182618-33-3Relevant articles and documents
Design and synthesis of Fmoc-SPPS-ready iodoarene amino acid pre-catalysts and their reactivity in the catalytic oxytosylation of ketones
Brummel, Beau R.,Giambalvo, Lauren N.,Gross, Kristopher G.,Kobra, Khadijatul,Lex, Timothy R.,McMillen, Colin D.,Panda, Soham,Pennington, William T.,Swasy, Maria I.,Whitehead, Daniel C.
supporting information, (2020/02/22)
A small suite of iodo-aryl amide containing amino acids were synthesized and assessed as catalysts for the hypervalent iodine(III) mediated α-oxytosylation of ketones. The efficiency of each catalyst was determined by comparing the relative rates of catalysis in the direct α-oxytosylation of propiophenone. In addition, these catalysts can be easily converted to congeners that are suitable for Fmoc-solid phase peptide synthesis for facile incorporation into a chiral peptide framework. This work facilitates the broader goal of our program to develop peptide-based enantioselective catalysts for hypervalent iodine chemistry.
Sulfonylaminovalerolactams and derivatives thereof as factor Xa inhibitors
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Page/Page column 41, (2008/06/13)
The present application describes sulfonylaminovalerolactams and derivatives thereof of Formula I: or pharmaceutically acceptable salt forms thereof, wherein ring G is a mono- or bicyclic carbocycle or heterocycle. Compounds of the present invention are useful as inhibitors of trypsin-like serine proteases, specifically factor Xa.
Modification of receptor selectivity and functional activity of cyclic cholecystokinin analogues
Amblard, Muriel,Rodriguez, Marc,Lignon, Marie-Francoise,Galas, Marie-Christine,Bernad, Nicole,Aumelas, Andre,Martinez, Jean
, p. 171 - 180 (2007/10/03)
We reported earlier on the synthesis and biological activity at the CCK-B receptor of cyclized derivatives of CCK. These peptides, in which the positions 28 and 31 were replaced by lysine residues, were bridged by a succinyl moiety. To determine the importance of the nature and size of the cyclic structure, cyclic analogues were synthesized in which: (i) the lysine residues were replaced by ornithine and diaminobutyric acid and (ii) the succinic moiety was replaced by a malonic, adipic and glutaric moiety. They were tested For their ability to inhibit the specific binding of 125I-BH-CCK-8 to CCK receptors in rat pancreatic acini and guinea pig brain membranes. They were also evaluated for their ability to stimulate amylase secretion from rat pancreatic acini. The potency and selectivity of these analogues were compared with those obtained with CCK-4 and compound JIMV320, a potent and selective CCK-B receptor ligand synthesized earlier in our laboratory.