ISSN:
0006-3525
Keywords:
molecular architecture
;
biomaterials
;
tissue engineering
;
cellular receptor binding
;
signal transduction
;
endothelial cell attachment
;
thrombosis
;
self-assembly
;
peptide-amphiphile
;
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
The development of biomaterials with desirable biocompatibility has presented a difficult challenge for tissue engineering researchers. First and foremost, materials themselves tend to be hydrophobic and/or thrombogenic in nature, and face compatibility problems upon implantation. To mediate this problem, researchers have attempted to graft proteins or protein fragments onto biomaterial surfaces to promote endothelial cell attachment and minimize thrombosis. We envisioned a novel approach, based on the capability of biomolecules to self-assemble into well-defined and intricate structures, for creating biomimetic biomaterials that promote cell adhesion and proliferation. One of the most intriguing self-assembly processes is the folding of peptide chains into native protein structures. We have developed a method for building proteinlike structural motifs that incorporate sequences of biological interest. A lipophilic moiety is attached onto an Nα-amino group of a peptide chain, resulting in a “peptide-amphiphile.” The alignment of amphiphilic compounds at the lipid-solvent interface is used to facilitate peptide alignment and structure initiation and propagation, while the lipophilic region adsorbs to hydrophobic surfaces. Peptide-amphiphiles containing potentially triple-helical or α-helical structural motifs have been synthesized. The resultant head group structures have been characterized by CD spectroscopy and found to be thermally stable over physiological temperature ranges. Triple-helical peptide-amphiphiles have been applied to studies of surface modification and cell receptor binding. Cell adhesion and spreading was promoted by triple-helical peptide-amphiphiles. Cellular interaction with the type IV collagen sequence α1(IV) 1263-1277 increased signal transduction, with both the time and level of induction dependent upon triple-helical conformation. Collectively, these results suggest that peptide-amphiphiles may be used to form stable molecular structures on biomaterial surfaces that promote cellular activities and improve biocompatibility. © 1998 John Wiley & Sons, Inc. Biopoly 47: 143-151, 1998
Additional Material:
6 Ill.
Type of Medium:
Electronic Resource
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