Two hevein homologs isolated from the seed of Pharbitis nil L. exhibit potent antifungal activity

Ja Choon Koo, So Young Lee, Hyun Jin Chun, Yong Hwa Cheong, Jae Su Choi, Shun Ichiro Kawabata, Masaru Miyagi, Susumu Tsunasawa, Kwon Soo Ha, Dong Won Bae, Chang Deok Han, Bok Luel Lee, Moo Je Cho

研究成果: ジャーナルへの寄稿学術誌査読

125 被引用数 (Scopus)


Two antifungal peptides (Pn-AMP1 and Pn-AMP2) have been purified to homogeneity from seeds of Pharbitis nil. The amino acid sequences of Pn- AMP11 (41 amino acid0 residues) and Pn-AMP2 (40 amino acid residues) were identical except that Pn-AMP1 has an additional serine residue at the carboxyl-terminus. The molecular masses of Pn-AMP1 and Pn-AMP2 were confirmed as 4299.7 and 4213.2 Da, respectively. Both the Pn-AMPs were highly basic (pI 12.02) and had characteristics of cysteine/glycine rich chitin-binding domain. Pn-AMPs exhibited potent antifungal activity against both chitin- containing and non-chitin-containing fungi in the cell wall. Concentrations required for 50% inhibition of fungal growth were ranged from 3 to 26 μg/ml for Pn-AMP1 and from 0.6 to 75 μg/ml for Pn-AMP2. The Pn-AMPs penetrated very rapidly into fungal hyphae and localized at septum and hyphal tips of fungi, which caused burst of hyphal tips. Burst of hyphae resulted in disruption of the fungal membrane and leakage of the cytoplasmic materials to our knowledge, Pn-AMPs are the first herein-like proteins that show similar fungicidal effects as thionins do.

ジャーナルBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
出版ステータス出版済み - 1月 15 1998

!!!All Science Journal Classification (ASJC) codes

  • 構造生物学
  • 生物理学
  • 生化学
  • 分子生物学


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