Interaction between integrin a Ⅱbβ 3 and synthesized cyclic hexapeptide containing RGD

O6; The RGD sequence generally exists in the extracellular matrix proteins and can be recognized by many integrin proteins. The binding ability of immobilized biotinylated cyclic hexapeptide [cyclo(-Arg-Gly-Asp-D-Phe-Lys-Gly-)] containing RGD to integrin a ab β3 was tested by the methods of ELISA an...

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Bibliographic Details
Published in:科学通报（英文版） 2000, Vol.45 (23), p.2148-2152
Main Authors: HU Bin, SUI Senfang, Zeno Guttenberg, Michael Baermann, Erich Sackmann
Format: Article
Language:English
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Summary:O6; The RGD sequence generally exists in the extracellular matrix proteins and can be recognized by many integrin proteins. The binding ability of immobilized biotinylated cyclic hexapeptide [cyclo(-Arg-Gly-Asp-D-Phe-Lys-Gly-)] containing RGD to integrin a ab β3 was tested by the methods of ELISA and SPR. Results showed that a spacer of 1.48-2.2 nm between the peptide and the biotin residue was long enough to send the RGD sequence into the binding center embedded within a Ⅱbβ 3, and the equilibrium dissociation constant was 1.1 μm. The work provides an ideal model system for the research of cell adhesion on solid surfaces.
ISSN:1001-6538
DOI:10.1007/BF02886319