Naslov
Effect of particle shape and size on the interactions of gold nanoparticles with proteins of different glycosylation status

Autori
Pem, Barbara ; Barbir, Rinea ; Ramírez-Jiménez, Rafael ; Martín-Rapún, Rafael ; Martínez de la Fuente, Jesus ; Vinković Vrček, Ivana

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

Izvornik
FIRST CA17140 COST CONFERENCE Book of Abstracts / - Riga, 2019, 27-27

Skup
CA17140 - Cancer nanomedicine - from the bench to the bedside (NANO2CLINIC)

Mjesto i datum
Riga, Latvija, 01.01.2019

Vrsta sudjelovanja
Predavanje

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
gold nanoparticles, transferrin, glycosylation

Sažetak
1st CA17140 Conference, October 15-17, 2019, Riga, Latvia27Effect of Particle Shape on Interactions of Gold Nanoparticles with Proteins of Different Glycosylation StatusB.Pem1, R.Barbir1, R.Ramírez-Jiménez2, R.Martín-Rapún2, 3, J.Martínez de la Fuente2, I.Vinković Vrček11 Institute for Medical Research and Occupational Health, Zagreb, Croatia ; 2Instituto de Ciencia de Materiales de Aragón (ICMA), Consejo Superior de Investigaciones Científicas (CSIC)& CIBER-BBN, Zaragoza, Spain ; 3Instituto de Nanociencia de Aragón, Universidad de Zaragoza, Zaragoza, SpainE-mail:bpem@imi.hrSystematic and comprehensive study of the nano-bio interface is necessary to provide further insight into specific aspects of biological applications of nanoparticles (NP), which will subsequently help in future design of NPs for nanomedicine [1–3]. When NPs are introduced to a biological medium, numerous interactions occur at the nano-bio interface. Upon contact with biological matrices, NPs become immediately coated by a layer of biomolecules, in particular a large panel of proteins that form a protein corona (PC). The structure and composition of the PC depends on the physicochemical properties of the NPs, the nature of the physiological environment, and the duration of exposure [4, 5]. Despite extensive investigation of interaction between NPs and proteins, the role of protein glycosylation on formation, characteristics and fate of PC-NP complexes is almost completely overlooked. This study aimed to examine the effect of protein glycosylation on the mechanism of PC formation on the surface of gold NPs designed as theranostic systems. The model system consisted of gold NPs of different shape and with different surface chemistry, and glycosylated human transferrin and non-glycosylated recombinant transferrin as model proteins. Fluorescence spectroscopy was employed to monitor intrinsic fluorescence quenching of proteins due to their adsorption on the NP surface. The binding constants were calculated from titration experiments using the Stern-Volmer equation. The obtained results clearly demonstrated that mechanism of PC-NP formation is dependent on both physico-chemical characteristics of NPs and protein glycosylation status.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija, Farmacija

POVEZANOST RADA