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Dynamic Debonding Force Measurements of Ligand (RGD)-Platelet Receptor (GP Ilb/IIIa) System under Physiological Conditions

Published online by Cambridge University Press:  02 July 2020

ImShik Lee  and
Roger E. Marchant
ImShik Lee
Affiliation:
Department of Biomedical Engineering, Case Western Reserve University. 10900 Euclid Avenue, Cleveland, OH44106-7207, UAS
Roger E. Marchant
Affiliation:
Department of Biomedical Engineering, Case Western Reserve University. 10900 Euclid Avenue, Cleveland, OH44106-7207, UAS
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ABSTRACT

Binding formation between a peptide sequence (GSSSGRGDSPA) which contains the cell adhesion sequence –RGD-found in fibrinogen, vWF, fibrinonectin, and vitronectin and human platelet intergrin GP Ilb/IIIa plays an important role in thrombus formation. Using atomic force microscopy (AFM), we visualized the detailed structures of membrane and submembrane of the cell, and measured the interaction forces between a peptide modified cantilever probe tip and platelet surface from pN to nN levels under physiological buffer. Direct measurements of the debonding force for the RGD ligand - GP Ilb/IIIa system are presented. To eliminate the possible measurement of the hgand-receptor pair, or of the ligand and AFM tip, following desorption of the ligand; the cantilever tip surface was modified with covalent coupling chemistry rather than physical absorption. Our results showed that the single molecular rupturing force was 93.3 ± 10.41 pN with considerable chain extension in the receptor. The rupturing forces showed a logarithmic dependence of the rate of loading

Type
Biomaterials
Information
Microscopy and Microanalysis , Volume 6 , Issue S2: Proceedings: Microscopy & Microanalysis 2000, Microscopy Society of America 58th Annual Meeting, Microbeam Analysis Society 34th Annual Meeting, Microscopical Society of Canada/Societe de Microscopie de Canada 27th Annual Meeting, Philadelphia, Pennsylvania August 13-17, 2000 , August 2000 , pp. 974 - 975
Copyright
Copyright © Microscopy Society of America

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References

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