A research project you are working on involves the study of sugar binding to hum

Question

A research project you are working on involves the study of sugar binding to human serum albumin (HSA). The sugars to be tested are not fluorescent, and you do not wish to use a secondary fluorescent probe. HSA has only one tryptophan residue, and you know that this amino acid is fluorescent. You find that the tryptophan fluorescence spectrum of HSA undergoes changes when various sugars are added. Can you explain the results of this experiment and discuss the significance of the finding? (Hint: If a ligand is binding to a protein, it can affect the fluorescence spectrum of protein in two ways: 1. By binding close to the protein chromophore and directly perturbing its spectrum, or 2. By inducing conformational changes in the protein that may cause perturbation in protein fluorescence).

Explanation / Answer

Human serum albumin (HSA) is the most abundant serum protein and is prone to glycation by sugars sucha as glucose and fructose. The changes brought in by glycation of HSA includes quenching of tryptophan fluorescence either due to binding of sugar molecule close to the protein chromosphere or by inducing conformation changes in the protein structure.

The results of the above study that is changes in HSA fluorescence on addition of sugar have great significance in detecting hyperglycemia in the diabetes patients. The glycation of HSA by sugars and resulting changes in fluorescence can be used to detect and measure the sugar concentration in the blood of a diabetic person by establishing a correlation between the concentration of sugar and the change in the fluorescence spectrum of HSA.

Thanks!

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