Biochemical and biophysical research communications, 2021-01, Vol.534, p.387-394
2021
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- Autor(en) / Beteiligte
- Titel
- Non enzymatic covalent modification by glycolysis end product converts hemoglobin into its oxidative stress potency state
- Ist Teil von
- Biochemical and biophysical research communications, 2021-01, Vol.534, p.387-394
- Ort / Verlag
- United States: Elsevier Inc
- Erscheinungsjahr
- 2021
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- The effect of glycation by Pyruvic acid (PA) on the early and advanced conformational changes in Hemoglobin (Hb) was studied. Multi Spectroscopic measurement revealed that Hb undergoes structural conformational changes and unbound heme upon incubation with PA. These covalent modifications were followed by the reduction of heme centre and these reduction processes initiates its peroxidase-like activity. An extended PA glycation resulted in the appearance of advanced glycation end products fluorescence, with notable changes in compositions of secondary structure. The amyloidogenic state was confirmed by SEM, fluorescence microscope observation. This study reveals an insight to the role of pyruvic acid which increases the oxidative stress due to the heme reduction and diabetic complication. The conformational change of PA glycated Hb. Figure was created with BioRender.com. [Display omitted] •Glycation led to the conformational and secondary structural changes in Hemoglobin.•Spectroscopy study revealed changes in heme orientation.•Amyloid formation has been determined in glycated hemoglobin using microscopic analysis(SEM).
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0006-291XeISSN: 1090-2104DOI: 10.1016/j.bbrc.2020.11.072Titel-ID: cdi_proquest_miscellaneous_2466296926
- Format
- –
- Schlagworte
- Aggregation, Amyloidogenesis, Amyloidogenic Proteins - chemistry, Amyloidogenic Proteins - metabolism, Arginine - chemistry, Carboxymethyl lysine, Coloring Agents, Congo Red, Electron Spin Resonance Spectroscopy, EPR, Glycated Hemoglobin A - chemistry, Glycated Hemoglobin A - metabolism, Glycated Hemoglobin A - ultrastructure, Glycation, Glycation End Products, Advanced - chemistry, Glycation End Products, Advanced - metabolism, Glycolysis, Glycosylation, Heme - chemistry, Hemoglobins - chemistry, Hemoglobins - metabolism, Hemoglobins - ultrastructure, Humans, In Vitro Techniques, Lysine - chemistry, Microscopy, Electron, Scanning, Oxidation-Reduction, Oxidative Stress, Protein Aggregates, Protein Conformation, Protein Structure, Secondary, Pyruvic Acid - chemistry, Secondary structure, Spectrometry, Fluorescence, Spectrophotometry, Ultraviolet