Formation of left-handed helices in hybrid peptide oligomers with cis beta-sugar amino acid and L-Ala as building blocks.
Residue based control of specific helical folding is explored in hybrid peptide oligomers consisting of alternating L-Ala and cis-beta-furanoid sugar amino acid (FSAA) residues as building blocks; two series of these hybrid oligomers are designed, synthesized and extensively characterized by using NMR, CD, FT-IR and MD simulation studies; results show the co-existence of left-handed 11- and 14/15-helical conformations in these short oligomers of Boc-(alpha/beta) and Boc-(beta/alpha) series.
Jagadeesh
Bharatam
B
Center for Nuclear Magnetic Resonance, Indian Institute of Chemical Technology, Hyderabad-7, India. bj@iict.res.in
Prabhakar
Anabathula
A
Sarma
Ganti Dattatreya
GD
Chandrasekhar
Srivari
S
Chandrashekar
Gudise
G
Reddy
Marepally Srinivasa
MS
Jagannadh
Bulusu
B
D000409:Alanine / Q000737:chemistry*; D002241:Carbohydrates / Q000737:chemistry*; D003198:Computer Simulation; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008968:Molecular Conformation; D010455:Peptides; D017550:Spectroscopy, Fourier Transform Infrared
D002241:Carbohydrates; D010455:Peptides; D000409:Alanine