2P077 Formation process of amyloid aggregates of apomyoglobin under constant temperature
2P077 一定温度下におけるアポミオグロビンのアミロイド凝集体形成過程(蛋白質 C) 物性(安定性、折れたたみなど)))

M. Koizumi, M. Hirai, K. Inoue, K. Miura
2005 Seibutsu Butsuri  
Agenetically engineered dis 岨 fide ・ deficient variant ef hen lysozyme ( OSS ) 1 in which the eight Cys residues are repluced by Ser or Ala, is i皿 t血 sically denatured in its monome 【ic state . The OSS is reported 駄)spontaneously fc )rm an a皿 yloid − like fiber under mild acidic eondi − tions with certain ionic strength ( Niraura ct all PNAS 101 , 4089, 2004 ). E ) tarnination by AFM reveals that the OSS fomns protefibrilS 〔 Kamatari et a1 . , J. MoL BioL, in press , 2005 ) . In the present
more » ... , we have studied the growth and the sive diStribut − ion of protofibrilS from OSS using ato 血 c f' 〕r microscepy ( AFM ) 、 Under a solution condition containing 20mM sodium acetate and 30mM NaC1 , pH4 . O , the OSS molecules at 5 mg ! mL form protofiblils which grows rapidly ( Within a few hours ) up to 150 nm . During this time , CD spec − tral changes take place from random − coil to bcta form . The length distribution of the protofibnl apProxh 皿 ately follcrws an ercponentially d reash 鳴 function of length as theoretically pred並 cted . Press旺 「 e jump Teal −t血 e IH NMR wa8 apphed to study tレe kinetic process of association and dissociation of OSS . The experiments show that the f(〕mation of the protofibrils 血Uy reversible under pressure , The proMe of the protofibril gmwth observed by AFM ε皿 d the kinetic process observed by NMR are cQns te皿t wlth the two growth med 夏 訃 niSms of the pretoribrils , i. e . , the addition of monomers t。 the temini of the protofibrils at the early phase ofthe groWth and the end − t〔Lend jo 血 ing Qf already gエown protefibrils at the ter phase of the gloWth,
doi:10.2142/biophys.45.s139_1 fatcat:l3efwiaw65b4jnyxvrqgoyaaou