Incorporation of Ahc into model dipeptides as an inducer of a beta-turn with a distorted amide bond. Conformational analysis.
The proline residue of dipeptides Ser-Pro and Pro-Ser has been replaced by 7-azabicyclo[2.2.1]heptane-1-carboxylic acid (Ahc), a conformationally restricted analogue of proline that is capable of mimicking distorted amides. The conformational analysis of the new peptides in the solid state revealed that the Ahc-Ser sequence displays a type I beta-turn, which includes a distorted amide bond. In contrast, the Ser-Ahc sequence exists in a nonfolded structure.
Avenoza
Alberto
A
Departamento de Química, Universidad de La Rioja, Grupo de Síntesis Química de La Rioja, U.A.-C.S.I.C., 26006 Logroño, Spain. alberto.avenoza@dq.unirioja.es
Busto
Jesús H
JH
Peregrina
Jesús M
JM
Rodríguez
Fernando
F
D019086:Bridged Bicyclo Compounds, Heterocyclic / Q000737:chemistry*; D002264:Carboxylic Acids / Q000737:chemistry*; D002384:Catalysis; D002855:Chromatography, Thin Layer; D004151:Dipeptides / Q000138:chemical synthesis* / Q000737:chemistry; D004952:Esters / Q000138:chemical synthesis / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D015394:Molecular Structure; D011392:Proline / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012694:Serine / Q000737:chemistry*; D014961:X-Ray Diffraction
C410425:7-Azabicycloheptane carboxylic acid; D019086:Bridged Bicyclo Compounds, Heterocyclic; D002264:Carboxylic Acids; D004151:Dipeptides; D004952:Esters; C465982:prolyl-serine; C465983:seryl-proline; D012694:Serine; D011392:Proline