PACIONI NATALIA
Artículos
Título:
Human serum albumin as protecting agent of silver nanoparticles: role of the protein conformation and amine groups in the nanoparticle stabilization
Autor/es:
EMILIO I. ALARCON; CARLOS J. BUENO-ALEJO; CHRISTOPHER W. NOEL; KEVIN G. STAMPLECOSKIE; NATALIA L. PACIONI; HORACIO POBLETE; J. C. SCAIANO
Editorial:
SPRINGER
Referencias:
Lugar: Berlin; Año: 2013 vol. 15 p. 1 - 1
Resumen:
hermally denatured human serum albumin interacts with ca. 3.0 nm spherical AgNP enhancing the fluorescence of Trp-214 at large protein/nanoparticle ratios. However, using native HSA, no changes in the emission were observed. The observation is likely due to differences between native and denatured protein packing resulting from protein corona formation. We have also found that NH2 blocking of the protein strongly affects the ability of the protein to protect AgNP from different salts/ions such as NaCl, PBS, Hank buffer, Tris - HCl, MES, and DMEM. Additionally, AgNP can be readily prepared in aqueous solutions by a photochemical approach employing HSA as an in situ protecting agent. The role of the protein in this case is beyond that of protecting agent; thus, Ag+ ions and I-2959 complexation within the protein structure also affects the efficiency of AgNP formation. Blocking NH2 in HSA modified the AgNP growth profile, surface plasmon band shape, and long-term stability sugge