e HFN7.1 antibody directed to the flexible linker between the 9th and 10th type III repeats of FN. That the activity of FN upon adsorption on SAMs was greater on OH terminated SAMs than CH3 terminated 
ones was previously assessed, and our results confirm the finely tuned chemistry-mediated conformation of FN that leads to a monotonically dependence of FN activity on surface composition, as the CH3/OH balance on the surface is altered. It is known that FN has a compact folded structure in physiological buffer that is stabilized through ionic interactions between arms. FN interactions with chemical groups of the substrate give rise to conformational changes in the molecule that must lead to the occlusion of the cell binding domains. It is likely that FN orients at the CH3 surface, so that its hydrophobic segments interact with the methyl groups in PEA, maybe throughout the heparin-binding fragment. Different supramolecular organization of the protein at the material interface is also reflected in protein distribution on the material surface, as directly observed with AFM images in 4 May 2011 | Volume 6 | Issue 5 | e19610 However, cells are able to synthesize and deposit FN matrix more abundantly and better organized into fibrillar networks on the hydroxyl terminated and the 70%-OH SAMs surfaces. Matrix degradation Surface Chemistry Directs Protein Remodeling Differences in the availability of FN adhesion domains on the different SAMs influence the initial cell-material interaction, as determined by focal adhesion formation and F-actin cytoskeleton development. Gene expression of b1 integrin subunit increases with the fraction of 9671117 OH groups in the sample, which leads to the development of vinculin plaques and actin fibers only on those SAMs on which FN adsorption occurs with the most favorable conformation, i.e. on those chemistries with the highest fraction of OH groups. The influence of surface chemistry on FN conformation and cell adhesion has been established for SAMs based on different chemical groups. In particular, differences in integrin binding and focal adhesion assembly between OH and CH3 SAMs most likely resulted from surface chemistry dependent differences in the functional presentation of adsorbed FN, whose major integrin-binding RGD domain is particularly 1235560-28-7 sensitive to the underlying chemistry. Likewise, it was previously found that the number of cells on FBS-coated CH3/OH mixed SAMs increases as the fraction of OH groups does; up to 80% OH and then it remains constant. Phosphorylation of FAK has been shown to be sensitive to surface chemistry. In our case, increasing the fraction of 5 May 2011 | Volume 6 | Issue 5 | e19610 Surface Chemistry Directs Protein Remodeling hydroxyl groups on the sample leads to similar FAK levels but with higher and higher levels of phosphorylation of Y-397, the autophosphorylation site in FAK and a binding site for Src and PI-3 kinases, which suggests a stepwise activation of signaling cascades as a function of hydroxyl groups on the surface increases. That is to say, activation of signaling pathways is directly related to integrin binding and focal adhesion formation, which are regulated by the availability of binding domains in FN upon adsorption on different chemistries. It has been demonstrated that FAK regulates cell adhesion strengthening via integrin activation and binding. Moreover, our results are consistent with the role Y- 6 May 2011 | Volume 6 | Issue 5 | e19610 Surface Chemistry Direc
