Pregled bibliografske jedinice broj: 1124217
Protein glycosylation affects nano-bio interactions depending on particle size and surface functionalization
Protein glycosylation affects nano-bio interactions depending on particle size and surface functionalization // NanoTox 2021 Virtual Conference : Book of Abstracts
Edinburgh, 2021. str. 127-127 (poster, međunarodna recenzija, sažetak, znanstveni)
CROSBI ID: 1124217 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Protein glycosylation affects nano-bio interactions depending on particle size and surface functionalization
Autori
Barbir, Rinea ; Ramírez Jiménez, Rafael ; Martín-Rapún, Rafael ; Domazet Jurašin, Darija ; Martinez de la Fuente, Jesus ; Vinković Vrček, Ivana
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
NanoTox 2021 Virtual Conference : Book of Abstracts
/ - Edinburgh, 2021, 127-127
Skup
10th International Conference on Nanotoxicology (NanoTox 2021)
Mjesto i datum
Edinburgh, Ujedinjeno Kraljevstvo, 20.04.2021. - 22.04.2021
Vrsta sudjelovanja
Poster
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
nanomedicine ; biomolecular corona ; BSA ; Transferrin
Sažetak
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.
Izvorni jezik
Engleski
Znanstvena područja
Kemija, Interdisciplinarne prirodne znanosti, Farmacija
POVEZANOST RADA
Projekti:
HRZZ-PZS-2019-02-4323 - Siguran pristup za razvoj nano-sustava za ciljanu isporuku lijekova u mozak (SENDER) (Vinković Vrček, Ivana, HRZZ ) ( CroRIS)
Ustanove:
Institut za medicinska istraživanja i medicinu rada, Zagreb,
Institut "Ruđer Bošković", Zagreb
