Novel helical foldamers: organized heterogeneous backbone folding in 1 : 1 alpha/nucleoside-derived-beta-amino acid sequences

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 nuclei...

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Veröffentlicht in:Chemical communications (Cambridge, England) England), 2010-10, Vol.46 (37), p.6962-6964
Hauptverfasser: Chandrasekhar, Srivari, Kiranmai, Nayani, Kiran, Marelli Udaya, Devi, Ambure Sharada, Reddy, Gangireddy Pavan Kumar, Idris, Mohammed, Jagadeesh, Bharatam
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acids - chemistry
Molecular Conformation
Molecular Dynamics Simulation
Nucleosides - chemistry
Oligopeptides - chemistry
Protein Folding
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Zusammenfassung: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.
ISSN:1359-7345
1364-548X
DOI:10.1039/c0cc01724h