Effects of the surface polarity of nanomaterials on their interaction with complement protein gC1q. Issue 69 (18th November 2020)

• Record Type: Journal Article
• Authors: Wang, Shuai; Ou, Xinwen; Wutthinitikornkit, Yanee; Yi, Ming; Li, Jingyuan
• Is Part Of: RSC advances. Volume 10:Issue 69(2020)
• Page Start: 41993
• Page End: 42000
• Publication Date: 2020-11-18
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/d0ra05493c
• Languages: English
• ISSNs: 2046-2069

Abstract

Abstract : The dependence of the recognition mode of gC1q on the surface polarity of nanomaterials is mainly attributed to its distinct surface residue composition. Abstract : There are increasing studies about the biocompatibility of nanomaterials (NMs) as their applications in biomedicine become more widespread. The biocompatibility of NMs involves the recognition by the immune system including complement protein gC1q. In this work, the interaction of graphene oxide (GO) and self-assembled monolayer (SAM)-coated gold (111) surface with gC1q was studied by molecular dynamics (MD) simulations. The impacts of surface polarity of GO on its interaction with gC1q and the possible immune response were discussed by comparing the binding behavior of gC1q to the GO sheets with different oxidation degrees ( i.e., C5 O1 (OH)1 and C20 O1 (OH)1 ). We find the ghB module of gC1q tends to bind to GO sheet (C5 O1 (OH)1 ) with strong surface polarity, as the ghB module forms more hydrogen bonds with this GO sheet. On the other hand, the ghC module of gC1q tends to bind to GO (C20 O1 (OH)1 ) with weak surface polarity, as the ghC module tends to form pi–pi stacking and stronger hydrophobic interaction with this GO sheet. Similar phenomena are also found in the adsorption of gC1q with SAM: ghC prefers to bind to hydrophobic CH3 -SAM, and ghB prefers to bind to charged COO-SAM. The different binding modules of gC1q may result in different activation levels of complement system. Our findings suggest that the surface polarity of NMs regulates the interaction of NMs with gC1q and the subsequent immune response. In other words, the biocompatibility of NMs may be regulated by adjusting their surface polarity.