Sequence-dependent interactions between model peptides and lipid bilayers
文献类型：期刊论文
| 作者 | Lei, HZ; Tian, T; Du, QQG; Hu, J; Zhang, Y |
| 刊名 | NUCLEAR SCIENCE AND TECHNIQUES
 |
| 出版日期 | 2017 |
| 卷号 | 28期号:9页码:- |
| 关键词 | Atomic-force Microscopy Protein Misfolding Diseases Amyloid-like Peptides Beta-sheet Tapes Membrane Interactions Ion Channels Aggregation Afm Specificity Interfaces |
| ISSN号 | 1001-8042 |
| DOI | 10.1007/s41365-017-0280-1 |
| 文献子类 | 期刊论文 |
| 英文摘要 | Studying interaction between peptides and lipid membranes is helpful for understanding the working mechanism of amyloidogenic peptides and antimicrobial peptides, which are toxic to cells through disruption of the cell membrane. Although many efforts have been made to find out common mechanisms of the peptide-induced membrane disruption, detailed information on how the peptide's amino acid sequence affects its interaction with lipid bilayers is still lacking. In this study, three peptides termed as Pep11, P11-2, and QQ11, which share a similar backbone, were employed to explore how modifications on the peptide sequence as well as terminal groups influenced its interaction with the lipid membrane. Atomic force microscopy data revealed that the peptides could deposit on the membranes and induce defects with varied morphologies and stiffness. Fluorescence resonance energy transfer (FRET) experiments indicated that the introduction of the three peptides resulted in different FRET effects on either liquid or gel lipid membranes. DPH fluorescence anisotropy and Laurdan's generalized polarization analysis showed that P11-2 could insert into the lipid membrane and impact the lipid hydrophobic region while QQ11 influenced the order of the hydrophilic head of the lipid membrane. With these results, we have illustrated how these peptides interacted differently with the lipid membrane because of the modification of their sequences. Although these peptides did not relate to disease and antibiosis, we hope these results still could provide some clues for partly understanding the working mechanism of amyloidogenic peptides and antimicrobial peptides. |
| WOS关键词 | ATOMIC-FORCE MICROSCOPY ; PROTEIN MISFOLDING DISEASES ; AMYLOID-LIKE PEPTIDES ; BETA-SHEET TAPES ; MEMBRANE INTERACTIONS ; ION CHANNELS ; AGGREGATION ; AFM ; SPECIFICITY ; INTERFACES |
| 语种 | 英语 |
| WOS记录号 | WOS:000408853800005 |
| 源URL | [http://ir.sinap.ac.cn/handle/331007/28813]  |
| 专题 | 上海应用物理研究所_中科院上海应用物理研究所2011-2017年 |
| 推荐引用方式 GB/T 7714 | Lei, HZ,Tian, T,Du, QQG,et al. Sequence-dependent interactions between model peptides and lipid bilayers[J]. NUCLEAR SCIENCE AND TECHNIQUES,2017,28(9):-. |
| APA | Lei, HZ,Tian, T,Du, QQG,Hu, J,&Zhang, Y.(2017).Sequence-dependent interactions between model peptides and lipid bilayers.NUCLEAR SCIENCE AND TECHNIQUES,28(9),-. |
| MLA | Lei, HZ,et al."Sequence-dependent interactions between model peptides and lipid bilayers".NUCLEAR SCIENCE AND TECHNIQUES 28.9(2017):-. |
入库方式： OAI收割
来源：上海应用物理研究所
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。