Indolactam-V Is Involved in the CH/ Interaction with Pro-11 of the PKC
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- 作者：Yu Nakagawa ; Kazuhiro Irie ; Ryo C. Yanagita ; Hajime Ohigashi ; and Ken-ichiro Tsuda
- 刊名：Journal of the American Chemical Society
- 出版年：2005
- 出版时间：April 27, 2005
- 年：2005
- 卷：127
- 期：16
- 页码：5746 - 5747
- 全文大小：80K
- 年卷期：v.127,no.16(April 27, 2005)
- ISSN：1520-5126
文摘
The CH/
interaction between the indole ring of indolactam-V (IL-V) and the hydrogen atom at position 4 of Pro-11 of the PKC
C1B domain was evaluated using the mutant peptide of the PKC C1B domain, in which the CH/ interaction was inhibited by substitution of the hydrogen atom with a fluorine atom. IL-V showed about a 10 times lower binding affinity to the mutant peptide compared to the wild-type peptide, suggesting that the CH/ interaction could play a pivotal role in the binding of IL-V to the PKC C1B domain. On the other hand, benzolactam-V8 (BL-V8), with the benzene ring instead of the indole ring of IL-V, might lack the CH/ interaction. The low binding affinity of BL-V8 could be enhanced by the effective formation of the CH/ interaction as exemplified by the synthesis of naphtholactam-V8 (NL-V8).
interaction between the indole ring of indolactam-V (IL-V) and the hydrogen atom at position 4 of Pro-11 of the PKC C1B domain was evaluated using the mutant peptide of the PKC C1B domain, in which the CH/ interaction was inhibited by substitution of the hydrogen atom with a fluorine atom. IL-V showed about a 10 times lower binding affinity to the mutant peptide compared to the wild-type peptide, suggesting that the CH/ interaction could play a pivotal role in the binding of IL-V to the PKC C1B domain. On the other hand, benzolactam-V8 (BL-V8), with the benzene ring instead of the indole ring of IL-V, might lack the CH/ interaction. The low binding affinity of BL-V8 could be enhanced by the effective formation of the CH/ interaction as exemplified by the synthesis of naphtholactam-V8 (NL-V8).