ArticlePloS one2013
Molten globule of hemoglobin proceeds into aggregates and advanced glycated end products.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 92 citations in OpenAlex.
- Distinct Molten-Globule Conformations in an Interacting Protein Domain Resolved byAngewandte Chemie (International ed. in English) · 2026Article
- Label-Free Evaluation of Advanced Glycation End Products by a Comprehensive Biophysical Analysis.Analytical chemistry · 2026Article
- Mechanistic Insights Into Protein Aggregation Inhibition by Green-Synthesized Silver Nanoparticles: A Study on Human Lysozyme.IET nanobiotechnology · 2026Article
- Association of Hemoglobin and Myoglobin into Supramolecular Complexes: Significance for Life and Practice.International journal of molecular sciences · 2025Review
- An overview on glycation: molecular mechanisms, impact on proteins, pathogenesis, and inhibition.Biophysical reviews · 2024Review
- Antiglycation and Antioxidant Effect of Nitroxyl towards Hemoglobin.Antioxidants (Basel, Switzerland) · 2022Article
- Heme Protein Binding of Sulfonamide Compounds: A Correlation Study by Spectroscopic, Calorimetric, and Computational Methods.ACS omega · 2022Article
- 4-Chloro-1,2-phenylenediamine induced structural perturbation and genotoxic aggregation in human serum albumin.Frontiers in chemistry · 2022Article
- Refolding of Hemoglobin Under Macromolecular Confinement: Impersonating In Vivo Volume Exclusion.Journal of fluorescence · 2021Article
- Understanding the Role of Protein Glycation in the Amyloid Aggregation Process.International journal of molecular sciences · 2021Review
- Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods.Molecules (Basel, Switzerland) · 2020Review
- Article
- Silk Fibroin/Collagen/Chitosan Scaffolds Cross-Linked by a Glyoxal Solution as Biomaterials toward Bone Tissue Regeneration.Materials (Basel, Switzerland) · 2020Article
- Hemoglobin structure at higher levels of hemoglobin A1C in type 2 diabetes and associated complications.Chinese medical journal · 2020Article
- Glyoxal modification mediates conformational alterations in silk fibroin: Induction of fibrillation with amyloidal features.Journal of biosciences · 2020Article
- Covalent Modification by Glyoxals Converts Cytochrome c Into its Apoptotically Competent State.Scientific reports · 2019Article
- Article
- Formation of Pentosidine Cross-Linking in Myoglobin by Glyoxal: Detection of Fluorescent Advanced Glycation End Product.Journal of fluorescence · 2017Article
- Amyloid Fibrils from Hemoglobin.Biomolecules · 2017Article
- The impact of the HbA1c level of type 2 diabetics on the structure of haemoglobin.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Conformational alterations of bovine hemoglobin (Hb) upon sequential addition of glyoxal over a range of 0-90% v/v were investigated. At 20% v/v glyoxal, molten globule (MG) state of Hb was observed by altered tryptophan fluorescence, high ANS binding, existence of intact heme, native-like secondary structure as depicted by far-UV circular dichroism (CD) and ATR-FTIR spectra as well as loss in tertiary structure as confirmed by near-UV CD spectra. In addition, size exclusion chromatography analysis depicted that MG state at 20% v/v glyoxal corresponded to expanded pre-dissociated dimers. Aggregates of Hb were detected at 70% v/v glyoxal. These aggregates of Hb had altered tryptophan environment, low ANS binding, exposed heme, increased β-sheet secondary structure, loss in tertiary structure, enhanced thioflavin T (ThT) fluorescence and red shifted Congo Red (CR) absorbance. On incubating Hb with 30% v/v glyoxal for 0-20 days, advanced glycation end products (AGEs) were detected on day 20. These AGEs were characterised by enhanced tryptophan fluorescence at 450 nm, exposure of heme, increase in intermolecular β-sheets, enhanced ThT fluorescence and red shift in CR absorbance. Comet assay revealed aggregates and AGEs to be genotoxic in nature. Scanning electron microscopy confirmed the amorphous structure of aggregates and branched fibrils of AGEs. The transformation of α-helix to β-sheet usually alters the normal protein to amyloidogenic resulting in a variety of protein conformational disorders such as diabetes, prion and Huntington's.
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