title: Arginine controls heat-induced cluster-cluster aggregation of lysozyme at around the isoelectric point.
abstract: 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.
authors.affiliation: Institute of Applied Physics, University of Tsukuba, Tsukuba, Ibaraki, Japan.
authors.forename: Shunsuke
authors.initials: S
authors.lastname: Tomita
authors.forename: Hiroki
authors.initials: H
authors.lastname: Yoshikawa
authors.forename: Kentaro
authors.initials: K
authors.lastname: Shiraki
mesh_terms: D000818:Animals; D001120:Arginine / Q000494:pharmacology*; D002645:Chickens; D006358:Hot Temperature; D007526:Isoelectric Point; D007700:Kinetics; D008027:Light; D046529:Microscopy, Electron, Transmission; D009113:Muramidase / Q000737:chemistry* / Q000187:drug effects / Q000648:ultrastructure; D055503:Protein Multimerization / Q000187:drug effects; D012542:Scattering, Radiation
chemical_list: D001120:Arginine; D009113:Muramidase