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タイトル: Affinity selection and sequence-activity relationships of HIV-1 membrane fusion inhibitors directed at the drug-resistant variants
著者: Oishi, Shinya  kyouindb  KAKEN_id
Watanabe, Kentaro
Ito, Saori
Tanaka, Michinori
Nishikawa, Hiroki
Ohno, Hiroaki  kyouindb  KAKEN_id
Shimane, Kazuki
Izumi, Kazuki
Sakagami, Yasuko
Kodama, Eiichi N.
Matsuoka, Masao  KAKEN_id
Asai, Akira
Fujii, Nobutaka  KAKEN_id
著者名の別形: 大石, 真也
発行日: 2010
出版者: Royal Society of Chemistry
誌名: MedChemComm
巻: 1
号: 4
開始ページ: 276
終了ページ: 281
抄録: Enfuvirtide is the first approved membrane fusion inhibitor against HIV-1. Although this drug is effective against multi-drug resistant strains, the emergence of enfuvirtide-resistant strains has been reported in patients who have received an enfuvirtide-containing regimen. Based on the high affinity of synthetic HIV-1 gp41 C-terminal heptad repeat (C-HR) peptides to the counterpart trimeric N-terminal heptad repeat (N-HR) coiled-coil structure, a novel screening approach has been established to facilitate the identification of potent fusion inhibitors against wild-type and enfuvirtide-resistant HIV-1. In this process, affinity selection using histidine-tagged N-HR peptides with the sequences derived from wild-type and resistant strains efficiently captured potent inhibitory peptides from a pool of highly water-soluble C-HR peptides with α-helix-inducible motifs. A highly potent peptide was found from a single amino acid substitution observed in an enfuvirtide-resistant variant as well as peptides with unprecedented modifications at the mutated site.
著作権等: © 2010 Royal Society of Chemistry
許諾条件により本文は2011-07-22に公開.
This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。
URI: http://hdl.handle.net/2433/126711
DOI(出版社版): 10.1039/c0md00091d
出現コレクション:学術雑誌掲載論文等

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