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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
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Pathway selection in peptide amphiphile assembly.

Peter A Korevaar1, Christina J Newcomb, E W Meijer

  • 1Institute for Complex Molecular Systems and Laboratory of Macromolecular and Organic Chemistry, Eindhoven University of Technology , 5600 MB Eindhoven, The Netherlands.

Journal of the American Chemical Society
|June 10, 2014
PubMed
Summary
This summary is machine-generated.

Different preparation methods for peptide amphiphiles create distinct supramolecular structures. Assembly into beta-sheets is slowed by solvents like hexafluoroisopropanol (HFIP) but forms stable filaments.

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Area of Science:

  • Supramolecular Chemistry
  • Materials Science
  • Biophysics

Background:

  • Supramolecular chemistry explores structure formation, but assembly pathways are understudied.
  • Peptide amphiphiles self-assemble into various structures based on environmental conditions.
  • Understanding assembly dynamics is crucial for controlling supramolecular morphology.

Purpose of the Study:

  • To investigate how different preparation protocols influence the self-assembly of peptide amphiphiles.
  • To determine the effect of solvents, specifically hexafluoroisopropanol (HFIP), on peptide amphiphile assembly.
  • To characterize the morphologies and kinetic stability of resulting supramolecular structures.

Main Methods:

  • Self-assembly of peptide amphiphiles in aqueous solutions with varying concentrations of HFIP.
  • Morphological characterization using techniques sensitive to secondary structure (e.g., spectroscopy, microscopy).
  • Kinetic analysis of assembly and disassembly processes.

Main Results:

  • Different preparation protocols yielded distinct supramolecular morphologies: long filaments with beta-sheets and smaller aggregates with random coil conformations.
  • The assembly rate into beta-sheets decreased with increasing HFIP concentration and was influenced by transient solution conditions.
  • A critical HFIP fraction (below 21%) was identified for spontaneous nucleation of beta-sheet filaments.
  • Formed beta-sheet assemblies exhibited high kinetic stability and slow disassembly.

Conclusions:

  • Preparation pathways significantly impact peptide amphiphile supramolecular morphology.
  • HFIP acts as a destabilizing solvent, modulating beta-sheet formation kinetics.
  • The study highlights the importance of assembly dynamics in controlling supramolecular structure and stability.
  • Insights into assembly dynamics offer a route to optimize pathways for specific functional applications.