A new approach to conformationally restricted peptide analogs: Rigid β-bends. 1. Enkephalin as an example
Autor: | Bruce L. Currie, John L. Krstenansky, R. L. Baranowski |
---|---|
Rok vydání: | 1982 |
Předmět: |
Models
Molecular Enkephalin Protein Conformation Stereochemistry Enkephalin Methionine Guinea Pigs Biophysics Peptide Ring (chemistry) Biochemistry Structure-Activity Relationship chemistry.chemical_compound Ileum Side chain Animals Guinea pig ileum Molecular Biology Pyrrole chemistry.chemical_classification Enkephalins Cell Biology Amino acid chemistry Biological Assay Enkephalin Leucine Muscle Contraction |
Zdroj: | Biochemical and Biophysical Research Communications. 109:1368-1374 |
ISSN: | 0006-291X |
DOI: | 10.1016/0006-291x(82)91928-3 |
Popis: | A means of producing a peptide analogue that is permanently fixed in a β-bend conformation has been devised. These analogues are based on appropriately substituted derivatives of the ring system, 5H-6-oxo-2,3,4,4a,7,7a-hexahydropyrano [2,3,-b]pyrrole. The substituents are chosen to represent the relevant side chains of amino acids. The first analogue of this type of enkephalin has been synthesized and was found to have the same order of magnitude of activity in the guinea pig ileum assay as morphine. |
Databáze: | OpenAIRE |
Externí odkaz: |