Exploring the inhibitory activity of short-chain phospholipids against amyloid fibrillogenesis of hen egg-white lysozyme
Journal
Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Journal Volume
1811
Journal Issue
5
Pages
301-313
Date Issued
2011
Author(s)
Abstract
Amyloid fibrillogenesis is an important pathological feature of a group of degenerative human diseases. The 129-residue enzyme hen egg-white lysozyme has been shown to form fibrils in vitro at pH 2.0 and 55 ¢XC. In this research, using various spectroscopic techniques, light scattering, and transmission electron microscopy, we first examined the influence of short-chain phospholipids on the amyloid fibrillogenesis and the structural changes derived from hen lysozyme in vitro. Both model short-chain phospholipids were observed to mitigate the fibrillogenesis of hen lysozyme. Also, urea-induced unfolding results suggested that the susceptibility of hen lysozyme to conformational changes elicited by the denaturant was observed to decrease upon addition of short-chain phospholipids. Moreover, our molecular dynamics simulations results demonstrated that the observed inhibitory action of short-chain phosoholipids against hen lysozyme fibrillogenesis might be attributable to the interference of £]-strand extension by the binding of phospholipids to lysozyme's £]-sheet-rich region. We believe that the outcome from this study may contribute to a better understanding the molecular factors affecting amyloid fibrillogenesis and the molecular mechanism(s) of the interactions between phospholipids/lipids and amyloid-forming proteins. ? 2011 Elsevier B.V. All rights reserved.
Subjects
Amyloid
Fibril
Inhibition
Lysozyme
Phospholipid
SDGs
Other Subjects
1,2 diheptanoyl sn glycero 3 phosphocholin; 1,2 dihexanoyl sn glycero 3 phosphocholine; amyloid; egg white; lysozyme; phospholipid; unclassified drug; urea; article; beta sheet; conformational transition; hen; hydrophobicity; light scattering; molecular dynamics; priority journal; protein secondary structure; simulation; transmission electron microscopy; Amyloid; Animals; Chickens; Female; Humans; Models, Molecular; Molecular Dynamics Simulation; Muramidase; Particle Size; Phosphatidylcholines; Phospholipids; Protein Denaturation; Protein Structure, Secondary; Urea
Type
journal article