engleski

Protein glycosylation affects nano-bio interactions depending on particle size and surface functionalization

Introduction The potential application of nanoparticles (NPs) in medicine has been subjected to several challenges, especially in terms of their interaction with biomolecules. Despite the numerous published data on nano-bio interactions, the role of protein glycosylation on the formation, characteristics, and fate of such nano-bio complexes is almost completely neglected, although most serum proteins are glycosylated. This study aimed to investigate the effect of glycosylation on the protein corona formation on surface of different AuNPs. For this purpose, we compared the mechanism of binding between different AuNPs to non-glycosylated proteins such as bovine serum albumin (BSA) and recombinant non-glycosylated transferrin (non-glycoTRF), with the glycosylated form of transferrin (glycoTRF). Results Differences in binding strengths were observed between proteins and AuNPs of different sizes. Correspondingly, changes in binding were observed upon interaction with AuNPs of the same surface structure, but different shape. Changes in the secondary structure and binding strength were not the same for glycoTRF and non-glycoTRF, after interaction with the same type of NPs. Conclusions Formation of the biomolecular corona, and thus biological fate of NPs depend not only on the physico-chemical properties of NPs, but also on the glycosylation status of proteins.

nanomedicine ; biomolecular corona ; BSA ; Transferrin

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