106429-38-3Relevant articles and documents
Inhibition and Dispersion of Bacterial Biofilms with 2-Aminobenzimidazole Derivatives
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Paragraph 0216; 0217; 0226; 0227, (2013/06/05)
Compounds described herein inhibit biofilm formation or disperse pre-formed biofilms of Gram-negative bacteria. Biofilm-inhibitory compounds can be encapsulated or contained in a polymer matrix for controlled release. Coatings, films, multilayer films, hydrogels, microspheres and nanospheres as well as pharmaceutical compositions and disinfecting compositions containing biofilm-inhibitory compounds are also provided. Methods for inhibiting formation of biofilms or dispersing already formed biofilms are provided. Methods for treating infections of gram-negative bacteria which form biofilms, particularly those of Pseudomonas and more particularly P. aeruginosa.
The chemical synthesis and antibiotic activity of a diverse library of 2-aminobenzimidazole small molecules against MRSA and multidrug-resistant A. baumannii
Huigens III, Robert W.,Reyes, Samuel,Reed, Catherine S.,Bunders, Cynthia,Rogers, Steven A.,Steinhauer, Andrew T.,Melander, Christian
supporting information; experimental part, p. 663 - 674 (2010/05/02)
Multidrug-resistant bacterial infections continue to be a rising global health concern. Herein is described the development of a class of novel 2-aminobenzimidazoles with antibiotic activity. These active 2-aminobenzimidazoles retain their antibiotic activity against several strains of multidrug-resistant Staphylococcus aureus and Acinetobacter baumannii when compared to susceptible strains.
Optimization of a coagulation factor VIIa inhibitor found in factor Xa inhibitor library
Sagi, Kazuyuki,Fujita, Koichi,Sugiki, Masayuki,Takahashi, Mitsuo,Takehana, Shunji,Tashiro, Kazumi,Kayahara, Takashi,Yamanashi, Masahiro,Fukuda, Yumiko,Oono, Seiji,Okajima, Akiko,Iwata, Seinosuke,Shoji, Masataka,Sakurai, Kuniya
, p. 1487 - 1496 (2007/10/03)
An inhibitor of the complex of factor VIIa and tissue factor (fVIIa/TF), 2-substituted-4-amidinophenylpyruvic acid 1a, was structurally modified with the aim of increasing its potency and selectivity. The lead compound 1a was originally found in our factor Xa (fXa) inhibitor library on the basis of structural similarity of the primary binding sites of fVIIa and fXa. The design was based on computational docking studies using the extracted active site of fVIIa. Compound 1j was found to inhibit factor VIIa/TF at nanomolar concentration with improved selectivity versus fXa and thrombin and it preferentially prolonged the clotting time in the TF-dependent extrinsic pathway.