Gold nanoparticles’ blocking effect on UV-induced damage to human serum albumin

• Published in: Journal of nanoparticle research : an interdisciplinary forum for nanoscale science and technology Vol. 15; no. 1; p. 1
• Main Authors: Calzolai, Luigi, Laera, Stefania, Ceccone, Giacomo, Gilliland, Douglas, Hussain, Rohanah, Siligardi, Giuliano, Rossi, Francois
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Netherlands 2013; Springer; Springer Nature B.V
• Subjects: Brief Communication; Characterization and Evaluation of Materials; Chemistry and Materials Science; Condensed matter: structure, mechanical and thermal properties; Cross-disciplinary physics: materials science; rheology; Exact sciences and technology; Inorganic Chemistry; Lasers; Materials Science; Nanocrystalline materials; Nanoparticles; Nanoscale materials and structures: fabrication and characterization; Nanotechnology; Optical Devices; Optics; Photonics; Physical Chemistry; Physics; Radiation effects on specific materials; Structure of solids and liquids; crystallography; Ultraviolet radiation; UV damage; Gold nanoparticles; Synchrotron radiation; Protein unfolding; Circular dichroism; Radiation effects; Gold; Macromolecules; Serum albumin; Nanoparticles; Proteins; Ultraviolet radiation; High energy; Damage; Nanostructured materials
• ISSN: 1388-0764; 1572-896X
• DOI: 10.1007/s11051-012-1412-5

Ultraviolet radiation can cause the unfolding and destabilization of proteins. By using high energy photons from a synchrotron radiation source, we show that the UV-induced destabilization of human serum albumin (HSA) can be detected and monitored by measuring the circular dichroism spectrum of the protein. The high flux radiation source damages the HSA protein by causing a partial unfolding of the protein and a significant reduction in the amount of its secondary structure. Gold nanoparticles can effectively stop this UV-induced unfolding of HSA caused by synchrotron radiation. These phenomena could offer interesting applications to protect HSA protein from UV-induced damage and provide an alternative method to measure the relative stability of HSA.