A particular hydrophobic cluster in the residual structure of reduced lysozyme drastically affects the amyloid fibrils formation.
Six hydrophobic clusters involved in long-range interaction have been identified in the residual structure of reduced lysozyme at pH 2. Recently, it was found that modulation in the residual structure affected amyloid formation. In this paper, we examined the effect of the hydrophobic cluster containing W111 (cluster 5) on amyloid fibril formation of reduced lysozyme. The reduced W62G lysozyme, in which most of the hydrophobic clusters except for cluster 5 are disrupted, formed hardly any amyloid fibrils in comparison with the reduced wild-type. However, the disruption of cluster 5 by the mutation of Trp111 to Gly allowed significant amyloid fibril formation of reduced W62G lysozyme. Moreover, the extent of amyloid formation in the reduced W62G/W111G lysozyme was greater than that of the reduced wild-type lysozyme. From the above results, it became clear that cluster 5 contributed to retarding the amyloid fibrils formation of the W62G lysozyme.
Mishima
Tomonori
T
Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan.
Ohkuri
Takatoshi
T
Monji
Akira
A
Imoto
Taiji
T
Ueda
Tadashi
T
D000682:Amyloid / Q000096:biosynthesis*; D000818:Animals; D002645:Chickens; D004529:Egg White; D057927:Hydrophobic and Hydrophilic Interactions; D008854:Microscopy, Electron; D009113:Muramidase / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure; D010084:Oxidation-Reduction
D000682:Amyloid; D009113:Muramidase