VV-hemorphin-5 association to lipid bilayers and alterations of membrane bending rigidity

IF 1.1 Q4 BIOPHYSICS AIMS Biophysics Pub Date : 2022-01-01 DOI:10.3934/biophy.2022025
I. Valkova, P. Todorov, V. Vitkova
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引用次数: 1

Abstract

The morphinomimetic properties of hemorphins are intensively studied with regard to new peptide drug developments. In this respect, the investigation of mechanical properties and stability of lipid membranes provides a useful background for advancement in pharmacological applications of liposomes. Here we probed the effect of the endogenous heptapeptide VV-hemorphin-5 (valorphin) on the bending elasticity of biomimetic lipid membranes of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) by analysis of thermal shape fluctuations of nearly spherical giant unilamellar vesicles. In a wide concentration range covering valorphin concentrations applied in nociceptive screening in vivo, we report alterations of the bilayer bending rigidity in a concentration-dependent non-monotonic manner. We performed quantitative characterization of VV-hemorphin-5 association to POPC membranes by isothermal titration calorimetry in order to shed light on the partitioning of the amphiphilic hemorphin between the aqueous solution and membranes. The calorimetric results correlate with flicker spectroscopy findings and support the hypothesis about the strength of valorphin-membrane interaction related to the peptide bulk concentration. A higher strength of valorphin interaction with the bilayer corresponds to a more pronounced effect of the peptide on the membrane's mechanical properties. The presented study features the comprehensive analysis of membrane bending elasticity as a biomarker for physicochemical effects of peptides on lipid bilayers. The reported data on thermodynamic parameters of valorphin interactions with phosphatidylcholine bilayers and alterations of their mechanical properties is expected to be useful for applications of lipid membrane systems in pharmacology and biomedicine.
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VV-hemorphin-5与脂质双分子层的关联及膜弯曲刚度的改变
关于新的多肽药物开发,hemorphin的拟吗啡特性被深入研究。在这方面,脂质膜的力学性质和稳定性的研究为脂质体的药理应用提供了有益的背景。本文通过分析近球形巨型单层囊泡的热形态波动,探讨内源性七肽VV-hemorphin-5 (valorphin)对1-棕榈酰-2-油酰- snn -甘油-3-磷脂胆碱(POPC)仿生脂膜弯曲弹性的影响。在广泛的浓度范围内,包括用于体内伤害性筛选的valorphin浓度,我们报告了以浓度依赖的非单调方式改变的双层弯曲刚度。我们通过等温滴定量热法对VV-hemorphin-5与POPC膜的关联进行了定量表征,以阐明两亲性hemorphin在水溶液和膜之间的分配。量热分析结果与闪烁光谱分析结果相一致,并支持了有关肽体积浓度与valorphin-membrane相互作用强度有关的假设。valorphin与双分子层相互作用的强度越高,对应于肽对膜的机械性能的更显著的影响。本研究的特点是全面分析膜弯曲弹性作为多肽对脂质双分子层的物理化学作用的生物标志物。本文所报道的valorphin与磷脂酰胆碱双分子层相互作用的热力学参数及其力学性能的变化,有望为脂质膜系统在药理学和生物医学上的应用提供有用的数据。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
AIMS Biophysics
AIMS Biophysics BIOPHYSICS-
CiteScore
2.40
自引率
20.00%
发文量
16
审稿时长
8 weeks
期刊介绍: AIMS Biophysics is an international Open Access journal devoted to publishing peer-reviewed, high quality, original papers in the field of biophysics. We publish the following article types: original research articles, reviews, editorials, letters, and conference reports. AIMS Biophysics welcomes, but not limited to, the papers from the following topics: · Structural biology · Biophysical technology · Bioenergetics · Membrane biophysics · Cellular Biophysics · Electrophysiology · Neuro-Biophysics · Biomechanics · Systems biology
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