Conformational changes of pediocin in an aqueous medium monitored by Fourier transform infrared spectroscopy: a biological implication

被引:13
作者
Gaussier, H
Lavoie, M
Subirade, M
机构
[1] Univ Laval, Dept Aliments & Nutr, Chaire Rech Canada Prot & Ailments Fonctionnels, Ctr Rech Stela, St Foy, PQ G1K 7P4, Canada
[2] Univ Laval, Inst Nutraceut & Ailments Fonctionnels, St Foy, PQ G1K 7P4, Canada
[3] Univ Laval, Fac Sci & Gen, Dept Biochim & Microbiol, St Foy, PQ G1K 7P4, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
pediocin PA-1; Fourier transform infrared spectroscopy; structure-activity relationship;
D O I
10.1016/S0141-8130(03)00018-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Fourier transform infrared (FTIR) spectroscopy was used to investigate the secondary structure of pediocin PA-1 in different aqueous media in relation to its antimicrobial activity. The experiments were performed at pD (pH meter corrected for deuterium isotope effect) 6, 7, and 8 and during a heating-cooling cycle of 20-80degreesC. At pD 6, (i.e. pediocin's most active form), the FTIR results show that pediocin adopts an unordered structure with a small contribution of p-turn. After a heating-cooling cycle, thermally-induced changes in pediocin are reversed and its activity is maintained. Increasing the pD to 7 and 8 leads to a more ordered secondary structure. For these two pD values, an increase in temperature induces an irreversible aggregation of protein as revealed by the amide F band. The analysis of the Tyr region provides more insight into the aggregation process. In fact, it appears to be a two-step process, involving first the C (carboxy)-terminus of pediocin and then the N (amino)-terminus. This study reveals two major points: (1) the preservation of pediocin flexibility is essential for maintaining its activity; and (2) the aggregation of its C-terminus is sufficient to induce a loss of activity, suggesting that this region plays an important role in the activity of pediocin. (C) 2003 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:1 / 9
页数:9
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