Abstract
AbstractThe 11/9‐helix is one of nontraditional helices available to α/β‐peptides with alternating residue types. Several β‐amino acid residues are known to promote 11/9‐helical folding with two types of intramolecular hydrogen bonds. Both β2‐amino acids and β3‐amino acids are common acyclic β‐amino acids that can be regarded as homologs of α‐amino acids with the same side chain group. However, β2‐amimo acids have not been widely used as much as β3‐amino acids partly because β2‐residue is believed to be not as strong as β3‐residue in promoting a distinct conformation. Here we report 11/9‐helical folding of α/β‐peptides that consist of L‐α‐alanine and (S)‐β2‐homoalanine with residue alternation. In addition, circular dichroism study reveals that β2‐homoalanine promotes 11/9‐helical folding more strongly than β3‐homoalanine in polar protic solvent conditions.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.