Glycation induced generation of amyloid fibril structures by glucose metabolites
Alsenaidy, Mohd Shahnawaz Khan, Nayyar Rabbani, Shams Tabrez, Islam B, Ajamaluddin Malik, Anwar Ahmed, Mohammad A Alsenaidy, Abdulrehman M . 2016
The non-enzymatic reaction (glycation) of reducing sugars with proteins has received increased interest in dietary and therapeutic research lately. In the present work, the impact of glycation on structural alterations of camel serum albumin (CSA) by different glucose metabolites was studied. Glycation of CSA was evaluated by specific fluorescence of advanced glycation end-products (AGEs) and determination of available amino groups. Further, conformational changes in CSA during glycation were also studied using 8-analino 1-nephthlene sulfonic acid (ANS) binding assay, circular dichroism (CD) and thermal analysis. Intrinsic fluorescence measurement of CSA showed a 22 nm red shift after methylglyoxal treatment, suggesting glycation induced denaturation of CSA. Rayleigh scattering analysis showed glycation induced turbidity and aggregation in CSA. Furthermore, ANS binding to native and glycated-CSA reflected perturbation in the environment of hydrophobic residues. However, CD spectra did not reveal any significant modifications in the secondary structure of the glycated-CSA. Thioflavin T (ThT) fluorescence of CSA increased after glycation, illustrated cross β-structure and amyloid formation. Transmission electron microscopy (TEM) analysis further reaffirms the formation of aggregate and amyloid. In summary, glucose metabolites induced conformational changes in CSA and produced aggregate and amyloid structures.
Polyphosphate polymers are chains of phosphate monomers chemically
bonded together via phosphoanhydride bonds. They are found in all prokaryotic and
eukaryotic organisms and are among…
Phosphate additions in processed foods are a health risk that has been overlooked. This study examined the
effects of a permitted food additive (E452; Sodium Hexametaphosphate (SHMP)) on…
Protein aggregation is implicated in different human diseases. It also makes the protein less desirable candidate for industry as they exhibit reduced biological activity. Proteins tend to…