116662-96-5Relevant articles and documents
Antibiotic N′,N″-dibenzyleremomycin with a reduced 1,2-peptide bond
Printsevskaya,Olsuf'eva,Lazhko,Preobrazhenskaya
, p. 65 - 73 (2002)
Eremomycin derivatives with benzylated amino groups of both residues of eremosamine and with (R) or (S)-2-amino-4-methylpentyl substituted for N-methyl-D-Leu, the first amino acid residue of its heptapeptide, were synthesized in order to study the role of
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
Deglycobleomycin A6 analogues modified in the methylvalerate moiety
Cai, Xiaoqing,Zaleski, Paul A.,Cagir, Ali,Hecht, Sidney M.
, p. 3831 - 3844 (2011/08/02)
Previous studies have indicated that the methylvalerate subunit of bleomycin (BLM) plays an important role in facilitating DNA cleavage by BLM and deglycoBLM. Eleven methylvalerate analogues have been synthesized and incorporated into deglycoBLM congeners by the use of solid-phase synthesis. The effect of the valerate moiety in the deglycoBLM analogues has been studied by comparison with the parent deglycoBLM A5 using supercoiled DNA relaxation and sequence-selective DNA cleavage assays. All of the deglycoBLM analogues were found to effect the relaxation of the plasmid DNA. Those analogues having aromatic C4-substituents exhibited cleavage efficiency comparable to that of deglycoBLM A5. Some, but not all, of the deglycoBLM analogues were also capable of mediating sequence-selective DNA cleavage.