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
Design and synthesis of dipeptidyl nitriles as potent, selective, and reversible inhibitors of cathepsin C
Guay, Daniel,Beaulieu, Christian,Jagadeeswar Reddy,Zamboni, Robert,Methot, Nathalie,Rubin, Joel,Ethier, Diane,David Percival
scheme or table, p. 5392 - 5396 (2010/05/02)
A series of dipeptide nitriles with a thienyl alanine in P2 were identified as potent and selective cathepsin C inhibitors. Incorporation of a substituted cyclopropyl moiety in P1 effectively protects these derivatives against hydrolase activity in whole blood.
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.