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Expanding the Conformational Pool of cis-β-Sugar Amino Acid: Accommodation of β-hGly Motif in Robust 14-Helix
Tendencies of forming stable helices of heterooligomers composed of alternating rigid cis-β-sugar amino acid and flexible β-hGly motifs have been investigated, using a combination of molecular mechanics, CD, FT-IR, and NMR techniques. The results show that the solution structures of these oligomers...
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Published in: | Journal of the American Chemical Society 2005-07, Vol.127 (27), p.9664-9665 |
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Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Tendencies of forming stable helices of heterooligomers composed of alternating rigid cis-β-sugar amino acid and flexible β-hGly motifs have been investigated, using a combination of molecular mechanics, CD, FT-IR, and NMR techniques. The results show that the solution structures of these oligomers exist as robust right-handed 14-helices. Here, we examine the role of conformationally rigid cis-β-sugar amino acid in preorganizing the conformation of β-hGly to form the 14-helix. Our findings also show that a right-handed 14-helix can be formed with as few as four properly sequenced heterogeneous residues. These results represent the expansion of the conformational pool of sugar amino acid in the design of well-folded 14-helices, which can be used to develop β-peptides endowed with biological activity. |
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ISSN: | 0002-7863 1520-5126 |
DOI: | 10.1021/ja051014d |