Two novel antifungal peptides distinct with a five‐disulfide motif from the bark of Eucommia ulmoides Oliv

FEBS Letters

Hu, Zhong²  Wang, Da-Cheng¹  Liu, Xiao-Zhu²  Zhang, Ying¹  Xiang, Ye¹  Huang, Ren-Huai¹ 

[1]Center for Molecular Biology, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Raod, Chaoyang District, Beijing 100101, PR China

[2]Kunming Institute of Botany, Chinese Academy of Sciences, Kunming 650204, PR China

关键词: Antifungal peptide;    Amino acid sequence;    Disulfide motif;    Eucommia ulmoides Oliv;    EAFP;    Eucommia antifungal peptide;    MALDI-TOF;    matrix-assisted laser desorption ionization-time of flight;    HPLC;    high performance liquid chromatography;    PD;    potato dextrose;    CHCA;    α-cyano-4-hydroxycinnamic acid;    CPY;    carboxypeptidase Y;    CAM;    carboxyamidomethyl;   

DOI  :  10.1016/S0014-5793(02)02829-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Two antifungal peptides, named EAFP1 and EAFP2, have been purified from the bark of Eucommia ulmoides Oliv. Each of the sequences consists of 41 residues with a N-terminal blockage by pyroglutamic acid determined by automated Edman degradation in combination with the tandem mass spectroscopy and the C-terminal ladder sequencing analysis. The primary structurs all contain 10 cysteines, which are cross-linked to form five disulfide bridges with a pairing pattern (C1–C5, C2–C9, C3–C6, C4–C7, C8–C10). This is the first finding of a plant antifungal peptide with a five-disulfide motif. EAFP1 and EAFP2 show characteristics of hevein domain and exhibit chitin-binding properties similar to the previously identified hevein-like peptides. They exhibit relatively broad spectra of antifungal activities against eight pathogenic fungi from cotton, wheat, potato, tomato and tobacco. The inhibition activity of EAFP1 and EAFP2 can be effective on both chitin-containing and chitin-free fungi. The values of IC₅₀ range from 35 to 155 μg/ml for EAFP1 and 18 to 109 μg/ml for EAFP2. Their antifungal effects are strongly antagonized by calcium ions.

【 授权许可】

Unknown