Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 187, Issue -, Pages 341-349Publisher
ELSEVIER
DOI: 10.1016/j.ijbiomac.2021.07.092
Keywords
Hen egg white lysozyme; N-benzylisatin; Protein aggregation; Systemic amyloidosis; Mass spectrometry
Funding
- Indian Council of Medical Research [2019-3694/GEN-BMS]
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The study found that N-benzylisatin has a inhibitory effect on stress-induced aggregation of HEWL, enhancing the conformational stability of HEWL.
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.
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