4.2 Article

Arginine Controls Heat-Induced Cluster-Cluster Aggregation of Lysozyme at Around the Isoelectric Point

Journal

BIOPOLYMERS
Volume 95, Issue 10, Pages 695-701

Publisher

WILEY
DOI: 10.1002/bip.21637

Keywords

arginine; diffusion-limited cluster-cluster aggregation; lysozyme; reaction-limited cluster-cluster aggregation; solution additive

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The process of protein aggregation has attracted a great deal of research attention, as aggregates are first of all a nuisance to preparation of high quality protein and secondly used as novel materials. In the latter case, the process of protein aggregation needs to be controlled. Here, we show how arginine (Arg) regulates the process of heat-induced protein aggregation. Dynamic light scattering and transmission electron microscopy revealed that heat-induced aggregation of lysozyme at around the isoelectric point occurred in a two-step process: formation of start aggregates, followed by further growth mediated by their sticking with diffusion-limited cluster-cluster aggregation. In the presence of Arg, the diffusion-limited regime changed to reaction-limited cluster-cluster aggregation. The data indicated that the solution additives that coexisted with proteins would affect the property of the formed product, such as morphology and mechanic strength. (C) 2011 Wiley Periodicals, Inc. Biopolymers 95: 695-701, 2011.

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