Vanillin restrains non-enzymatic glycation and aggregation of albumin by chemical chaperone like function

• Vanillin is a commonly used natural flavoring agent.
• Vanillin prevented both early and advanced glycation modification of albumin.
• Vanillin also inhibited lysine modification due to glycation.
• Vanillin showed chemical chaperone like activity by preventing the glycation induced conformational change in albumin as determined using circular dichroism.

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.