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Formation of stable secondary structures by oligomers that mimic natural peptides is a key asset for enhanced biological response. Here we show that oligomeric β3‐hexapeptides synthesized from l‐aspartic acid monomers (β3‐peptides 1, 5a, and 6) or homologated β3‐amino acids (β3‐peptide 2), fold into similar stable 14‐helical secondary structures in solution, except that the former form right‐handed 14‐helix and the later form left‐handed 14‐helix. β3‐Peptides from l‐Asp monomers contain an additional amide bond in the side chains that provides opportunities for more hydrogen bonding. However, based on the NMR solution structures, we found that β3‐peptide from l‐Asp monomers (1) and from homologated amino acids (2) form similar structures with no additional side‐chain interactions. These results suggest that the β3‐peptides derived from l‐Asp are promising peptide‐mimetics that can be readily synthesized using l‐Asp monomers as well as the right‐handed 14‐helical conformation of these β3‐peptides (such as 1 and 6) may prove beneficial in the design of mimics for right‐handed α‐helix of α‐peptides.


This is the accepted version of the following article:

Ahmed S, Sprules T, Kaur K. Structural similarity between b3-Peptides synthesized from and b3-homo-amino acids and L-aspartic acid monomers. Pept Sci. 2014; 102:359-367.

which has been published in final form at DOI: 10.1002/bip.22510. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.





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