Wang S.S.-S.Hung Y.-T.Wen W.-S.Lin K.-C.Chen G.-Y.2019-05-092019-05-09201113881981https://scholars.lib.ntu.edu.tw/handle/123456789/406737Amyloid 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.AmyloidFibrilInhibitionLysozymePhospholipid[SDGs]SDG31,2 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; Ureajournal article10.1016/j.bbalip.2011.02.0032-s2.0-79952706244https://www.scopus.com/inward/record.uri?eid=2-s2.0-79952706244&doi=10.1016%2fj.bbalip.2011.02.003&partnerID=40&md5=ed4311e1e6aace558d859bcd8b69f761