Alteration of human serum albumin tertiary structure induced by glycation. Spectroscopic study

Szkudlarek, Agnieszka; Maciążek-Jurczyk, Małgorzata; Chudzik, Mariola; Równicka-Zubik, J.; Sułkowska, Anna

doi:10.1016/j.saa.2015.09.018

Cited by 27 publications

(19 citation statements)

References 14 publications

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“…Tyr and Trp residues were the main objects of the research, and the wavelength intervals, Δλ, were 15 and 60 nm, respectively. From Figure , we interpret that the fluorescence intensity was decreased on addition of C3G, and the glycation process did not alter the λ max of HSA . Moreover, the λ max of HSA and gHSA shifted inconspicuously on addition of C3G as did the shape of the wave, which showed that binding of C3G to HSA and gHSA had little influence on the polarity of microenvironment near the aromatic amino acid residues.…”

Section: Resultsmentioning

confidence: 83%

“…Previously, Deanna et al proved that glycation altered the local structure around Trp214 and this alteration translated into an overall change in the stability of gHSA compared with HSA . In addition, Szkudlarek et al discovered that glycation could impact the fluorescence intensity of Trp and Tyr. Szkudlarek et al thought the residues´ glycation altered the nature of the tryptophanyl and tyrosyl environment, which was very sensitive to change .…”

Section: Resultsmentioning

confidence: 99%

“…In addition, Szkudlarek et al discovered that glycation could impact the fluorescence intensity of Trp and Tyr. Szkudlarek et al thought the residues´ glycation altered the nature of the tryptophanyl and tyrosyl environment, which was very sensitive to change . This previous work supports our results to a certain extent, although it still needs to be verified further.…”

Section: Resultsmentioning

confidence: 99%

“…They discovered that the electrochemical signal was decreased when HSA was glycated . Szkudlarek et al discussed the alteration in the HSA tertiary structure induced by glycation. They suggested that glycation could arise between Lys199, Lys212, Lys233, Lys276, Lys281, Lys286 and Arg218 residues and glycose.…”

Section: Resultsmentioning

confidence: 99%

“…They suggested that glycation could arise between Lys199, Lys212, Lys233, Lys276, Lys281, Lys286 and Arg218 residues and glycose. Glycation of these residues altered the nature of the tryptophanyl environment, which is very sensitive to change …”

Section: Resultsmentioning

confidence: 99%

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Spectroscopic andin silicostudy of binding mechanism of cynidine‐3‐O‐glucoside with human serum albumin and glycated human serum albumin

Gao

Jia

et al. 2016

Luminescence

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The drug-serum albumin interaction plays a dominant role in drug efficacy and disposition. The glycation of serum albumin that occurs during diabetes may affect its drug-binding properties in vivo. In order to evaluate the interactivity characteristics of cyanidin-3-O-glucoside (C3G) with human serum albumin (HSA) and glycated human serum albumin (gHSA), this study was undertaken using multiple spectroscopic techniques and molecular modeling analysis. Time-resolved fluorescence and the thermodynamic parameters indicated that the quenching mechanism was static quenching, and hydrogen bonding and Van der Waals force were the main forces. The protein fluorescence could be quenched by C3G, whereas the polarity of the fluorophore was not obviously changed. C3G significantly altered the secondary structure of the proteins. Furthermore, the interaction force that existed in the HSA-C3G system was greater than that in the gHSA-C3G system. Fluorescence excitation emission matrix spectra, red edge excitation shift, Fourier transform infrared spectroscopy and circular dichroism spectra provided further evidence that glycation could inhibit the binding between C3G and proteins. In addition, molecular modeling analysis supported the experimental results. The results provided more details for the application of C3G in the treatment of diabetes.

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Section: Resultsmentioning

confidence: 83%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 3 more Smart Citations

Spectroscopic andin silicostudy of binding mechanism of cynidine‐3‐O‐glucoside with human serum albumin and glycated human serum albumin

Gao

Jia

et al. 2016

Luminescence

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Phosphorescence, Fluorescence, and Chemiluminescence in Clinical Chemistry

Albani

2016

Encyclopedia of Analytical Chemistry

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Effect of (E,E)‐2,4‐decadienal on Side‐Chain Modification, Conformation Change, and Aggregation of Bovine Serum Albumin

et al. 2021

Euro J Lipid Sci & Tech

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Protein modification by active aldehydes is associated with ageing and some chronic diseases, and it is closely related to food quality and safety. In this study, the modification of bovine serum albumin (BSA) using trans,trans-2,4-decadienal at various concentrations (0-10 mm) is investigated. The results show that the changes in the number of free amino groups and arginine residues, carbonyl formation, aggregation characteristics, and fluorescent lipofuscin-like pigments (LFLP) fluorescence are more severe at (E,E)-2,4-decadienal concentrations of 4-10 mm, whereas the conformational changes are more significant at low concentrations (0.1-2 mm). In the BSA modified by 1-10 mm (E,E)-2,4-decadienal, the microenvironment of tryptophan residues to become more hydrophobic, the structure became compact, hydrophobic binding sites decreases, molecular weight and particle size increases, and covalently cross-linked heterogeneous aggregates increases. At the same time, the relationship between the oxidation parameters and samples is explained using principal component analysis and hierarchical cluster analysis. Practical Applications: (E,E)-2,4-decadienal is highly electrophilically active with biomacromolecules. However, compared to the widely studied malonaldehyde (MDA), acrolein (ACR), 4-hydroxynonenal (HNE), and 4-oxo-trans-2-nonenal (ONE)-protein adducts, research on the modification of a protein by (E,E)-2,4-decadienal is insufficient, and the chemical nature of (E,E)-2,4-decadienal-protein adducts is not clear. This study may be useful for extending our understanding of the specific role of (E,E)-2,4-decadienal in the formation of modified proteins during the occurrence of chronic diseases and provides a theoretical reference for food quality and safety problems caused by protein carbonylation during processing and storage.

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Alteration of human serum albumin tertiary structure induced by glycation. Spectroscopic study

Cited by 27 publications

References 14 publications

Spectroscopic andin silicostudy of binding mechanism of cynidine‐3‐O‐glucoside with human serum albumin and glycated human serum albumin

Spectroscopic andin silicostudy of binding mechanism of cynidine‐3‐O‐glucoside with human serum albumin and glycated human serum albumin

Phosphorescence, Fluorescence, and Chemiluminescence in Clinical Chemistry

Effect of (E,E)‐2,4‐decadienal on Side‐Chain Modification, Conformation Change, and Aggregation of Bovine Serum Albumin

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