Gelatin as a Potential Inhibitor of Insulin Amyloid Fibril Formation

Direct inhibition of amyloid fibrillation, the primary cause of many neurodegenerative diseases, using natural and synthetic molecules is one of the therapeutic strategies to prohibit the progression of amyloid diseases. Herein, we have demonstrated that, for the first time, gelatin, a commonly used gelling agent in food, was a potent inhibitor of amyloid fibril formation using insulin, a model protein for amyloid fibrillation. Thioflavin T and turbidity data indicated concentration‐dependent inhibition of insulin amyloid fibrillation by gelatin. Atomic force microscopy envisaged the inhibition of insulin fibrillation by gelatin. The spectroscopic analysis suggested that gelatin inhibits the insulin amyloid fibrillation by stabilising the native structure of insulin. 8‐anilinonaphthalene‐1‐sulfonic acid fluorescence data indicated that gelatin prevented the accessible exposed hydrophobic regions of insulin, which is required for insulin aggregation. Studies also suggested that the anti‐amyloidogenic efficiency of a mixture containing gelatin and a known amyloid inhibitor (Ferulic acid) was higher than their individual efficiency. Since gelatin is commonly used in drug formulation, its inherent anti‐amyloidogenic character may be beneficial in the formulation of anti‐amyloidogenic compounds. Hence, the current findings may have significant implications for the development of therapeutic agents for the prevention of disease‐related amyloid proteins. Gelatin as amyloid inhibitor: We have demonstrated that, for the first time, gelatin, commonly used as gelling agent and in making capsules, was a potential inhibitor for insulin amyloid fibril formation using various biophysical methods.