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新型胶原仿生八肽的结构特征及其纳米自组装潜力:实验与理论研究。

Structural Characterization of a New Collagen Biomimetic Octapeptide with Nanoscale Self-Assembly Potential: Experimental and Theoretical Approaches.

机构信息

Faculty of Chemistry, Alexandru Ioan Cuza University of Iasi, 11 Carol I, Iasi, 700506, Romania.

TRANSCEND Research Center, Regional Institute of Oncology, General Henri Mathias, No. 2-4, Iasi, 700483, Romania.

出版信息

Chempluschem. 2022 Feb;87(2):e202100462. doi: 10.1002/cplu.202100462.

DOI:10.1002/cplu.202100462
PMID:35104052
Abstract

Bioinspired peptides are attractive biomolecules which can improve our understanding of self-assembly processes for rational design of new peptide-based materials. Herein, a new amidated peptide FRSAPFIE (FRS), based on a sequence present in human collagen, was synthesized, characterized by mass spectrometry and subjected to self-assembling investigations. The optimal conditions for self-assembly were disclosed by dynamic light scattering at 32 °C and a peptide concentration of 0.51 %. In addition, AFM studies revealed ellipsoidal FRS shapes with an area between 0.8 and 3.1 μm . The ability of self-assembly was also proved using FAD dye as extrinsic fluorescence reporter. According to the theoretical analysis, the FRS peptide tends to form a bundle-type association, with a type of fibrillary tangles particle. Altogether, our findings address new challenges regarding the FRS peptide which can be used in further self-assembly studies to design biocompatible drug-delivery platforms.

摘要

仿生肽是一种有吸引力的生物分子,它可以增进我们对自组装过程的理解,从而实现基于肽的新型材料的合理设计。在此,我们合成了一种新的酰胺化肽 FRSAPFIE(FRS),该肽基于人胶原蛋白中的一个序列,通过质谱进行了表征,并进行了自组装研究。通过在 32°C 和肽浓度为 0.51%的条件下进行动态光散射,揭示了自组装的最佳条件。此外,原子力显微镜研究显示 FRS 形状为椭圆形,面积在 0.8 到 3.1μm 之间。使用 FAD 染料作为外源性荧光报告也证明了自组装的能力。根据理论分析,FRS 肽倾向于形成束状缔合,形成一种纤维缠结颗粒。总之,我们的研究结果为 FRS 肽提出了新的挑战,可用于进一步的自组装研究,以设计生物相容性的药物递送平台。

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