Physicochemical characteristics of protein-NP bioconjugates: The role of particle curvature and solution conditions on human serum albumin conformation and fibrillogenesis inhibition

Sonia Goy-López, Josué Juárez, Manuel Alatorre-Meda, Eudald Casals, Victor F. Puntes, Pablo Taboada, Victor Mosquera

Research output: Contribution to journalArticleResearchpeer-review

152 Citations (Scopus)

Abstract

Gold nanoparticles (Au NPs) from 5 to 100 nm in size synthesized with HAuCl 4 and sodium citrate were complexed with the plasma protein human serum albumin (HSA). Size, surface charge, and surface plasmon bands of the Au NPs are largely modified by the formation of a protein corona via electrostatic interactions and hydrogen bonding as revealed by thermodynamic data. Negative values of the entropy of binding suggested a restriction in the biomolecule mobility upon adsorption. The structure of the adsorbed protein molecules is slightly affected by the interaction with the metal surface, but this effect is enhanced as the NP curvature decreases. Also, it is observed that the protein molecules adsorbed onto the NP surface are more resistant to complete thermal denaturation than free protein ones as deduced from the increases in the melting temperature of the adsorbed protein. Differences in the conformations of the adsorbed protein molecules onto small (<40 nm) and large NPs were observed on the basis of potential data and FTIR spectroscopy, also suggesting a better resistance of adsorbed protein molecules to thermal denaturing conditions. We think this enhanced protein stability is responsible for a reduced formation of HSA amyloid-like fibrils in the presence of small Au NPs under HSA fibrillation conditions. © 2012 American Chemical Society.
Original languageEnglish
Pages (from-to)9113-9126
JournalLangmuir
Volume28
Issue number24
DOIs
Publication statusPublished - 19 Jun 2012

Fingerprint Dive into the research topics of 'Physicochemical characteristics of protein-NP bioconjugates: The role of particle curvature and solution conditions on human serum albumin conformation and fibrillogenesis inhibition'. Together they form a unique fingerprint.

Cite this