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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

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Nucleation effects in peptide foldamers.

Anupam Patgiri¹, Stephen T Joy, Paramjit S Arora

¹Department of Chemistry, New York University, New York, New York 10003, USA.

Journal of the American Chemical Society

|June 22, 2012

Summary

This summary is machine-generated.

Beta(3)-amino acid oligomers offer stable structural mimics of alpha-helices. These heterogeneous sequences show increased conformational rigidity compared to alpha-peptide helices, influenced by macrocycle templating.

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Area of Science:

Biochemistry
Organic Chemistry
Structural Biology

Background:

Oligomers of beta(3)-amino acids and mixed alpha-/beta(3)-residues are proteolytically stable structural mimics of alpha-helices.
These oligomers can adopt defined conformations even in short sequences.

Purpose of the Study:

To evaluate the impact of beta(3)-residues compared to alpha-amino acid analogs in prenucleated helices.
To investigate the conformational properties of heterogeneous sequences containing beta(3)-residues.

Main Methods:

Hydrogen-deuterium exchange experiments were employed.
Analysis of prenucleated helices with varying compositions of alpha- and beta(3)-residues.

Main Results:

Heterogeneous sequences with "alpha alpha alpha beta" repeats demonstrated greater conformational rigidity than homogeneous alpha-peptide helices.
The helical conformation templating by the macrocycle significantly influenced the observed rigidity.

Conclusions:

Beta(3)-residues enhance the conformational rigidity of helical oligomers.
Macrocycle structure plays a crucial role in dictating the conformational stability of these alpha-helix mimics.