304439-23-4Relevant articles and documents
Molecular recognition studies on naphthyridine derivatives
Iglesias-Sanchez, Jose Carlos,Maria, Dolores Santa,Claramunt, Rosa M.,Elguero, Jose
, p. 1213 - 1222 (2010)
The association constants Kb of three hosts I-III designed to have both enhanced hydrogen bonding donor strength and conformational preorganization with biotin analogues 1-5 are reported. 1H-NMR titrations under two different concent
Triazole biotin: A tight-binding biotinidase-resistant conjugate
Germeroth, Anne I.,Hanna, Jill R.,Karim, Rehana,Kundel, Franziska,Lowther, Jonathan,Neate, Peter G. N.,Blackburn, Elizabeth A.,Wear, Martin A.,Campopiano, Dominic J.,Hulme, Alison N.
, p. 7700 - 7704 (2013)
The natural amide bond found in all biotinylated proteins has been replaced with a triazole through CuAAC reaction of an alkynyl biotin derivative. The resultant triazole-linked adducts are shown to be highly resistant to the ubiquitous hydrolytic enzyme biotinidase and to bind avidin with dissociation constants in the low pM range. Application of this strategy to the production of a series of biotinidase-resistant biotin-Gd-DOTA contrast agents is demonstrated. The Royal Society of Chemistry 2013.
Biotin analogues with antibacterial activity are potent inhibitors of biotin protein ligase
Soares Da Costa, Tatiana P.,Tieu, William,Yap, Min Y.,Zvarec, Ondrej,Bell, Jan M.,Turnidge, John D.,Wallace, John C.,Booker, Grant W.,Wilce, Matthew C. J.,Abell, Andrew D.,Polyak, Steven W.
, p. 509 - 514 (2012/08/14)
There is a desperate need to develop new antibiotic agents to combat the rise of drug-resistant bacteria, such as clinically important Staphylococcus aureus. The essential multifunctional enzyme, biotin protein ligase (BPL), is one potential drug target f