Study on the structural changes of bovine serum albumin with effects on polydatin binding by a multitechnique approach

Polydatin is a traditional Chinese medicine which shows effective biological activity as antimicrobial and antiviral agent. The secondary structure changes of bovine serum albumin (BSA) were investigated by the methods of Fourier transform infrared spectroscopy (FT-IR), circular dichroism (CD) and Raman spectroscopy. The experimental results indicated that polydatin changed the secondary structure of BSA. The presence of polydatin decreased α-helix content of BSA. The conformations of disulfide bridges and the microenvironment of Tyr, Trp residues were also changed.

Structural changes of bovine serum albumin caused by the binding of polydatin have been studied by FT-IR, CD and Raman spectroscopy. Polydatin changed the conformations of BSA with decreasing of α-helix content and changing of the conformations of disulfide bridges.Figure optionsDownload as PowerPoint slideHighlights
► The interaction between bovine serum albumin (BSA) and polydatin has been studied.
► The secondary structure changes of BSA were investigated by multispectroscopy.
► Polydatin decreased α-helix content and increased β-sheet and β-turn structures of BSA.
► The conformations of disulfide bridges and the microenvironment of Tyr, Trp were also changed.