title: A synthetic zipper peptide motif orchestrated via co-operative interplay of hydrogen bonding, aromatic stacking, and backbone chirality.
abstract: Here, we report on a new class of synthetic zipper peptide which assumes its three-dimensional zipper-like structure via a co-operative interplay of hydrogen bonding, aromatic stacking, and backbone chirality. Structural studies carried out in both solid- and solution-state confirmed the zipper-like structural architecture assumed by the synthetic peptide which makes use of unusually remote inter-residual hydrogen-bonding and aromatic stacking interactions to attain its shape. The effect of chirality modulation and the extent of noncovalent forces in the structure stabilization have also been comprehensively explored via single-crystal X-ray diffraction and solution-state NMR studies. The results highlight the utility of noncovalent forces in engineering complex synthetic molecules with intriguing structural architectures.
authors.affiliation: Division of Organic Chemistry, National Chemical Laboratory, Dr. Homi Bhabha Road, Pune 411 008, India.
authors.forename: Roshna V
authors.initials: RV
authors.lastname: Nair
authors.forename: Sanjeev
authors.initials: S
authors.lastname: Kheria
authors.forename: Suresh
authors.initials: S
authors.lastname: Rayavarapu
authors.forename: Amol S
authors.initials: AS
authors.lastname: Kotmale
authors.forename: Bharatam
authors.initials: B
authors.lastname: Jagadeesh
authors.forename: Rajesh G
authors.initials: RG
authors.lastname: Gonnade
authors.forename: Vedavati G
authors.initials: VG
authors.lastname: Puranik
authors.forename: Pattuparambil R
authors.initials: PR
authors.lastname: Rajamohanan
authors.forename: Gangadhar J
authors.initials: GJ
authors.lastname: Sanjayan
mesh_terms: D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D010455:Peptides