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A Rapid and Chemical-free Hemoglobin Assay with Photothermal Angular Light Scattering
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Probing hemoglobin glyco-products by fluorescence spectroscopy
Aristos Ioannou1, Constantinos Varotsis1
1Cyprus University of Technology, Department of Environmental Science and Technology Limassol Cyprus c.varotsis@cut.ac.cy +357 25002802.
RSC Advances
|May 11, 2022
Summary
Dietary Maillard reaction products (MRPs) can modify human hemoglobin (Hb). These MRPs cause conformational changes in Hb, potentially leading to inactive hemichrome forms linked to blood disorders.
Area of Science:
- Biochemistry
- Protein Chemistry
Background:
- Maillard reaction products (MRPs) are formed from carbohydrate-protein interactions, leading to advanced glycation end-products (AGEs).
- Dietary MRPs are implicated as potential chemical modifiers of human proteins, including hemoglobin (Hb).
Purpose of the Study:
- To investigate the binding effects of isolated MRPs on hemoglobin (Hb).
- To elucidate the structural and functional consequences of MRP modification on Hb.
Main Methods:
- Utilized fluorescence spectrophotometry to study the reaction between MRPs and isolated hemoglobin.
- Analyzed changes in tryptophan fluorescence to detect structural modifications in Hb.
Main Results:
- Glycation of Hb by MRPs induced a Stokes shift in tryptophan fluorescence emission, indicating structural changes.
- Formation of new fluorescence features suggested the creation of modified hemoglobin species.
- Evidence of conformational changes in the β-Trp 37 moiety and altered motion of His 64 (E7) within the heme pocket.
Conclusions:
- MRPs binding to Hb leads to significant conformational alterations.
- These modifications can result in the formation of inactive hemichrome hemoglobin, a process potentially linked to blood disorders.
