Destructive and protective action of sodium dodecyl sulphate micelles on the native conformation of Bovine Serum Albumin: A study by extrinsic fluorescence probe 1-hydroxy-2-naphthaldehyde

• Published in: Chemical physics letters 2008-09, Vol.463 (1), p.183-188
• Main Authors: Singh, Rupashree Balia, Mahanta, Subrata, Guchhait, Nikhil
• Format: Article
• Language: English
• ISSN: 0009-2614; 1873-4448
• DOI: 10.1016/j.cplett.2008.08.017

The interaction of the anionic surfactant sodium dodecyl sulphate (SDS) with water soluble protein Bovine Serum Albumin (BSA) has been investigated using extrinsic fluorescence probe 1-hydroxy-2-naphthaldehyde (HN12). The characteristic excited state intramolecular proton transfer fluorescence band of HN12 has been used to study the stability of urea-denatured BSA in presence SDS micelles. The interaction of the anionic surfactant sodium dodecyl sulphate (SDS) with water soluble protein Bovine Serum Albumin (BSA) has been investigated spectroscopically using fluorescence probe 1-hydroxy-2-naphthaldehyde (HN12). The characteristic intramolecular proton transfer fluorescence band of HN12 has been used as an efficient reporter for the study of binding of SDS with BSA. The changes of spectral properties of HN12 demonstrate that SDS plays two opposite roles in the stability of protein BSA. It acts as a stabilizer at low concentration and destabilizer at high concentration to urea-denatured BSA.