The Serine-Proline Turn: A Novel Hydrogen-Bonded Template for Designing Peptidomimetics

The Serine-Proline Turn: A Novel Hydrogen-Bonded Template for Designing Peptidomimetics

Serine-Proline (SP) dipeptide motifs have been shown to form unique hydrogen-bonding patterns in protein crystal structures. Peptides were designed to mimic these patterns by forming the 6 + 10 and the 9 + 10 hydrogen-bonded rings. Factors that contribute to the formation of SP turns include control...

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Veröffentlicht in:Organic letters 2012-02, Vol.14 (3), p.732-735
Hauptverfasser: Song, Benben, Bomar, Martha G, Kibler, Patrick, Kodukula, Krishna, Galande, Amit K
Format: Artikel
Sprache:eng
Schlagworte:
Hydrogen Bonding
Models, Molecular
Molecular Conformation
Peptidomimetics - chemistry
Proline - chemistry
Serine - chemistry
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Zusammenfassung:Serine-Proline (SP) dipeptide motifs have been shown to form unique hydrogen-bonding patterns in protein crystal structures. Peptides were designed to mimic these patterns by forming the 6 + 10 and the 9 + 10 hydrogen-bonded rings. Factors that contribute to the formation of SP turns include controlling backbone flexibility and amino acid chirality along with creating a hydrophobic environment around the intramolecular hydrogen bonds.
ISSN:1523-7060
1523-7052
DOI:10.1021/ol203272k