Interactions between N-succinyl-chitosan and bovine serum albumin

Interactions between proteins and biocompatible amphiphilic chitosan derivatives have been investigated owing to their scientific and technological importance. In this study, the interactions between N-succinyl-chitosan (NSCS) and bovine serum albumin (BSA) are characterized by circular dichroism (CD); isothermal titration calorimetric (ITC); ultraviolet (UV) spectrum; fluorescence spectrum and transmission electron microscopy (TEM) techniques. ITC has been used to demonstrate that BSA binds to NSCS with a molar ratio of 30:1. The binding isotherms for these H-bond and hydrophobic interactions are exothermic. The CD and Fluorescence spectrum indicate that the conformation of BSA does not change significantly during the chain entanglements between BSA and NSCS. The NSCS entrapped BSA shows a nanosphere morphology revealed by TEM techniques. This study demonstrates the potential for NSCS matrix encapsulation of proteins or other hydrophilic bioactive drugs.