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Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Life Science / Faculty of Advanced Life Science >
Peer-reviewed Journal Articles, etc >
Three-Dimensional Structure of the Antimicrobial Peptide Cecropin P1 in Dodecylphosphocholine Micelles and the Role of the C-Terminal Residues
| Title: | Three-Dimensional Structure of the Antimicrobial Peptide Cecropin P1 in Dodecylphosphocholine Micelles and the Role of the C-Terminal Residues |
| Authors: | Gu, Hao Browse this author | | Kato, Takasumi Browse this author | | Kumeta, Hiroyuki Browse this author | | Kumaki, Yasuhiro Browse this author | | Tsukamoto, Takashi Browse this author | | Kikukawa, Takashi Browse this author | | Demura, Makoto Browse this author | | Ishida, Hiroaki Browse this author | | Vogel, Hans J. Browse this author | | Aizawa, Tomoyasu Browse this author →KAKEN DB |
| Issue Date: | 13-Sep-2022 |
| Publisher: | American Chemical Society |
| Journal Title: | ACS Omega |
| Volume: | 7 |
| Issue: | 36 |
| Start Page: | 31924 |
| End Page: | 31934 |
| Publisher DOI: | 10.1021/acsomega.2c02778 |
| Abstract: | Cecropin P1 (CP1) isolated from a large round-worm Ascaris suum, which is found in pig intestines, has been extensively studied as a model antimicrobial peptide (AMP). However, despite being a model AMP, its antibacterial mechanism is not well understood, particularly the function of its C-terminus. By using an Escherichia coli overexpression system with calmodulin as a fusion partner, we succeeded in the mass expression of recombinant peptides, avoiding toxicity to the host and degradation of CP1. The structure of the recombinant N-15-and C-13-labeled CP1 and its C-terminus truncated analogue in dodecylphosphocholine (DPC) micelles was determined by NMR. In this membrane-mimetic environment, CP1 formed an alpha-helix for almost its entire length, except for a short region at the C-terminus, and there was no evidence of a hinge, which is considered important for the expression of activity in other cecropins. Several NMR analyses showed that the entire length of CP1 was protected from water by micelles. Since the loss of the C-terminus of the analogue had little effect on the NMR structure or its interaction with the micelle, we investigated another role of the C-terminus of CP1 in its antimicrobial activity. The results showed that the C-terminal region affected the DNA-binding capacity of CP1, and this mechanism of action was also newly suggested that it contributed to the antimicrobial activity of CP1. |
| Type: | article |
| URI: | http://hdl.handle.net/2115/87401 |
| Appears in Collections: | 生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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