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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
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Concentration effect on the aggregation of a self-assembling oligopeptide.

S Y Fung1, C Keyes, J Duhamel

  • 1Department of Chemical Engineering, University of Waterloo, Waterloo, Ontario N2L 3G1, Canada.

Biophysical Journal
|June 28, 2003
PubMed
Summary

Oligopeptide concentration dictates self-assembly. EAK16-II forms protofibrils and fibrils above a critical aggregation concentration (CAC) of 0.1 mg/ml, impacting conformational diseases and biomedical applications.

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Area of Science:

  • Biochemistry
  • Materials Science
  • Biophysics

Background:

  • Concentration is crucial for controlling self-assembling oligopeptide aggregation.
  • Understanding oligopeptide aggregation mechanisms is vital for biomedical applications and studying fibrillogenesis in diseases.

Purpose of the Study:

  • To propose an aggregation mechanism for the oligopeptide EAK16-II based on concentration effects.
  • To determine the critical aggregation concentration (CAC) of EAK16-II.
  • To characterize the nanostructures and aggregation kinetics of EAK16-II.

Main Methods:

  • Surface tension measurements to determine the critical aggregation concentration (CAC).
  • Atomic force microscopy (AFM) to image and analyze aggregate nanostructures.
  • Light scattering (LS) measurements to monitor fibril formation kinetics in bulk solution.

Main Results:

  • The critical aggregation concentration (CAC) for EAK16-II was determined to be approximately 0.1 mg/ml.
  • Atomic force microscopy revealed globular and fibrillar aggregates with quantified dimensions.
  • Light scattering data indicated concentration-dependent aggregation rates, with faster kinetics above the CAC.

Conclusions:

  • EAK16-II aggregation into protofibrils and fibrils is concentration-dependent, proceeding via seeding and/or nucleation.
  • The study elucidates oligopeptide self-assembly, offering insights into fibrillogenesis and informing biomedical engineering.
  • The findings highlight the importance of the CAC in dictating aggregation pathways and kinetics.