclear magnetic resonance

Hirokazu Tamamura, Masataka Kuroda, Masao Masuda, Akira Otaka, Susumu Funakoshi, Hideki Nakashima, Naoki Yamamoto, Michinori Waki, Akiyoshi Matsumoto, Jean M. Lancelin, Daisuke Kohda, Shinichi Tate, Fuyuhiko Inagaki, Nobutaka Fujii

Research output: Contribution to journalArticle

93 Citations (Scopus)

Abstract

The solution structure of tachyplesin I, which was isolated from membrane acid extracts of the hemocytes from the Japanese horseshoe crab (Tachypleus tridentatus), was determined by nuclear magnetic resonance (NMR) and distance geometry calculation. Tachyplesin I takes an antiparallel β-sheet structure with a type-II β-turn. Recently, among more than 20 synthetic peptides associated with tachyplesin and its isopeptide (polyphemusin), we found that a novel compound, which we designated as T22 ([Tyr5,12, Lys7]-polyphemusin II), strongly inhibited the human immunodeficiency virus (HIV)-1-induced cytopathic effect and viral antigen expression. The solution structure of T22 was investigated using NMR, and its secondary structure was confirmed to be similar to that of tachyplesin I. The anti-parallel β-sheet structure and the several amino-acid side chains on the plane of the β-sheet of T22 are thought to be associated with the expression of anti-HIV activity.

Original languageEnglish
Pages (from-to)209-216
Number of pages8
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume1163
Issue number2
DOIs
Publication statusPublished - May 13 1993
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology

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