Tertiary Butanol Induced Amyloidogenesis of Hen Egg White Lysozyme (HEWL) Is Facilitated by Aggregation-Prone Alkali-Induced Molten Globule Like Conformational State

Author(s): Mahrukh Hameed, Basir Ahmad, Rizwan Hassan Khan, Khurshid Iqbal Andrabi, Khalid Majid Fazili

Journal Name: Protein & Peptide Letters

Volume 16 , Issue 1 , 2009

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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.

Keywords: Hen egg white lysozyme, amyloid, thioflavin binding, dynamic light scattering

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Article Details

Year: 2009
Page: [56 - 60]
Pages: 5
DOI: 10.2174/092986609787049448

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