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Increased anti‐HIV‐1 activity of CD4 CDR3‐related synthetic peptides by scrambling and further structural modifications, including d ‐isomerization and dimerization
Author(s) -
Kumagai Kazuo,
Tokunaga Kenzo,
Tsutsumi Masahiro,
Ikuta Kazuyoshi
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80255-s
Subject(s) - dimer , chemistry , peptide , circular dichroism , stereochemistry , isomerization , human immunodeficiency virus (hiv) , syncytium , scrambling , sequence (biology) , peptide sequence , structure–activity relationship , biochemistry , in vitro , biology , virology , cell , gene , linguistics , philosophy , organic chemistry , catalysis
We recently showed that S1, a sequence‐scrambled form of CD4 CDR3‐related synthetic peptide, has more potent inhibitory activities on HIV‐1 replication and HIV‐1‐induced syncytium formation than the original form. In this study, a series of derivatives of S1 were synthesized and their anti‐HIV‐1 activities were evaluated. A d ‐isomer was as potent as S1, and a homodimer was 10‐ to 18‐fold more potent than S1. The increased antiviral activity of the dimer peptide was related to α‐helix formation, as detected by circular dichroism.

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