Naslov
Effect of Surface Composition on Interaction of Silver Nanoparticles with Serum Transport Proteins

Autori
Šinko, Goran ; Capjak, Ivona ; Vinković Vrček, Ivana

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

Izvornik
12th Meeting of the Slovenian Biochemical Society with International Participation, Book of Abstracts, 20-23 September 2017, Bled, Slovenia / Goričar, Katja ; Hudler, Petra - Ljubljana : Slovenian Biochemical Society, 2017, 120-120

ISBN
978-961-93879-4-8

Skup
12th Meeting of the Slovenian Biochemical Society with International Participation

Mjesto i datum
Bled, Slovenija, 20.09.2017. - 23.09.2017

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
Silver nanoparticles ; Circular dichroism ; Bovine serum albumin ; Alpha-1-acid glycoprotein

Sažetak
Nanotechnology is gaining more and more significance in daily life by developing nano-based products. Due to specific physico-chemical properties nanoparticles (NPs) are used and applied in many fields, i.e. food technology, innovative materials, medical devices, pharmaceuticals. Silver nanoparticles (AgNPs) belong to the most commercialized metallic NPs due to their broad spectrum biocidal activity against multidrug-resistant bacteria, fungi, and viruses. The use of NPs in biology and medicine requires a molecular-level understanding of how NPs interact with macromolecules. It has been established that serum proteins present in blood will adsorb onto the surface of NPs, forming a “protein corona” which forms interface with biological medium. In this study, we used bovine serum albumin (BSA) and alpha-1-acid glycoprotein (α1AGP) as model proteins. Albumin is the most abundant low glycosylated protein (55 % in serum) which binds water, fat-soluble hormones and xenobiotics. Alpha-1-acid glycoprotein is plasma glycosylated alpha-globulin (3 % in serum) and serves as a carrier of basic and neutrally charged lipophilic compounds. Significant changes in protein secondary structure may affect protein carrier function. Therefore, preservation of its structure is important for normal function. Aim of this study was to understand how surface composition of AgNPs affects protein secondary structure due to formation of AgNP-protein complexes. We have prepared AgNPs with structurally diverse surface coatings: trisodium citrate (CIT), sodium bis(2-ethylhexyl) sulfosuccinate (AOT), cetyltrimethylammonium bromide (CTAB), poly(vinylpyrrolidone) (PVP), poly(L-lysine) (PLL), Brij-35 and Tween-20. Circular dichroism (CD) spectroscopy was used to evaluate differences in the absorption of left and right circularly polarized light to probe protein secondary structure. Proportion of the eight structural elements including α-helicity was calculated from experimental CD curves using BeStSel method. CD spectroscopy showed that exposure of BSA to cationic CTAB- and PLL-coated AgNPs did not perturb the secondary structure of BSA but reduction in α-helicity was observed (- 29 %). In case of a1AGP, reduction in α-helicity was observed for cationic CTAB- and anionic AOT-coated AgNPs (- 70 %).

Izvorni jezik
Engleski

Znanstvena područja
Kemija

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