Hydrogelation of self-assembling RGD-based peptides

被引：108

作者：

Cheng, G. ^{[1
]}

Castelletto, V. ^{[1
]}

Jones, R. R. ^{[1
]}

Connon, C. J. ^{[1
]}

Hamley, I. W. ^{[1
,2
]}

机构：

[1] Univ Reading, Sch Chem Pharm & Food Biosci, Reading RG6 6AD, Berks, England

[2] Diamond Light Source, Didcot OX11 0DE, Oxon, England

来源：

SOFT MATTER | 2011年 / 7卷 / 04期

基金：

英国工程与自然科学研究理事会;

关键词：

AMYLOID-BETA-PEPTIDE; REVERSED HYDROLYSIS; IN-VITRO; BIOMATERIALS; DIPEPTIDES; SCAFFOLDS; FRAGMENT; ADHESION; ACID;

D O I：

10.1039/c0sm00408a

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070305 [高分子化学与物理];

摘要：

The self-assembly of tripeptides based on the RGD cell adhesion motif is investigated. Two tripeptides containing the Fmoc [N-(fluorenyl)-9-methoxycarbonyl] aromatic unit were synthesized, Fmoc-RGD and a control peptide containing a scrambled sequence, Fmoc-GRD. The Fmoc is used to control self-assembly via aromatic stacking interactions. The self-assembly and hydrogelation properties of the two Fmoc-tripeptides are compared. Both form well defined amyloid fibrils (as shown by cryo-TEM and SAXS) with beta-sheet features in their circular dichroism and FTIR spectra. Both peptides form self-supporting hydrogels, the dynamic shear modulus of which was measured. Preliminary cell culture experiments reveal that Fmoc-RGD can be used as a support for bovine fibroblasts, but not Fmoc-GRD, consistent with the incorporation of the cell adhesion motif in the former peptide.

引用

页码：1326 / 1333

页数：8

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