Modification with N-benzylisatin restricts stress-induced aggregation of hen egg white lysozyme: Anti-amyloidogenic property of isatin derivative with possible clinical implications.

Hen egg white lysozyme (HEWL) is a structural homolog of human lysozyme and is widely used as a model protein to investigate protein aggregation. The effect of N-benzylisatin on stress-induced aggregation of HEWL has been investigated in the present study. Interaction of the isatin derivative with HEWL induced changes in protein secondary and tertiary structural conformation as evident from different biophysical and spectroscopic studies. In addition, modification with N-benzylisatin was found to increase the conformational stability of HEWL and afford considerable resistance to the protein to stress-induced aggregation as indicated from subsequent experimental studies, including thioflavin T fluorescence, microscopic imaging and dynamic light scattering analysis. Protein modification was analysed and confirmed by MALDI-TOF and ESI-MS studies. The results highlight possible clinical implications of isatin derivative in the treatment of protein misfolding and conformational disorders. • Interaction with N-benzylisatin causes structural changes of hen egg white lysozyme. • N-benzylisatin induces changes in surface hydrophobicity of hen egg white lysozyme. • N-benzylisatin induced modification of hen egg white lysozyme was analysed by mass spectrometric studies. • N-benzylisatin modification increases conformational stability of hen egg white lysozyme. • N-benzylisatin modification restricts stress-induced aggregation of hen egg white lysozyme. [ABSTRACT FROM AUTHOR]