110769-86-3Relevant articles and documents
A formyl peptide substituted with a conformationally constrained phenylalanine residue evokes a selective immune response in human neutrophils
Hayashi, Ryo,Miyazaki, Masaya,Osada, Satoshi,Kawasaki, Hiroshi,Fujita, Ichiro,Hamasaki, Yuhei,Kodama, Hiroaki
supporting information, p. 668 - 675 (2013/02/25)
Formyl-Met-Leu-Phe-OH (fMLP) binds to formyl peptide receptors, FPR1 and FPR2, and evokes migration and superoxide anion production in human neutrophils. To obtain a more effective and selective ligand, fMLP analogs in which the Phe residue was substitute
PEPTIDYL NITRILES AND USE THEREOF AS DIPEPTIDYL PEPTIDASE I INHIBITORS
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Page/Page column 62, (2009/07/17)
The present invention provides compounds of formula (I) in which n, y, X1, X2, A, B, R1, R2, R3, R4 and R5 are as defined in the specification, a process for their preparation, pharmaceutical compositions containing them and their use as dipeptidyl peptidase I (DPPI) inhibitors.
Preparation of dipeptoid mimetics for the tetrapeptide cholecystokinin, CCK(30-33)
Walford,Campbell,Horwell
, p. 188 - 191 (2007/10/03)
The diastereoselective synthesis of 2,3-methanophenylalanine methyl esters (5) has been achieved in 58% yield. The preparation of the dehydropeptides (1, R = Me; 2, R = H) and the cyclopropylpeptides (3, R = Me; 4, R = H) possessing good binding affinities for the CCK-A and CCK-B receptors is described. Conformational studies of the dipeptide esters 1 and 3 indicated the presence of a β-turn within the peptide backbone, although there was no preference in type. The Phe and Trp moieties, however, did prefer to be situated on the same side of the peptide turn which is favourable for receptor binding.
