Tertiary butanol induced amyloidogenesis of hen egg white lysozyme (HEWL) is facilitated by aggregation-prone alkali-induced molten globule like conformational state.
Proteins may form undesirable aggregates during the process of folding. Increasing evidence suggests that amyloid fibrils may arise from partially folded precursor molecules. We have previously demonstrated that hen egg white lysozyme [HEWL] exists as molten globule at pH 12.7. Here, we report that lysozyme at pH 7.0 and 11.0 are nearly stable to the addition of up to 45% t-butanol, but treatment of the alkali-induced molten globule form of HEWL [AMGL] with 20% t-butanol caused the formation of amyloid-like fibrils as evidenced by enhanced Thioflavin T binding and DLS measurements.
Hameed
Mahrukh
M
Institute of Biotechnology, A.M.U Aligarh, 202002, India.
Ahmad
Basir
B
Khan
Rizwan Hassan
RH
Andrabi
Khurshid Iqbal
KI
Fazili
Khalid Majid
KM
D000682:Amyloid / Q000138:chemical synthesis*; D000818:Animals; D052160:Benzothiazoles; D002645:Chickens; D002942:Circular Dichroism; D005260:Female; D008027:Light; D009113:Muramidase / Q000737:chemistry* / Q000187:drug effects; D020836:Protein Structure, Quaternary; D012542:Scattering, Radiation; D013050:Spectrometry, Fluorescence; D013844:Thiazoles / Q000737:chemistry; D020002:tert-Butyl Alcohol / Q000494:pharmacology*
D000682:Amyloid; D052160:Benzothiazoles; D013844:Thiazoles; C009462:thioflavin T; D009113:Muramidase; D020002:tert-Butyl Alcohol