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Title 

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

Authors 

Song Yub ShinJoo Hyun KangDong Gun LeeZhe Zhu JinSo Youn JangKil Lyong KimKyung Soo Hahm

Publisher 

The Korean Society for Applied Microbiology

Issue Date 

1999

Citation 

Journal of Microbiology and Biotechnology, vol. 9, no. 3, pp. 276-281

Keywords 

Aspergillus giganteusanfifungal proteinfragment peptidesfunctional sequence

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.

ISSN 

1017-7825

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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