2014
DOI: 10.1371/journal.pone.0087256
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On the Characterization of Intermediates in the Isodesmic Aggregation Pathway of Hen Lysozyme at Alkaline pH

Abstract: Protein aggregation leading to formation of amyloid fibrils is a symptom of several diseases like Alzheimer’s, type 2 diabetes and so on. Elucidating the poorly understood mechanism of such phenomena entails the difficult task of characterizing the species involved at each of the multiple steps in the aggregation pathway. It was previously shown by us that spontaneous aggregation of hen-eggwhite lysozyme (HEWL) at room temperature in pH 12.2 is a good model to study aggregation. Here in this paper we investiga… Show more

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Cited by 22 publications
(14 citation statements)
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“…From the fitted kinetic data to a sigmoidal function [ 45 ], the obtained values of the half-time for aggregation (t 1/2 ) and the apparent rate constant (k app = 1/τ) are 138.0 h and 0.028 h -1 , respectively. The lag time (t lag [ThT] = t 1/2 −2τ), deduced from these parameters, has a value of 66.6 h. Generally, these parameters are dependent of several factors such as the protein concentration, temperature, pH and cosolvents [ 27 41 ].…”
Section: Resultsmentioning
confidence: 99%
“…From the fitted kinetic data to a sigmoidal function [ 45 ], the obtained values of the half-time for aggregation (t 1/2 ) and the apparent rate constant (k app = 1/τ) are 138.0 h and 0.028 h -1 , respectively. The lag time (t lag [ThT] = t 1/2 −2τ), deduced from these parameters, has a value of 66.6 h. Generally, these parameters are dependent of several factors such as the protein concentration, temperature, pH and cosolvents [ 27 41 ].…”
Section: Resultsmentioning
confidence: 99%
“…Those parameters are dependent on the conditions used for the brillation as protein concentration, solvents, temperature and pH. 38,40,41 Eqn (1) tted all curves adequately, providing the values of t lag and apparent rate of bril formation (k) summarised in Table S1 (ESI †). At t SA ¼ 0 h, no uorescence was observed in any sample, indicating that no b-sheet aggregates or brils were formed at this stage.…”
Section: Resultsmentioning
confidence: 99%
“…Fibrils prepared in an acidic medium can be disassembled by SDS into lysozyme monomers and hydrolysis-originated fragments (discussed subsequently). In contrast, at a high pH, lysozyme transforms into aggregates by intermolecular disulfide cross-linking [29,30]. Although the molecular mechanisms of lysozyme fibrillation were different under acidic and alkaline conditions, EGCG exhibited an inhibitory effect on amyloid formation under both conditions.…”
Section: Inhibitory Effects Of Egcg On Lysozyme Fibrillationmentioning
confidence: 95%