Characterization of heat induced spherulites of lysozyme reveals new insight on amyloid initiation.

ABSTRACT: Here, we report results obtained during our experiments to visualize how heat transforms globular protein, lysozyme into building block of β-amyloids. Light scattering experiments showed formation of lower order associated species around 50-70 °C followed by rapid cooperativity to β-amyloid fibrils. Interestingly, crystallization drops set at higher temperatures either led to aggregates or spherulites. The latter possess an amorphous β-fibril rich core with thin crystalline needles projecting outwards. Diffraction of the crystalline outgrowths revealed novel dimers and trimers of lysozyme where individual chains were similar to monomer with marginal gain in β-sheet content. Importantly, analysis of Amide I stretching frequencies showed that protein loses its secondary structure at temperat

SUBMITTER: Sharma P 

PROVIDER: S-EPMC4772699 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature