Heterogeneous Macromolecular crowding effect on nucleation-independent fibril formation of Lysozyme: Spectroscopic analysis of Structure, Stability, and fibrillation rate

Heterogeneous Macromolecular crowding effect on nucleation-independent fibril formation of Lysozyme: Spectroscopic analysis of Structure, Stability, and fibrillation rate

[Display omitted] •Studied effect of homotypic and heterotypic crowding on fibril rate and stability.•In mixed crowders fibril rate is comparable or slower than the individual crowders.•Crowders stabilize lysozyme and induce two-state unfolding at higher concentration.•Stability or fibril rate is no...

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Veröffentlicht in:Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy Molecular and biomolecular spectroscopy, 2024-07, Vol.315, p.124276, Article 124276
Hauptverfasser: Ghosh, Subhasree, Prabhu, N. Prakash
Format: Artikel
Sprache:eng
Schlagworte:
Animals
Circular Dichroism
Kinetics
Macromolecular Substances - chemistry
Muramidase - chemistry
Muramidase - metabolism
Protein Stability
Spectrometry, Fluorescence
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Zusammenfassung:[Display omitted] •Studied effect of homotypic and heterotypic crowding on fibril rate and stability.•In mixed crowders fibril rate is comparable or slower than the individual crowders.•Crowders stabilize lysozyme and induce two-state unfolding at higher concentration.•Stability or fibril rate is not correlated with size or viscosity of the crowders.•Excluded volume and direct interactions contribute to changes induced by crowders.
ISSN:1386-1425
1873-3557
DOI:10.1016/j.saa.2024.124276