期刊論文

學年 102
學期 2
出版(發表)日期 2014-04-24
作品名稱 Deletion of the Carboxyl-Terminal Residue Disrupts the Amino-Terminal Folding, Self-Association and Thermal Stability of an Amphipathic Antimicrobial Peptide
作品名稱(其他語言)
著者 李長欣
單位 淡江大學化學學系
出版者
著錄名稱、卷期、頁數 Journal of Peptide Science 20(6), p.438-445
摘要 Understanding the complex relationship between amino acid sequence and protein behaviors, such as folding and self-association, is a major goal of protein research. In the present work, we examined the effects of deleting a C-terminal residue on the intrinsic properties of an amphapathic α-helix of mastoparan-B (MP-B), an antimicrobial peptide with the sequence LKLKSIVSWAKKVL-NH2. We used circular dichroism and nuclear magnetic resonance to demonstrate that the peptide MP-B[1-13] displayed significant unwinding at the N-terminal helix compared with the parent peptide of MP-B, as the temperature increased when the residue at position 14 was deleted. Pulsed-field gradient nuclear magnetic resonance data revealed that MP-B forms a larger diffusion unit than MP-B[1-13] at all experimental temperatures and continuously dissociates as the temperature increases. In contrast, the size of the diffusion unit of MP-B[1-13] is almost independent of temperature. These findings suggest that deleting the flexible, hydrophobic amino acid from the C-terminus of MP-B is sufficient to change the intrinsic helical thermal stability and self-association. This effect is most likely because of the modulation of enthalpic interactions and conformational freedom that are specified by this residue. Our results implicate terminal residues in the biological function of an antimicrobial peptide. Copyright © 2014 European Peptide Society and John Wiley & Sons, Ltd.
關鍵字 antimicrobial peptide;diffusion;enthalpic interaction;self-association;thermal stability
語言 en
ISSN 1075-2617
期刊性質 國內
收錄於 SCI
產學合作
通訊作者
審稿制度
國別 TWN
公開徵稿
出版型式 ,電子版,紙本
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