Denaturation of human serum albumin initiated by cetyltrimethylammonium bromide as monitored via the intrinsic fluorescence of the protein and fluorescence of an eosin probe

Abstract

An analysis of the intrinsic fluorescence of the protein and the fluorescence of the eosin molecular probe in solutions of the protein was used to study the denaturation of human serum albumin (HSA) under the action of cetyltrimethylammonium bromide (CTAB), a cationic detergent, at various pH values. The denaturation of HSA under the influence of CTAB is a single-stage process over the entire pH range covered, pH (3.5–8.0). The maximum possible loosening of HSA globules in the presence of CTAB is reached at [CTAB] = 4 mmol/l. This detergent effectively denatures HSA at pH values higher than the pI of the protein (4.7).