Peptide-induced bilayer thinning structure of unilamellar vesicles and the related binding behavior as revealed by X-ray scattering

Please use this identifier to cite or link to this item: https://ir.lib.ncu.edu.tw/handle/987654321/105566

Title:	Peptide-induced bilayer thinning structure of unilamellar vesicles and the related binding behavior as revealed by X-ray scattering
Authors:	李明道;Su, Chun-Jen;Wu, Shiuan-Shiaou;Jeng, U-Ser;Lee, Ming-Tao;Su, An-Chung;Liao, Kuei-Fen;Lin, Wei-Yu;Huang, Yu-Shan;Chen, Chun-Yu
Contributors:	理學院物理學系
Keywords:	Alamethicin - chemistry;Biophysics - methods;Fourier Analysis;Lipid Bilayers - chemistry;Melitten - chemistry;Membrane;Models, Statistical;Peptide;Peptides - chemistry;Protein Binding;Scattering, Radiation;Scattering, Small Angle;Thermodynamics;Unilamellar Liposomes - chemistry;Vesicle;Water - chemistry;X-Ray Diffraction - methods;X-ray scattering;X-Rays
Date:	2013-02-01
Issue Date:	2026-04-23 12:37:23 (UTC+8)
Publisher:	Elsevier;Netherlands: Elsevier B.V
Abstract:	摘要： We have studied the bilayer thinning structure of unilamellar vesicles (ULV) of a phospholipid 1,2-dierucoyl-sn-glycero-3-phosphocholine (di22:1PC) upon binding of melittin, a water-soluble amphipathic peptide. Successive thinning of the ULV bilayers with increasing peptide concentration was monitored via small-angle X-ray scattering (SAXS). Results suggest that the two leaflets of the ULV of closed bilayers are perturbed and thinned asymmetrically upon free peptide binding, in contrast to the centro-symmetric bilayer thinning of the substrate-oriented multilamellar membranes (MLM) with premixed melittin. Moreover, thinning of the melittin-ULV bilayer associates closely with peptide concentration in solution and saturates at ~4%, compared to the ~8% maximum thinning observed for the correspondingly premixed peptide-MLM bilayers. Linearly scaling the thinning of peptide-ULV bilayers to that of the corresponding peptide-MLM of a calibrated peptide-to-lipid ratio, we have deduced the number of bound peptides on the ULV bilayers as a function of free peptide concentration in solution. The hence derived X-ray-based binding isotherm allows extraction of a low binding constant of melittin to the ULV bilayers, on the basis of surface partition equilibrium and the Gouy–Chapman theory. Moreover, we show that the ULV and MLM bilayers of di22:1PC share a same thinning constant upon binding of a hydrophobic peptide alamethicin; this result supports the linear scaling approach used in the melittin-ULV bilayer thinning for thermodynamic binding parameters of water-soluble peptides. Bilayer thinning behaviors for the melittin-bound, free-floating unilamellar vesicles and the substrate-oriented multilamellar membranes of zwitterionic phospholipids. [Display omitted] ► Peptide-induced asymmetric bilayer thinning behavior is revealed. ► Small-angle X-ray scattering and X-ray diffraction results are integrated. ► Articulating the membrane thinning structure with peptide binding affinity. ► ULV and MLM bilayers share a same bilayer thinning constant. 其他題名： Biochim Biophys Acta 出版者： Netherlands: Elsevier B.V 出版日期： 2013-02 出處： Biochimica et biophysica acta, 2013-02, Vol.1828 (2), p.528-534 資源來源： Elsevier ScienceDirect Journals Complete 版權： 2012 Elsevier B.V. 版權： Copyright © 2012 Elsevier B.V. All rights reserved. 識別號： ISSN: 0005-2736 識別號： ISSN: 0006-3002 識別號： EISSN: 1879-2642 識別號： DOI: 10.1016/j.bbamem.2012.10.027 識別號： PMID: 23123565
Appears in Collections:	[Department of Physics] journal & Dissertation

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