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Int. J. Mol. Sci. 2013, 14(2), 2832-2845; doi:10.3390/ijms14022832

Measurement of the Interaction Between Recombinant I-domain from Integrin alpha 2 beta 1 and a Triple Helical Collagen Peptide with the GFOGER Binding Motif Using Molecular Force Spectroscopy

1
Nanoscience Centre, Department of Engineering, Cambridge University, Cambridge, CB3 0FF, UK
2
Department of Biochemistry, Cambridge University, Cambridge, CB2 1QW, UK
3
National Physical Laboratory, Teddington, TW11 0LW, UK
*
Authors to whom correspondence should be addressed.
Received: 4 December 2012 / Revised: 8 January 2013 / Accepted: 21 January 2013 / Published: 29 January 2013
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Abstract

The role of the collagen-platelet interaction is of crucial importance to the haemostatic response during both injury and pathogenesis of the blood vessel wall. Of particular interest is the high affinity interaction of the platelet transmembrane receptor, alpha 2 beta 1, responsible for firm attachment of platelets to collagen at and around injury sites. We employ single molecule force spectroscopy (SMFS) using the atomic force microscope (AFM) to study the interaction of the I-domain from integrin alpha 2 beta 1 with a synthetic collagen related triple-helical peptide containing the high-affinity integrin-binding GFOGER motif, and a control peptide lacking this sequence, referred to as GPP. By utilising synthetic peptides in this manner we are able to study at the molecular level subtleties that would otherwise be lost when considering cell-to-collagen matrix interactions using ensemble techniques. We demonstrate for the first time the complexity of this interaction as illustrated by the complex multi-peaked force spectra and confirm specificity using control blocking experiments. In addition we observe specific interaction of the GPP peptide sequence with the I-domain. We propose a model to explain these observations.
Keywords: integrin; alpha 2 beta 1; collagen; atomic force microscopy; single moleculeforce spectroscopy integrin; alpha 2 beta 1; collagen; atomic force microscopy; single moleculeforce spectroscopy
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Attwood, S.J.; Simpson, A.M.C.; Hamaia, S.W.; Bihan, D.; Roy, D.; Farndale, R.W.; Welland, M.E. Measurement of the Interaction Between Recombinant I-domain from Integrin alpha 2 beta 1 and a Triple Helical Collagen Peptide with the GFOGER Binding Motif Using Molecular Force Spectroscopy. Int. J. Mol. Sci. 2013, 14, 2832-2845.

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