Amyloid formation in denatured single-mutant lysozymes where residual structures are modulated.
Reduced hen lysozyme has a residual structure involving long-range interaction. It has been demonstrated that a single mutation (A9G, W62G, W111G, or W123G) in the residual structure differently modulates the long-range interactions of reduced lysozyme. To examine whether such variations in the residual structure affect amyloid formation, reduced and alkylated mutant lysozymes were incubated under the amyloid-fibrillation condition. From the analyses of CD spectra and thioflavine T fluorescences, it was suggested that variation in residual structure led to different amyloid formation. Interestingly, the extent of amyloid formation did not always correlate with the extent to which the residual structure was maintained, resulting in the involvement of a hydrophobic cluster normally contained in W111 in the reduced lysozyme.
Mishima
Tomonori
T
Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka 812-8582, Japan.
Ohkuri
Takatoshi
T
Monji
Akira
A
Imoto
Taiji
T
Ueda
Tadashi
T
D000682:Amyloid / Q000096:biosynthesis / Q000737:chemistry*; D000818:Animals; D052160:Benzothiazoles; D002645:Chickens; D002942:Circular Dichroism; D005453:Fluorescence; D057927:Hydrophobic and Hydrophilic Interactions; D009113:Muramidase / Q000737:chemistry / Q000235:genetics*; D020125:Mutation, Missense; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011489:Protein Denaturation; D013844:Thiazoles
D000682:Amyloid; D052160:Benzothiazoles; D013844:Thiazoles; C009462:thioflavin T; D009113:Muramidase