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Title 

Role of amino acid residues within the disulfide loop of thanatin, a potent antibiotic peptide

Authors 

Myung Kyu LeeLina ChaSi Hyung LeeKyung Soo Hahm

Publisher 

Springer Verlag (Germany)

Issue Date 

2002

Citation 

Journal of Biochemistry and Molecular Biology, vol. 35, no. 3, pp. 291-296

Keywords 

amino acidantiinfective agentcyclopeptidedisulfidethanatinamino acid sequencecircular dichroismgram negative bacteriumgram positive bacteriumhuman

Abstract 

Thanatin, a 21-residue peptide, is an inducible insect peptide with a broad range of activity against bacteria and fungi. It has a C-terminal disulfide loop, like the frog skin secretion antimicrobial peptides of the brevinin family. In this study, we tried to find the effect of a number of amino acids between the disulfide bond. Thanatin showed stronger antibacterial activity to Gram negative bacteria than other mutants, except Th1; whereas, the mutant peptides with deletion had higher activity to Gram positive bacteria than thanatin. An increase in the number of amino acid(s) using the alanine residue decreased the antibacterial activity in all of the bacteria. Th1 with deletion of threonine at position 15 (Thr(1)(2)) showed similar antibacterial activity against Gram-negative bacteria, but had higher activity against the Gram positive bacteria. In order to study the structure-function relationship, we measured liposome disruption by the peptides and CD spectra of the peptides. Th1 also showed the highest liposome leaking activity and alpha-helical propensity in the sodium dodecyl sulfate solution, compared with other peptides. Liposome disruption activity was closely correlated with the anti-Gram positive bacterial activity. All of the peptides showed no hemolytic activity. Th1 was considered to be useful as an antimicrobial peptide with broad spectrum without toxicity

ISSN 

1225-8687

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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