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Updated: May 12, 2026
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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Sequence length determinants for self-assembly of amphipathic β-sheet peptides
Naomi R Lee1, Charles J Bowerman, Bradley L Nilsson
1Department of Chemistry, University of Rochester, Rochester, NY, 14627-0216.
Biopolymers
|April 5, 2013
Summary
Minute changes in amphipathic peptide sequences dramatically alter self-assembly. Truncated peptides showed varied fibril formation, highlighting sequence length and strand registry effects on self-assembly.
Area of Science:
- Biochemistry
- Materials Science
- Peptide Science
Background:
- Amphipathic peptides with alternating hydrophobic and hydrophilic residues self-assemble into β-sheet fibrils.
- The Ac-(FKFE)2-NH2 peptide forms β-sheet bilayers with sequestered hydrophobic cores.
Purpose of the Study:
- To investigate the self-assembly of truncated Ac-(FKFE)2-NH2 peptides (Ac-FKFEFKF-NH2 and Ac-KFEFKFE-NH2).
- To understand the impact of sequence length and strand registry on peptide self-assembly.
Main Methods:
- Molecular modeling was used to hypothesize self-assembly behavior.
- Synthesis and characterization of truncated peptide derivatives.
- Analysis of fibril morphology and self-assembly propensity.
Main Results:
- Ac-FKFEFKF-NH2 self-assembled into fibrils with distinct morphologies.
- Ac-KFEFKFE-NH2 exhibited a significantly reduced self-assembly propensity, sometimes failing to assemble.
- Minute sequence alterations led to dramatic changes in self-assembly outcomes.
Conclusions:
- Peptide sequence length and strand registry critically influence β-sheet bilayer formation.
- Hydrophobicity and charge distribution are key factors in self-assembly.
- Fine-tuning peptide sequences offers a method to control self-assembly processes and resulting structures.
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