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Functionalised amyloid fibrils for roles in cell adhesion

Gras, S.L., Tickler, A.K., Squires, A.M., Devlin, G.L., Horton, M.A., Dobson, C.M. and MacPhee, C.E. (2008) Functionalised amyloid fibrils for roles in cell adhesion. Biomaterials, 29 (11). pp. 1553-1562. ISSN 0142-9612

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To link to this article DOI: 10.1016/j.biomaterials.2007.11.028

Abstract/Summary

We describe experiments designed to explore the possibility of using amyloid fibrils as new nanoscale biomaterials for promoting and exploiting cell adhesion, migration and differentiation in vitro. We created peptides that add the biological cell adhesion sequence (RGD) or a control sequence (RAD) to the C-terminus of an 11-residue peptide corresponding to residues 105-115 of the amyloidogenic protein transthyretin. These peptides readily self-assemble in aqueous solution to form amyloid fibrils, and X-ray fibre diffraction shows that they possess the same strand and sheet spacing in the characteristic cross-beta structure as do fibrils formed by the parent peptide. We report that the fibrils containing the RGD sequence are bioactive and that these fibrils interact specifically with cells via the RGD group displayed on the fibril surface. As the design of such functionalized fibrils can be systematically altered, these findings suggest that it will be possible to generate nanomaterials based on amyloid fibrils that are tailored to promote interactions with a wide variety of cell types. (c) 2007 Elsevier Ltd. All rights reserved.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:11282
Uncontrolled Keywords:self-assembly, nanotopography, XRD (X-ray diffraction), fibrils, bioactivity, RGD peptide , SYNCHROTRON X-RAY, PROTEIN AGGREGATION, PEPTIDE FIBRILS, IN-VITRO, FIBRONECTIN, MECHANISM, DOMAIN, AMYLOIDOGENESIS, TRANSTHYRETIN, RECOGNITION

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