Disordered Flanks Prevent Peptide Aggregation
Author Information
Author(s): Sanne Abeln, Daan Frenkel
Primary Institution: FOM Institute for Atomic and Molecular Physics, Amsterdam, The Netherlands
Hypothesis
The presence of disordered regions adjacent to small binding motifs can suppress aggregation of hydrophobic peptides in solution.
Conclusion
Disordered flanks adjacent to small peptide binding motifs help prevent aggregation without adversely affecting the binding strength to substrates.
Supporting Evidence
- Disordered regions in proteins are common and play a role in preventing aggregation.
- Simulations showed that small hydrophobic peptides aggregate without disordered flanks.
- Disordered flanks do not hinder the binding and folding of the binding motif.
Takeaway
This study shows that parts of proteins that are not folded can help stop them from sticking together, which is important for their function.
Methodology
The study used Monte Carlo simulations to investigate the effects of disordered regions on peptide aggregation and binding.
Limitations
The model used is highly simplified and may not fully represent the complexity of real proteins.
Digital Object Identifier (DOI)
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