Structural similarity between β3-peptides synthesized from β3-homo-amino acids and aspartic acid monomers

Authors

  • Sahar Ahmed,

    1. Faculty of Pharmacy and Pharmaceutical Sciences, University of Alberta, Edmonton, AB, Canada
    2. Department of Pharmacognosy and Medicinal Chemistry, Faculty of Pharmacy, Taibah University, Kingdom of Saudi Arabia
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  • Tara Sprules,

    1. Quebec/Eastern Canada High Field NMR Facility, McGill University, Montreal, QC, Canada
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  • Kamaljit Kaur

    Corresponding author
    1. Faculty of Pharmacy and Pharmaceutical Sciences, University of Alberta, Edmonton, AB, Canada
    • Correspondence to: Kamaljit Kaur, Faculty of Pharmacy and Pharmaceutical Sciences, University of Alberta, Edmonton, Alberta, Canada, T6G 2E1; e-mail: kkaur@ualberta.ca

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  • This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

ABSTRACT

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. © 2014 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 102: 359–367, 2014.

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