|
|||||
|
|
Molecular scaffold of a new pokeweed antifungal peptide deduced by H nuclear magnetic resonance |
|
| Authors: | Guang-Hua Gao Wei Liu Ji-Xun Dai Jin-Feng Wang Zhong Hu Ying Zhang Da-Cheng Wang |
| Affiliation: | a Laboratory of Molecular Biophysics, Institute of Biophysics, Chinese Academy of Science, 15 Datun Road, Chaoyang District, Beijing 100101, People's Republic of China b National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Science, 15 Datun Road, Chaoyang District, Beijing 100101, People's Republic of China c Kunming Institute of Botany, Chinese Academy of Sciences, Kunming 650204, People's Republic of China |
| Abstract: | The antifungal peptide from seeds of Phytolacca Americana (Pokeweed), designated PAFP-S hereinafter, is a recently found cationic peptide which consists of 38 amino acid residues and exihibites a broad spectrum of antifungal activity, including inhibition of certain saprophytic fungi and some plant pathogens. The secondary structure and three cysteine pairings have been investigated by 1H NMR analysis. The results show that the molecular scaffold of PAFP-S features a triple-stranded antiparallel β-sheet knotted by a typical disulfide bridge motif, which characterizes the knottin fold. CD spectroscopy indicates a high stability of the molecule in solution. Therefore, PAFP-S should be a new member of the knottin structural family and the first antifungal peptide that adopts the knottin-like fold. |
| Keywords: | Antifungal peptide Secondary structure Cysteine pairing Knottin-like peptide |
| 本文献已被 ScienceDirect 等数据库收录！ | |