Novel helical foldamers: organized heterogeneous backbone folding in 1 : 1 alpha/nucleoside-derived-beta-amino acid sequences.
Secondary structural conformation of hybrid oligo-peptides comprised of 1 : 1 alternating Nucleoside Derived beta-Amino acid (NDA) and l-amino acid residues has been reported. The studies reveal that the NDA residues organize the heterogeneous backbone featuring the surface properties of both nucleic acids and peptides, to adopt a novel 11/8-helical fold.
Chandrasekhar
Srivari
S
Organic Division-I, Indian Institute of Chemical Technology (CSIR), Uppal Road, Tarnaka, Hyderabad-500 607 (AP), India. srivaric@iict.res.in
Kiranmai
Nayani
N
Kiran
Marelli Udaya
MU
Devi
Ambure Sharada
AS
Reddy
Gangireddy Pavan Kumar
GP
Idris
Mohammed
M
Jagadeesh
Bharatam
B
D000596:Amino Acids / Q000737:chemistry*; D008968:Molecular Conformation; D056004:Molecular Dynamics Simulation; D009705:Nucleosides / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry*; D017510:Protein Folding
D000596:Amino Acids; D009705:Nucleosides; D009842:Oligopeptides