Journal
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
Volume 296, Issue -, Pages -Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2023.122650
Keywords
Protein denaturation; Raman spectroscopy; Kinetics; Cadmium; Lysozyme
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This study investigated the influence of Cd(II) ions on the denaturation kinetics of hen egg white lysozyme (HEWL) under thermal and acidic conditions. Various techniques including Raman spectroscopy, fluorescence, AFM imaging, circular dichroism spectroscopy, and transmittance assays were employed to analyze the structural changes. The results showed that Cd(II) ions efficiently accelerated the disruption of tertiary structure and promoted the direct formation of organized β-sheets from α-helices. Furthermore, Cd(II) ions facilitated the assembly of initially disordered oligomers into aggregates with random structures similar to gels instead of amyloid fibrils, indicating an off-pathway denaturation pathway. These findings enhance the understanding of ion-specific effects.
To study the influence of Cd(II) ions on denaturation kinetics of hen egg white lysozyme (HEWL) under thermal and acidic conditions, spontaneous Raman spectroscopy in conjunction with Thioflavin-T fluorescence, AFM imaging, far-UV circular dichroism spectroscopy, and transmittance assays was conducted. Four distinctive Raman spectral markers for protein tertiary and secondary structures were recorded to follow the kinetics of conformational transformation. Through comparing variations of these markers in the presence or absence of Cd (II) ions, Cd(II) ions show an ability to efficiently accelerate the disruption of tertiary structure, and meanwhile, to promote the direct formation of organized & beta;-sheets from the uncoiling of & alpha;-helices by skipping intermediate random coils. More significantly, with the action of Cd(II) ions, the initially resulting oligomers with disordered structures tend to assemble into aggregates with random structures like gels more than amyloid fibrils, along with a so-called off-pathway denaturation pathway. Our results advance the in-depth understanding of corresponding ion-specific effects.
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