Non-classical Helices with cis Carbon-Carbon Double Bonds in the Backbone: Structural Features of α,γ-Hybrid Peptide Foldamers.
The impact of geometrically constrained cis α,β-unsaturated γ-amino acids on the folding of α,γ-hybrid peptides was investigated. Structure analysis in single crystals and in solution revealed that the cis carbon-carbon double bonds can be accommodated into the 12-helix without deviation from the overall helical conformation. The helical structures are stabilized by 4→1 hydrogen bonding in a similar manner to the 12-helices of β-peptides and the 310 helices of α-peptides. These results show that functional cis carbon-carbon double bonds can be accommodated into the backbone of helical peptides.
Department of Chemistry, Indian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pashan, Pune-, 411008, India.
Mothukuri
M
Ganesh Kumar
Department of Chemistry, Indian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pashan, Pune-, 411008, India.
Varsha J
VJ
Thombare
Department of Chemistry, Indian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pashan, Pune-, 411008, India.
Mona M
MM
Katariya
Department of Chemistry, Indian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pashan, Pune-, 411008, India.
Kuruva
K
Veeresh
Department of Physical Chemistry, School of Chemistry, Madurai Kamaraj University, Madurai-, 625 021, India.
K Muruga Poopathi
KM
Raja
Department of Chemistry, Indian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pashan, Pune-, 411008, India. hn.gopi@iiserpune.ac.in.
Hosahudya N
HN
Gopi
D002244:Carbon / Q000737:chemistry*; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013237:Stereoisomerism
D010455:Peptides; D002244:Carbon
X-ray crystallography; foldamers; non-natural amino acids; peptide helices; peptides