Naslov
Size, shape and surface structure affect interaction of metallic nanoparticles with transport proteins

Autori
Capjak, Ivona ; Barbir, Rinea ; Domazet Jurašin, Darija ; Debeljak, Željko ; Šinko, Goran ; Dutour Sikirić, Maja ; Vinković Vrček, Ivana

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

Izvornik
17th European Symposium on Organic Reactivity / Vančik, Hrvoj ; Namjesnik, Danijel - Zagreb : Hrvatsko kemijsko društvo, 2019, 79-79

ISBN
978-953-55232-9-1

Skup
17th European Symposium on Organic Reactivity (ESOR 2019)

Mjesto i datum
Dubrovnik, Hrvatska, 08.09.2019. - 13.09.2019

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
protein corona ; silver nanoparticles

Sažetak
Metallic nanoparticles are currently being used in an increasing number of consumer and medical products, due to particular properties of metals at nanoscale. This necessitates safety assessment for human health including evaluation of fate, transformation and interaction of NPs within biological environment.[1, 2] This study aimed to determine how different physico-chemical properties of silver nanoparticles (AgNPs) affect their behavior and interaction with albumin and α1-acid glycoprotein as nonglycosylated and glycosylated transport proteins from human blood. For this purpose, sixteen types of AgNPs of different shape (spherical, triangular and cubic), size (10 and 50 nm) and surface stabilization were prepared[3] After careful characterization of their size distribution, surface charge, dissolution, and behavior in water, phosphate buffer, and physiological solution, effect of various physicalchemical properties of AgNPs on the binding affinities for these two proteins was evaluated. In addition, changes in the secondary protein structure due to binding to AgNPs surface were evaluated by circular dichroism. Obtained results demonstrated that the surface charge and nominal diameter of AgNPs both have a significant role in nano-bio interactions. Proteins present in the media bind to the AgNPs surface immediately after their suspension in these media. Binding constants of proteins to AgNPs surface are similar to binding between these proteins and some drugs. Binding of albumin to AgNPs results in a greater and more varied alteration of the protein structure compared to α1-acid glycoprotein.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

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