Abstract
Crystalline dipeptides, (R) -arylglycyl- (R) -arylglycines (aryl = phenyl or naphthyl), have a straight glycylglycine backbone to construct a two-dimensional layer by intermolecular salt formation between COOH and NH2 groups. Guest molecules are included between the layers via host-guest interactions such as hydrogen bonding, aromaticaromatic interaction, and CH/πinteraction.α-Hydroxy esters and sulfoxides were recognized with high enantioselectivity to be included in the chiral cavities. Motifs of the dipeptide aggregation depend on the kinds of guests : sulfoxide and ether guests assemble the dipeptide molecules in parallel, whereas α-hydroxy esters arrange them in antiparallel. Interestingly, the peptide recognized poly (ethylene glycol) s, which penetrated through the crystal lattice. Longer polymers were preferably recognized and the inclusion crystals became more thermally stable. We also demonstrated that these simple dipeptide hosts change their conformation according to the shape of the guest. This seems like a flexible model for the recognition of substrates by enzymes.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: 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.
