Dimerization effects on coacervation property of an elastin-derived synthetic peptide (FPGVG)5
Dimerization effects on coacervation property of an elastin-derived synthetic peptide (FPGVG)5
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二聚化对弹性蛋白衍生合成肽 (FPGVG) 凝聚特性的影响5
DOI：
10.1002/psc.2876
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发表时间：
2016
影响因子：
2.1
通讯作者：
Takeru Nose
中科院分区：
文献类型：
--
作者：
Keitaro Suyama;Suguru Taniguchi;Daiki Tatsubo;Iori Maeda;Takeru Nose
弹性蛋白是弹性纤维的核心蛋白，在生理条件下表现为凝聚（温度依赖性可逆结合/解离）。由于这一特性，弹性蛋白和弹性蛋白衍生肽被认为是开发各种生物医学产品、皮肤替代品、合成血管移植物和药物输送系统的有用基础材料。虽然弹性蛋白衍生的多肽（Val‐Pro‐Gly‐Val‐Gly） n也已被证明具有凝聚特性，但需要足够高的（VPGVG）重复数（n> 40）才能实现凝聚。在本研究中，新开发了一系列弹性蛋白衍生肽（Phe‐Pro‐Gly‐Val‐Gly）5二聚体，具有较高的聚势。与常用的弹性蛋白衍生肽类似物相比，这些新型二聚肽在明显较低的浓度和温度下表现出聚集性；这一结果表明，二聚化可以增强肽的凝聚能力。圆二色性（CD）测量表明，当共聚时，二聚体经历了类似的温度依赖性和可逆构象变化。分子动力学计算结果表明，sheet - turn - sheet基序涉及在二聚体中常见的II型β - turn - like结构，并导致它们形成球状构象。这些合成的肽二聚体不仅可以作为弹性蛋白和弹性蛋白衍生肽结构分析的模型肽，而且可以作为开发各种温度敏感生物医学和工业产品的基础材料。版权所有©2016欧洲多肽协会和约翰威利父子有限公司
Elastin, a core protein of the elastic fibers, exhibits the coacervation (temperature‐dependent reversible association/dissociation) under physiological conditions. Because of this characteristic, elastin and elastin‐derived peptides have been considered to be useful as base materials for developing various biomedical products, skin substitutes, synthetic vascular grafts, and drug delivery systems. Although elastin‐derived polypeptide (Val‐Pro‐Gly‐Val‐Gly)nalso has been known to demonstrate coacervation property, a sufficiently high (VPGVG)nrepetition number (n> 40) is required for coacervation. In the present study, a series of elastin‐derived peptide (Phe‐Pro‐Gly‐Val‐Gly)5dimers possessing high coacervation potential were newly developed. These novel dimeric peptides exhibited coacervation at significantly lower concentrations and temperatures than the commonly used elastin‐derived peptide analogs; this result suggests that the coacervation ability of the peptides is enhanced by dimerization. Circular dichroism (CD) measurements indicate that the dimers undergo similar temperature‐dependent and reversible conformational changes when coacervation occurs. The molecular dynamics calculation results reveal that the sheet‐turn‐sheet motif involving a type II β‐turn‐like structure commonly observed among the dimers and caused formation of globular conformation of them. These synthesized peptide dimers may be useful not only as model peptides for structural analysis of elastin and elastin‐derived peptides, but also as base materials for developing various temperature‐sensitive biomedical and industrial products. Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd.