Structure and antibiotic activity of fragment peptides of antifungal protein isolated from Aspergillus giganteus

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Title
Structure and antibiotic activity of fragment peptides of antifungal protein isolated from Aspergillus giganteus
Author(s)
Song Yub Shin; Joo Hyun Kang; Dong Gun Lee; Zhe Zhu Jin; So Youn Jang; Kil Lyong Kim; Kyung Soo Hahm
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 9, no. 3, pp. 276-281
Publication Year
1999
Abstract
In order to determine the functional region of the antifungal protein (AFP) isolated from Aspergillus giganteus responsible for growth inhibitory activity and the promotion of phospholipid vesicle aggregation, overlapping peptides covering the complete sequence of AFP were synthesized. The antibiotic activity against bacterial, fungal, and tumor cells, and the vesicle-aggregation activity of the synthetic peptides were investigated. The AFP functional sequence responsible for antibiotic and vesicle-aggregation activity was determined to be located within the region between AFP residues 19 to 32. AFP (19-32) exhibited an α-helical conformation in a cell membrane-like environment. AFP (19-32) displayed potent antibiotic activity against bacterial, fungal, and tumor cells without peptide toxicity as indicated by hemolysis. Accordingly, AFP (19-32) could be used as a good model for the design of effective antibiotic agents with powerful antibiotic activity yet without any cytotoxic effects against the host organism.
Keyword
Aspergillus giganteusanfifungal proteinfragment peptidesfunctional sequence
ISSN
1017-7825
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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