Naslov
Interaction of Differently Sized, Shaped, and Functionalized Silver and Gold Nanoparticles with Glycosylated versus Nonglycosylated Transferrin

Autori
Barbir, Rinea ; Ramírez Jiménez, Rafael ; Martín- Rapún, Rafael ; Strasser, Vida ; Domazet Jurašin, Darija ; Dabelić, Sanja ; Martínez de la Fuente, Jesus ; Vinković Vrček, Ivana.

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
COST ACTION CA17140 NANO2CLINIC 1st STSM VIRTUAL CONFERENCE Book of abstracts / - , 2022, 15-15

Skup
COST ACTION CA17140 NANO2CLINIC 1st STSM VIRTUAL CONFERENCE

Mjesto i datum
Online konferencija, 16.03.2022

Vrsta sudjelovanja
Predavanje

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
AgNP, AuNP, glycosylation

Sažetak
Possible application of metal nanoparticles (NPs) in medicine has been challenged by numerous factors, especially regarding their biocompatibility, efficacy, and safety. Exposure of NPs to a biological medium results in their direct interaction with biological macromolecules and leads to the formation of a dynamic biomolecular layer known as the biomolecular corona. Despite numerous published data on nano- biointeractions, the role of protein glycosylation in the formation, characteristics, and fate of such nano-biocomplexes has been almost completely neglected, although most serum proteins are glycosylated. This study aimed to systematically investigate the differences in interaction of metallic NPs with glycosylated vs nonglycosylated transferrin. To reach this aim, we compared interaction mechanisms between differently sized, shaped, and surface- functionalized silver and gold nanoparticles to commercially available human transferrin (TRF), a glycosylated protein, and to its non-glycosylated recombinant form (ngTRF). Bovine serum albumin (BSA) was also included in the study for comparative purposes. After performing NPs characterization fluorescence quenching and circular dichroism methods were used to evaluate protein binding constants on the nanosurface and conformational changes after the protein–NP interactions, respectively. Competitive binding of TRF, ngTRF, and BSA to the surface of different NPs was evaluated by separating them after extraction from protein corona by gel electrophoresis following quantification with a commercial protein assay. It was found that the strength of protein binding to NPs, changes in secondary protein structure and composition of protein corona depend not only on the physicochemical properties of NPs, but also on the presence of glycans on proteins. The obtained results emphasize the importance of protein glycosylation for nano-bio interactions, which contributes to understanding the effect of NPs on biological systems and can be used in the development of new diagnostic, prognostic and therapeutic nanotools.

Izvorni jezik
Engleski

POVEZANOST RADA