Observability limits for toponium at hadron colliders.
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Journal Article↗
Biomedical subjects
N Fabiano
Publications and source records attributed to N Fabiano.
A crystal-state, solution and theoretical study of the preferred conformation of linear C alpha, alpha-diphenylglycine derivatives and dipeptides with potential anticonvulsant activity.
Several linear molecules containing the C alpha, alpha-diphenylglycine residue were prepared as potential anticonvulsants. The conformational preferences of the C alpha, alpha-diphenylglycine residue were assessed in these synthetic derivatives and dipeptides by X-ray diffraction, FTIR absorption and 1H NMR techniques, and by conformational energy computations. Five (out of six) derivatives adopt the fully extended C5 conformation in the crystal state. This intramolecularly H-bonded form is largely populated in chloroform solution in all the derivatives investigated. Conformational energy computations in vacuo support the view that the intramolecularly H-bonded C7-ring form is the most stable structure for these compounds. Only one linear derivative exhibits a (modest) anticonvulsant activity.
Animals↗
Conformational versatility of the N alpha-acylated tripeptide amide tail of oxytocin. Synthesis and crystallographic characterization of three C2 alpha-backbone modified, conformationally restricted analogues.
The synthesis, physical and analytical characterization, and crystal-state structural analysis by X-ray diffraction of three analogues of the N alpha-acylated tripeptide amide tail of oxytocin, each containing a cyclic C alpha, alpha-disubstituted glycine at position 2, have been performed. The peptides are Boc-L-Pro-Ac3c-Gly-NH2, Z-L-Pro-Ac5c-Gly-NH2 and Z-L-Pro-Ac6c-Gly-NH2. While the former is folded in a type-II beta-turn conformation at the -L-Pro-Ac3c- sequence, the two latter tripeptides form two consecutive (type-II, type-I') beta-turns. The Ac5c- and Ac6c-tripeptides are the first examples of such a highly folded structural combination in a position-2 analogue of the N alpha-acylated -L-Pro-L-Leu-Gly-NH2 sequence.
Acylation↗