Sequence-dependent interactions between model peptides and lipid bilayers

doi:10.1007/s41365-017-0280-1

CORC > 上海应用物理研究所 > 中国科学院上海应用物理研究所 > 中科院上海应用物理研究所2011-2017年

	Sequence-dependent interactions between model peptides and lipid bilayers
	Lei, HZ; Tian, T; Du, QQG; Hu, J; Zhang, Y
刊名	NUCLEAR SCIENCE AND TECHNIQUES
	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
内容类型	期刊论文
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):-.