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Effect of RGD secondary structure and the synergy site PHSRN on cell adhesion, spreading and specific integrin engagement

Paper ID Volume ID Publish Year Pages File Format Full-Text
11502 744 2006 12 PDF Available
Title
Effect of RGD secondary structure and the synergy site PHSRN on cell adhesion, spreading and specific integrin engagement
Abstract

The relationship between the form of cell adhesion, ligand presentation, and cell receptor function was characterized using model Langmuir–Blodgett supported films, containing lipid-conjugated peptide ligands, in which isolated variables of the ligand presentation were systematically altered. First, the conformation of an adhesive Arginine–Glycine–Aspartic acid (RGD) peptide was varied by synthesizing linear and looped RGD peptide-containing amphiphiles and subsequently measuring the impact on the function of human umbilical vein endothelial cells. Secondly, the contribution of non-contiguous ligands to cellular engagement was assessed using multi-component biomimetic films. The peptide amphiphiles were composed of fibronectin-derived headgroups—GRGDSP, and its synergy site Pro–His–Ser–Arg–Asn (PHSRN)—attached to hydrocarbon tails. The peptide amphiphiles were diluted using polyethylene glycol (PEG) amphiphiles, where PEG inhibited non-specific cell adhesion. Cells adhered and spread on GRGDSP/PEG systems in a dose-dependent manner. The presentation of GRGDSP influenced integrin cell surface receptor specificity. Results demonstrated that β1-containing integrins mediated adhesion to the linear GRGDSP presentation to a greater extent than did the αvβ3 integrin, and looped GRGDSP preferentially engaged αvβ3. GRGDSP/PHSRN/PEG mixtures that closely mimicked the RGD–PHSRN distance in fibronectin, enhanced cell spreading over their two-component analogues. This study demonstrated that controlling the microenvironment of the cell was essential for biomimetics to modulate specific binding and subsequent signaling events.

Keywords
Looped RGD; Cyclic RGD; PHSRN; HUVEC; α5β1 integrin; αvβ3 integrin
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Effect of RGD secondary structure and the synergy site PHSRN on cell adhesion, spreading and specific integrin engagement
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biomaterials - Volume 27, Issue 20, July 2006, Pages 3863–3874
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us