Vanillin restrains non-enzymatic glycation and aggregation of albumin by chemical chaperone like function
Saurabh Awasthi, N.T. Saraswathi
International Journal of Biological Macromolecules
Vanillin a major component of vanilla bean extract is commonly used a natural flavoring agent. Glycation is known to induce aggregation and fibrillation of globular proteins such as albumin, hemoglobin. Here we report the inhibitory potential of vanillin toward early and advanced glycation modification and amyloid like aggregation of albumin based on the determination of both early and advanced glycation and conformational changes in albumin using circular dichroism. Inhibition of aggregation and fibrillation of albumin was determined based on amyloid specific dyes i.e., Congo red and Thioflavin T and microscopic imaging. It was evident that vanillin restrains glycation of albumin and exhibits protective effect toward its native conformation.
Circular dichroism, Secondary structure, Aggregation, Biochemistry