Insulin aggregation tracked by its intrinsic TRES

Chung, Li Hung C.; Birch, David J. S.; Vyshemirsky, Vladislav; Ryadnov, Maxim G.; Rolinski, Olaf J.

doi:10.1063/1.5008477

Cited by 6 publications

(8 citation statements)

References 41 publications

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“…As a result of considering one polymeric chain interacting with one or several INS units, the comparison between simulations and experimental findings become difficult, because the experimental results indicate that multiple units of CS and INS as well, are involved in the complete complexation process. Furthermore, it has been described that both species have pH dependent self-aggregation kinetics that cannot be discarded, − even though the concentrations used in this work were low enough to minimize this effect …”

Section: Resultsmentioning

confidence: 99%

Combined Experimental and Molecular Simulation Study of Insulin–Chitosan Complexation Driven by Electrostatic Interactions

Prudkin-Silva

Pérez

Martínez

et al. 2019

J. Chem. Inf. Model.

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Protein−polysaccharide complexes constructed via self-assembly methods are often used to develop novel biomaterials for a wide range of applications in biomedicine, food, and biotechnology. The objective of this work was to investigate theoretically and to demonstrate via constant-pH Monte Carlo simulations that the complexation phenomenon between insulin (INS) and the cationic polyelectrolyte chitosan (CS) is mainly driven by an electrostatic mechanism.Experimental results obtained from FTIR spectra and ζ-potential determinations allowed us to complement the conclusions.The characteristic absorption bands for the complexes could be assigned to a combination of signals from CS amide I and INS amide II. The second peak corresponds to the interaction between the polymer and the protein at the level of amide II. INS− CS complexation processes not expected when INS is in its monomeric form, but for both tetrameric and hexameric forms, incipient complexation due to charge regulation mechanism took place at pH 5. The complexation range was observed to be 5.5 < pH < 6.5. In general, when the number of INS units increases in the simulation process, the solution pH at which the complexation can occur shifts toward acidic conditions. CS's chain interacts more efficiently, i.e. in a wider pH range, with INS aggregates formed by the highest monomer number. The charge regulation mechanism can be considered as a previous phase toward complexation (incipient complexation) caused by weak interactions of a Coulombic nature. 36 biotechnology. 2,3 Self-assembly is a ubiquitous and natural 37 process that lead to complex nanostructures with outstanding 38 functionalities. 4 In particular, the implementation of pH-

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Section: Resultsmentioning

confidence: 99%

Combined Experimental and Molecular Simulation Study of Insulin–Chitosan Complexation Driven by Electrostatic Interactions

Prudkin-Silva

Pérez

Martínez

et al. 2019

J. Chem. Inf. Model.

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“…Tyr is known to be sensitive to local microenvironments e.g. in evolving insulin, [9] during the process of glycation as shown in this paper and in the aggregation of beta-amyloid [10]. Therefore, we reason that the fluorescence response of the residue, both steady-state and time-resolved, can be used to monitor fibrillogenesis.…”

Section: Introductionmentioning

confidence: 90%

Protein fibrillogenesis model tracked by its intrinsic time-resolved emission spectra

Chung¹,

Birch²,

Vyshemirsky³

et al. 2019

Methods Appl. Fluoresc.

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The excited-state kinetics of the fluorescence of tyrosine in a de novo protein fibrillogenesis model was investigated as a potential tool for monitoring protein fibre formation and complexation with glucose (glycation). In stark contrast to insulin the time-resolved emission spectra (TRES) recorded over the period of 700 hours in buffered solutions of the model with and without glucose revealed no apparent changes in Tyr fluorescence responses. This indicates the stability of the model and provides a measurement-supported basis for its use as a reference material in fluorescence studies of protein aggregation.

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“…Our method explores the time-resolved emission spectra (TRES) obtained at discrete times throughout the fluorescence decays . Changes in TRES of the intrinsic fluorophores observed in aggregating proteins are usually complex, , as they are caused by the compilation of multiple effects, mainly the heterogeneity of the sample and the dielectric relaxation of fluorophores. In these studies, we aim to verify whether the alterations in TRES triggered by collagen glycation are sufficient to help in understanding the actual mechanisms of glycation, and thus potential pathways of its prevention.…”

Section: Introductionmentioning

confidence: 99%

Collagen Glycation Detected by Its Intrinsic Fluorescence

et al. 2021

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Collagen's long half-life (in skin approximately 10 years) makes this protein highly susceptible to glycation and formation of the advanced glycation end products (AGEs). Accumulation of cross-linking AGEs in the skin collagen has several detrimental effects; thus, the opportunity for non-invasive monitoring of skin glycation is essential, especially for diabetic patients. In this paper, we report using the time-resolved intrinsic fluorescence of collagen as a biomarker of its glycation. Contrary to the traditional fluorescence intensity decay measurement at the arbitrarily selected excitation and detection wavelengths, we conducted systematic wavelength-and time-resolved measurements to achieve time-resolved emission spectra. Changes in the intrinsic fluorescence kinetics, caused by both collagen aggregation and glycation, have been detected.

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Insulin aggregation tracked by its intrinsic TRES

Cited by 6 publications

References 41 publications

Combined Experimental and Molecular Simulation Study of Insulin–Chitosan Complexation Driven by Electrostatic Interactions

Combined Experimental and Molecular Simulation Study of Insulin–Chitosan Complexation Driven by Electrostatic Interactions

Protein fibrillogenesis model tracked by its intrinsic time-resolved emission spectra

Collagen Glycation Detected by Its Intrinsic Fluorescence

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