Structural similarity between β3‐peptides synthesized from β3‐homo‐amino acids and aspartic acid monomers. Issue 4 (July 2014)

• Record Type: Journal Article
• Authors: Ahmed, Sahar; Sprules, Tara; Kaur, Kamaljit
• Is Part Of: Biopolymers. Volume 102:Issue 4(2014)
• Page Start: 359
• Page End: 367
• Publication Date: 2014-07
• Subjects: Biopolymers -- Periodicals; Peptides -- Periodicals; Spectrum analysis -- Periodicals; 572.33
• DOI: 10.1002/bip.22510
• Languages: English
• ISSNs: 0006-3525

Abstract

<abstract abstract-type="main"> <title>ABSTRACT</title> <p>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 <sc>l</sc>‐aspartic acid monomers (β³‐peptides <bold>1</bold>, <bold>5a, </bold> and <bold>6</bold>) or homologated β³‐amino acids (β³‐peptide <bold>2</bold>), 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 <sc>l</sc>‐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 <sc>l</sc>‐Asp monomers (<bold>1</bold>) and from homologated amino acids (<bold>2</bold>) form similar structures with no additional side‐chain interactions. These results suggest that the β³‐peptides derived from <sc>l</sc>‐Asp are promising peptide‐mimetics that can be readily synthesized using <sc>l</sc>‐Asp monomers as well as the right‐handed 14‐helical conformation of these β³‐peptides (such as <bold>1</bold> and <bold>6)</bold> 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.</p> </abstract>