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Concentration Effect on the Aggregation of a Self-Assembling Oligopeptide

S. Y. Fung ^*, C. Keyes , J. Duhamel  and P. Chen ^*

^* Department of Chemical Engineering and Department of Chemistry, University of Waterloo, Waterloo, Ontario N2L 3G1, Canada

Correspondence: Address reprint requests to P. Chen, Fax: 1-519-746-4979; E-mail: p4chen{at}cape.uwaterloo.ca.

Concentration is a key parameter in controlling the aggregation of self-assembling oligopeptides. By investigating the concentration effects, an aggregation mechanism of EAK16-II is proposed. Depending on the critical aggregation concentration (CAC) of EAK16-II, the oligopeptide aggregates into protofibrils through seeding and/or a nucleation process. Protofibrils then associate with each other to form fibrils. The CAC was found to be 0.1 mg/ml by surface tension measurements. The nanostructures of aggregates were imaged and analyzed by atomic force microscopy. Globular and fibrillar aggregates were observed, and their dimensions were further quantified. To ensure that the aggregates were formed in bulk solution, light scattering (LS) measurements were conducted to monitor the fibril formation with time. The LS profile showed two different rates of aggregation depending on whether the peptide concentration was above or below the CAC. At high concentrations, the LS intensity increased strongly at early times. At low concentrations, the LS intensity increased only slightly. Our study provides information about the nature of the oligopeptide self-assembly, which is important to the understanding of the fibrillogenesis occurring in conformational diseases and to many biomedical engineering applications.

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