Quantitative assessment of peptide-lipid interactions. Ubiquitous fluorescence methodologies

被引:62
作者
Matos, Pedro M. [1 ]
Franquelim, Henri G. [1 ]
Castanho, Miguel A. R. B. [1 ]
Santos, Nuno C. [1 ]
机构
[1] Univ Lisbon, Inst Mol Med, Fac Med, P-1649028 Lisbon, Portugal
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2010年 / 1798卷 / 11期
关键词
Peptide; Protein; Lipid; Membrane; Fluorescence; Partition; MODEL SYSTEMS; MEMBRANE INSERTION; BINDING; PROTEIN; RECEPTOR; TIME; PROBES; ORIENTATION; VESICLES; BILAYERS;
D O I
10.1016/j.bbamem.2010.07.012
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
Peptide-membrane interactions have been gaining increased relevance, mainly in biomedical investigation, as the potential of the natural, nature-based and synthetic peptides as new drugs or drug candidates also expands. These peptides must face the cell membrane when they interfere with or participate in intracellular processes. Additionally, several peptide drugs and drug leads actions occur at the membrane level (e.g., antimicrobial peptides, cell-penetrating peptides and enveloped viruses membrane fusion inhibitors). Here we explore fluorescence spectroscopy methods that can be used to monitor such interactions. Two main approaches are considered, centered either on the peptide or on the membrane. On the first, we consider mainly the methodologies based on the intrinsic fluorescence of the aminoacid residues tryptophan and tyrosine. Regarding membrane-centric approaches, we review methods based on lipophilic probes sensitive to membrane potentials. The use of fluorescence constitutes a simple and sensitive method to measure these events. Unraveling the molecular mechanisms that govern these interactions can unlock the key to understand specific biological processes involving natural peptides or to optimize the action of a peptide drug. (C) 2010 Elsevier B.V. All rights reserved.
引用
收藏
页码:1999 / 2012
页数:14
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