Chiral recognition of dipeptides in a biomembrane model.
Chiral recognition of the enantiomeric couples of ditryptophan and diphenylalanine was observed by (1)H NMR spectroscopy in micelles formed by sodium N-dodecanoyl-L-prolinate. Ditryptophan showed a selective association with the Z domains of the amidic aggregates, whereas diphenylalanine did not show any selectivity in the association. Partition coefficients between water and aggregates were evaluated by diffusion NMR experiments. Intramolecular distances of ditryptophan isomers associated with chiral aggregates were obtained by ROESY experiments and were used as constraints in molecular mechanics calculations. From these calculations, information on the conformation of the peptides in the chiral aggregates was obtained.
IMC-Sezione Meccanismi di Reazione, CNR, c/o Dipartimento di Chimica, Università La Sapienza, Roma, Italy.
Cecilia
C
Bombelli
Stefano
S
Borocci
Federica
F
Lupi
Giovanna
G
Mancini
Luisa
L
Mannina
Anna Laura
AL
Segre
Stéphane
S
Viel
D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism; D004151:Dipeptides / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D008567:Membranes, Artificial; D008823:Micelles; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D010649:Phenylalanine / Q000737:chemistry / Q000378:metabolism; D011392:Proline / Q000031:analogs & derivatives / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D013237:Stereoisomerism; D013816:Thermodynamics; D014364:Tryptophan / Q000737:chemistry / Q000378:metabolism
D004151:Dipeptides; D008567:Membranes, Artificial; D008823:Micelles; D010649:Phenylalanine; D014364:Tryptophan; D011392:Proline