Furan-based locked Z-vinylogous γ-amino acid stabilizing protein α-turn in water-soluble cyclic α3γ tetrapeptides.
Described here is the design, synthesis, and conformational analysis of cyclic tetrapeptides (CTPs) with α3γ architecture containing a furan-based locked Z-vinylogous amino acid (Vaa). This unnatural amino acid locks into a γ-turn that induces type IαRS-turn in the CTPs. Stabilized by a 13-membered intramolecular H-bond, these CTPs show robust conformation in water and aprotic solvent irrespective of the sequence of tripeptide consisting of α-amino acids used.
Medicinal and Process Chemistry Division and ‡Centre for Nuclear Magnetic Resonance, SAIF, CSIR-Central Drug Research Institute , Lucknow, Uttar Pradesh 226031, India.
Yarkali
Y
Krishna
Shrikant
S
Sharma
Ravi S
RS
Ampapathi
Dipankar
D
Koley
D000596:Amino Acids / Q000737:chemistry*; D018360:Crystallography, X-Ray; D005663:Furans / Q000737:chemistry*; D008958:Models, Molecular; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D010456:Peptides, Cyclic / Q000138:chemical synthesis* / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012997:Solvents; D014867:Water
D000596:Amino Acids; D005663:Furans; D010456:Peptides, Cyclic; D012997:Solvents; D014867:Water