Coordination chemistry of peptides. Part II. Crystal structure of cyclo-L-methionylglycine and studies of metal complexation.
The structure of the title compound displays a nearly planar diketopiperazine ring. The side chain is folded on the ring, the S atom making a significantly short contact with the methionine carbonyl atom. The crystal packing shows an unusual assembly of alternating layers of peptide and crystallization water molecules. The side chain sulfur atom is found to be the primary site for metal coordination of the ligand, while in some systems there is evidence of additional coordination through deprotonated amide nitrogens.
D004151:Dipeptides / Q000138:chemical synthesis; D006046:Gold; D007202:Indicators and Reagents; D009682:Magnetic Resonance Spectroscopy; D008628:Mercury; D008670:Metals; D008958:Models, Molecular; D009904:Optical Rotation; D010165:Palladium; D010984:Platinum; D011485:Protein Binding; D011487:Protein Conformation; D013053:Spectrophotometry; D014961:X-Ray Diffraction
D004151:Dipeptides; D007202:Indicators and Reagents; D008670:Metals; D010984:Platinum; D010165:Palladium; C035582:cyclo-methionylglycine; D006046:Gold; D008628:Mercury