Time-dependent pH scanning of the acid-induced unfolding of human serum albumin reveals stabilization of the native form by palmitic acid binding
01 Pubblicazione su rivista
DEL GIUDICE Alessandra, Dicko Cedric, Galantini Luciano, Pavel Nicolae Viorel
ISSN: 1520-6106
The most abundant plasma protein, human serum albumin (HSA), is known to undergo several conformational transitions in an acidic environment. To avoid buffer effects and correlate global and local structural changes, we developed a continuous acidification method and simultaneously monitored the protein changes by both small-angle scattering (SAXS) and fluorescence. The progressive acidification, based on the hydrolysis of glucono-?-lactone from pH 7 to pH 2.5, highlighted a multistep unfolding involving the putative F form (pH 4) and an extended and flexible conformation (pH