Structural differences between native Hen egg white lysozyme and its fibrils under different environmental conditions

Spectrochim Acta A Mol Biomol Spectrosc. 2013 Oct;114:368-76. doi: 10.1016/j.saa.2013.05.060. Epub 2013 May 29.

Abstract

The difference in molecular structure of native HEWL and its fibrils, grown at a pH value near physiological pH 7.4 and at a pH value just above the pI, 10.7 in presence and absence of Cu(II) ions, is discussed. We focus on differences between the molecular structure of the native protein and fibrils using principal component analysis of their Raman spectra. The overlap areas of the scores of each species are used to quantify the difference in the structure of the native HEWL and fibrils in different environments. The overall molecular structures are significantly different for fibrils grown at two pH values. However, in presence of Cu(II) ions, the fibrils have similarities in their molecular structures at these pH environments. Spectral variation within each species, as obtained from the standard deviations of the scores in PCA plots, reveals the variability in the structure within a particular species.

Keywords: Fibrils; HEWL; Principal component analysis; Raman scattering.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid / chemistry*
  • Animals
  • Chickens
  • Copper / chemistry
  • Hydrogen-Ion Concentration
  • Muramidase / chemistry*
  • Principal Component Analysis
  • Protein Conformation
  • Spectrum Analysis, Raman

Substances

  • Amyloid
  • Copper
  • hen egg lysozyme
  • Muramidase