A COMPARATIVE-STUDY OF THE SOLUTION STRUCTURES OF TACHYPLESIN-I AND A NOVEL ANTI-HIV SYNTHETIC PEPTIDE, T22 ([TYR(5,12), LYS(7)]-POLYPHEMUSIN-II), DETERMINED BY NUCLEAR-MAGNETIC-RESONANCE

被引:102
作者
TAMAMURA, H
KURODA, M
MASUDA, M
OTAKA, A
FUNAKOSHI, S
NAKASHIMA, H
YAMAMOTO, N
WAKI, M
MATSUMOTO, A
LANCELIN, JM
KOHDA, D
TATE, S
INAGAKI, F
FUJII, N
机构
[1] TOKYO MED & DENT UNIV, SCH MED, DEPT MICROBIOL, TOKYO 113, JAPAN
[2] SEIKAGAKU CORP, TOKYO, JAPAN
[3] TOKYO METROPOLITAN INST MED SCI, DEPT MOLEC PHYSIOL, TOKYO 113, JAPAN
关键词
TACHYPLESIN-I; POLYPHEMUSIN-II; NMR; H-1; ANTI-HIV PEPTIDE; DISTANCE GEOMETRY; (XPLOR);
D O I
10.1016/0167-4838(93)90183-R
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 beta-sheet structure with a type-II beta-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 beta-sheet structure and the several amino-acid side chains on the plane of the beta-sheet of T22 are thought to be associated with the expression of anti-HIV activity.
引用
收藏
页码:209 / 216
页数:8
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