Journal
RSC ADVANCES
Volume 5, Issue 93, Pages 76257-76262Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c5ra12831e
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Funding
- CSIR, India [01/2507/11-EMR-II]
- CSIR, India
- IISER-Kolkata
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Solvent interaction has a significant effect on the folding and structural diversity of short aromatic gamma-peptides that lead to a change in initial helical conformation. The internal rigidity of building blocks promotes the helical conformations of the gamma-peptides containing m-aminobenzoic acid and N, N'-dicyclohexylurea. Various solution state NMR experiments show the existence of intermolecular hydrogen bonded structures of the short aromatic gamma-peptides. In a polar protic solvent (MeOH), the helical strand interacts with the solvent molecules and expands to a more open (nearly extended) structure which further self-assembles to form a supramolecular sheet like structure. However, crystals obtained from chloroform show a supramolecular double helix which is stabilized by intermolecular hydrogen bonding and pi-pi stacking interactions. The report describes how significantly different self-assembled structures are developed from compounds folded in a subtly different manner by interaction with the solvent.
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