919103-31-4Relevant academic research and scientific papers
BETA-LACTAMASE INHIBITORS
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, (2013/04/25)
Disclosed herein inter alia are Boron containing compounds and methods for treating infections related to antibiotic resistant microorganisms.
Structure guided development of potent reversibly binding penicillin binding protein inhibitors
Woon, Esther C. Y.,Zervosen, Astrid,Sauvage, Eric,Simmons, Katie J.,Zivec, Matej,Inglis, Steven R.,Fishwick, Colin W. G.,Gobec, Stanislav,Charlier, Paulette,Luxen, Andre,Schofield, Christopher J.
, p. 219 - 223 (2011/04/26)
Following from the evaluation of different types of electrophiles, combined modeling and crystallographic analyses are used to generate potent boronic acid based inhibitors of a penicillin binding protein. The results suggest that a structurally informed approach to penicillin binding protein inhibition will be useful for the development of both improved reversibly binding inhibitors, including boronic acids, and acylating inhibitors, such as β-lactams.
Crystal structure of a complex between the actinomadura R39 dd -peptidase and a peptidoglycan-mimetic boronate inhibitor: Interpretation of a transition state analogue in terms of catalytic mechanism
Dzhekieva, Liudmila,Rocaboy, Mathieu,Kerff, Frederic,Charlier, Paulette,Sauvage, Eric,Pratt
, p. 6411 - 6419 (2011/04/16)
The Actinomadura R39 dd-peptidase is a bacterial low molecular weight class C penicillin-binding protein. It has previously been shown to catalyze hydrolysis and aminolysis of small d-alanyl-d-alanine terminating peptides, especially those with a side cha
Expanding the scope of PNA-encoded libraries: divergent synthesis of libraries targeting cysteine, serine and metallo-proteases as well as tyrosine phosphatases
Debaene, Fran?ois,Da Silva, Julien A.,Pianowski, Zbigniew,Duran, Fernando J.,Winssinger, Nicolas
, p. 6577 - 6586 (2008/02/05)
Seven PNA-encoded combinatorial libraries targeting proteases and phosphatases with covalent reversible and irreversible mechanism-based inhibitors were prepared. The libraries were synthesized using modified PNA monomers, which dramatically increase the water solubility of the libraries in biologically relevant buffers. The libraries were shown to selectively inhibit targeted enzymes.
Boro-norleucine as a P1 residue for the design of selective and potent DPP7 inhibitors
Shreder, Kevin R.,Wong, Melissa S.,Corral, Sergio,Yu, Zhizhou,Winn, David T.,Wu, Min,Hu, Yi,Nomanbhoy, Tyzoon,Alemayehu, Senaiet,Fuller, Stacy R.,Rosenblum, Jonathan S.,Kozarich, John W.
, p. 4256 - 4260 (2007/10/03)
Dipeptide-based inhibitors with C-substituted (alkyl or aminoalkyl) α-amino acids in the P2 position and boro-norleucine (boro-Nle) in the P1 position were synthesized. Relative to boro-proline, boro-Nle as a P1 residue was shown able to significantly dial out DPP4, FAP, DPP8, and DPP9 activity. Dab-boro-Nle (4g) proved to be the most selective and potent DPP7 inhibitor with a DPP7 IC50 value of 480 pM.
