Tuning self-assembly in elastin-derived peptides

被引：22

作者：

Bochicchio, Brigida ^{[1
]}

Pepe, Antonietta ^{[1
]}

Crudele, Maria ^{[1
]}

Belloy, Nicolas ^{[2
,3
]}

Baud, Stephanie ^{[2
,3
]}

Dauchez, Manuel ^{[2
,3
]}

机构：

[1] Univ Basilicata, Dept Sci, I-85100 Potenza, Italy

[2] Univ Reims, UMR CNRS MEDyC 7369, Lab SiRMa, F-51687 Reims 2, France

[3] Univ Reims, Multiscale Mol Modeling Plateform, Fac Sci, F-51687 Reims 2, France

来源：

SOFT MATTER | 2015年 / 11卷 / 17期

关键词：

PROTEIN SECONDARY STRUCTURE; POLYPROLINE-II STRUCTURE; MOLECULAR-DYNAMICS; AMYLOID FIBRILS; GLYCINE-RICH; STRUCTURAL-CHARACTERIZATION; HUMAN TROPOELASTIN; NMR-SPECTROSCOPY; SEQUENCE; AGGREGATION;

D O I：

10.1039/c5sm00072f

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Elastin-derived peptides are gaining increasing interest as potential biomaterials. Previous studies have demonstrated that short elastin-derived peptides are able to self-assemble into fibrils as the entire elastin protein. The motif responsible for that is the XGGZG motif at least three-fold repeated. In this work we have synthesized and studied, at molecular and supramolecular levels, four pentadecapeptides obtained by switching the X and Z residue with leucine and/or valine. We found that the four peptides formed different supramolecular structures corresponding to specific molecular conformations. Our results show that not only the residue type but also the exact position occupied by the residue in the motif is crucial in driving the self-aggregation. The aim of this work is to provide the basis for designing elastin-derived peptides with tunable supramolecular architecture.

引用

页码：3385 / 3395

页数：11

共 46 条

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