Protein fibril formation in the presence of glycerol or sorbitol

What is it about?

Impact of glycerol and sorbitol on assembly of iron-bound ovotransferrin (OVT) into nanofibrils was investigated. Thioflavin T fluorescence result indicated that the presence of glycerol or sorbitol could reduce the rate of OVT fibrillation. Sodium dodecyl sulfate polyacrylamide gel electrophoresis demonstrated that 60% sorbitol could retard hydrolysis of OVT completely for a period of time during thermal treatment, and decoupling hydrolysis from fibril self-assembly helped to identify the building blocks of OVT nanofibrils. OVT nanofibrils were composed of both intact OVT monomers and OVT-derived peptides. Influence of glycerol and sorbitol on morphology of OVT nanofibrils was studied using atomic force microscopy. The presence of glycerol or sorbitol shortened OVT nanofibrils, and the presence of 60% glycerol or sorbitol could increase thickness of OVT nanofibrils. Hopefully, this work may provide new insight about building blocks of protein nanofibrils and impact of polyols on protein fibrillation.

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Why is it important?

1. The presence of glycerol or sorbitol could reduce the rate of ovotransferrin fibrillation. 2. Sorbitol could significantly retard hydrolysis of iron-bound ovotransferrin. 3. Both intact monomers and peptides were building blocks of ovotransferrin nanofibrils. 4. The presence of glycerol or sorbitol shortened ovotransferrin nanofibrils. 5. The presence of 60% glycerol or sorbitol increased thickness of ovotransferrin nanofibrils.

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