172348-68-4Relevant academic research and scientific papers
Binding cooperativity between a ligand carbonyl group and a hydrophobic side chain can be enhanced by additional H-bonds in a distance dependent manner: A case study with thrombin inhibitors
Said, Ahmed M.,Hangauer, David G.
, p. 405 - 424 (2015/05/05)
One of the underappreciated non-covalent binding factors, which can significantly affect ligand-protein binding affinity, is the cooperativity between ligand functional groups. Using four different series of thrombin inhibitors, we reveal a strong positiv
Dipeptide p-amidinobenzylamides with N-terminal sulfonyl or aminosulfonyl radicals
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, (2008/06/13)
Compounds of the formula I STR1 in which R1, A and B have the meanings stated in the description, and the preparation thereof are described. The novel compounds are suitable for controlling diseases.
D-Phe-Pro-p-amidinobenzylamine: A potent and highly selective thrombin inhibitor
Wiley, Michael R.,Chirgadze, Nickolay Y.,Clawson, David K.,Craft, Trelia J.,Gifford-Moore, Donetta S.,Jones, Noel D.,Olkowski, Jennifer L.,Weir, Leonard C.,Smith, Gerald F.
, p. 2387 - 2392 (2007/10/03)
The design, synthesis, and enzyme inhibitory profile of D-Phe-Pro-p-Amidinobenzylamine are presented. This compound has inhibitory activity equivalent to D-Phe-Pro-Arg-H, two orders of magnitude more potent than D-Phe-Pro-Agmatine. The results indicate that binding energy provided by the covalent bond of a transition-state analog can be replaced with noncovalent interactions.
