Physicochemical Characteristics of Protein–NP Bioconjugates: The Role of Particle Curvature and Solution Conditions on Human Serum Albumin Conformation and Fibrillogenesis Inhibition

• Published in: Langmuir 2012-06, Vol.28 (24), p.9113-9126
• Main Authors: Goy-López, Sonia, Juárez, Josué, Alatorre-Meda, Manuel, Casals, Eudald, Puntes, Victor F, Taboada, Pablo, Mosquera, Victor
• Format: Article
• Language: English
• Subjects: Chemistry, Physical; Gold - chemistry; Gold - pharmacology; Humans; Metal Nanoparticles - chemistry; Models, Molecular; Particle Size; Protein Conformation; Serum Albumin - antagonists & inhibitors; Serum Albumin - chemistry; Solutions; Structure-Activity Relationship; Surface Properties
• ISSN: 0743-7463; 1520-5827
• DOI: 10.1021/la300402w

Gold nanoparticles (Au NPs) from 5 to 100 nm in size synthesized with HAuCl4 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 (