The Serine-Proline Turn: A Novel Hydrogen-Bonded Template for Designing Peptidomimetics.
- Resource Type
- Article
- Authors
- Song, Benben; Bomar, Martha G.; Kibler, Patrick; Kodukula, Krishna; Galande, Amit K.
- Source
- Organic Letters. Feb2012, Vol. 14 Issue 3, p732-735. 4p.
- Subject
- *HYDROGEN bonding
*SERINE
*PROLINE
*CHEMICAL templates
*PEPTIDOMIMETICS
*RING formation (Chemistry)
- Language
- ISSN
- 1523-7060
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. [ABSTRACT FROM AUTHOR]