We also showed that the neuroprotective effects of 17E6 and ab58524 were not completely abolished after siFAK treatment. The survival rate of cells significantly decreased as the apoptotic rate increased. All of these results indicate that other signaling pathways may participate to mediate an and b1 Itg function. It 
has been reported by Wright S that a2b1 and anb1 facilitate the accumulation of Ab and formation of the Ab network by Pyk2. Sylvie M also reported that anb3 and anb5 regulate mitotic cell death via ILK and RhoB signaling pathways, which participate in the radioresistance of glioma cells. Moreover, Itgs can regulate cell survival and the cell cycle via PI3K/Akt or Rac/JNK signaling pathways, which are activated by Cdc42. In this study, we found that FAK AbMole Isovitexin expression and its phosphorylation increased following Ab treatment, which indicated that Ab-treatment may induce FAK expression and initiate autophosphorylation at the Tyr397 site. After treating the cells with 17E6 and ab58524, the expression of FAK decreased, and its phosphorylation increased. Treatment with 17E6 and ab58524 may further promote FAK phosphorylation and activate cell survival via PI3K/Akt signaling inhibit the expression of the tumor suppressor protein p53 or activate FAK/paxillin/p130CAS signaling pathways. Following siFAK treatment, FAK phosphorylation may be reduced, thus resulting in an increase in apoptosis. Taken together, both an and b1 Itgs participate to mediate Abinduced apoptosis in hippocampal neurons. The underlying pathogenesis may be related to activation of tyrosine-phosphorylation by FAK. According to our study, inhibition of the interaction between Ab and Itgs or the interruption of FAK activation may effectively inhibit apoptosis in hippocampal neurons in AD pathogenesis. Thus, this study may provide insight towards the development of novel AD treatments. The interaction of proteins with different biomaterials plays a vital role in describing their biocompatibility. Depending on the surface the overall protein structure may vary from native to unfolded. Especially on hydrophobic surfaces proteins tend to unfold. Experiments on pyrolytic graphite have shown that proteins irrespective of their primary sequence, secondary structure and molecular weight unfold and form nanopatterns. Molecular dynamics simulations on the other hand provide a direct method for theoretically analyzing the adsorption processes at an atomistic scale. A major problem that arises when using MD to study protein adsorption is the limited time scale of only a few hundred ns. The experimental time scale when these processes are investigated usually ranges from ms to hours. It has been shown by Wei et al. that very long simulations are necessary since major adsorption steps like dehydration take a long time and denaturing events even longer. Strategies to overcome this sampling problem are needed. A computationally efficient method using an implicit inviscid water environment has first been established for protein adsorption processes by Raffaini et al..