Structure–activity relationship of a novel pentapeptide with cancer cell growth‐inhibitory activity |
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| Authors: | Masakatsu Kamiya Keisuke Oyauchi Yoshinori Sato Takuya Yokoyama Mofei Wang Tomoyasu Aizawa Yasuhiro Kumaki Mineyuki Mizuguchi Kunio Imai Makoto Demura Koichi Suzuki Keiichi Kawano |
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| Affiliation: | 1. Graduate School of Life Science, Hokkaido University, Sapporo 060‐0810, Japan;2. Faculty of Agriculture, Iwate University, Morioka 020‐8550, Japan;3. Graduate School of Science, Hokkaido University, Sapporo 060‐0810, Japan;4. Faculty of Pharmaceutical Sciences, Toyama University, Toyama 093‐0194, Japan;5. Graduate School of Bioresources, Mie University, Tsu 514‐8507, Japan |
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| Abstract: | We previously reported that yamamarin, a pentapeptide with an amidated C‐terminus (DILRG‐NH2) isolated from larvae of the silkmoth, and its palmitoylated analog (C16‐DILRG‐NH2) suppressed proliferation of rat hepatoma (liver cancer) cells. In this study, we investigated the structure–activity relationship of yamamarin by in vitro assay and spectroscopic methods (CD and NMR) for various analogs. The in vitro assay results demonstrated that the chemical structure of the C‐terminal part (‐RG‐NH2) of yamamarin is essential for its activity. The CD and NMR results indicated that yamamarin and its analog adopt predominantly a random coil conformation. Moreover, a comparison of NMR spectra of DILRG‐NH2 and C16‐DILRG‐NH2 revealed that the N‐terminal palmitoyl group of C16‐DILRG‐NH2 did not affect the conformation of the C‐terminal part, which is essential for activity. Together, these results should assist in the design of more sophisticated anticancer drugs. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd. |
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| Keywords: | insect pentapeptide cell growth suppression NMR CD |
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