858354-78-6Relevant articles and documents
Synthesis and antimicrobial activity of α-aminoboronic-containing peptidomimetics
Gozhina, Olga V.,Svendsen, John Sigurd,Lejon, Tore
, p. 20 - 24 (2014)
A library of 175 dipeptidomimetics and tripeptidomimetics containing an α-amino boronic acid or boronate has been synthesized, and the activity toward Mycobacterium tuberculosis, Candida albicans, Staphylococcus aureus, Streptococcus pyogenes, Escherichia coli and Pseudomonas aeruginosa has been screened. Although there is no clear structure-activity relationship, several compounds exhibit promising activity against different pathogens. Copyright
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.
scheme or table, 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.
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.