170701-10-7Relevant academic research and scientific papers
Structure-activity relationships of the peptide deformylase inhibitor BB-3497: Modification of the P2′ and P3′ side chains
Davies, Stephen J.,Ayscough, Andrew P.,Beckett, R. Paul,Clements, John M.,Doel, Sheila,Pratt, Lisa M.,Spavold, Zoe M.,Thomas, S. Wayne,Whittaker, Mark
, p. 2715 - 2718 (2007/10/03)
Structural modifications to the peptide deformylase inhibitor BB-3497 are described. In this paper, we describe the initial SAR around this lead for modifications to both the P2′ and P3′ side chains. Enzyme inhibition and antibacterial activity data revealed that a variety of substituents are tolerated at the P2′ and P3′ positions of the inhibitor backbone. The data from this study highlights the potential for modification at the P2′ and P3′ positions to optimise the physicochemical properties.
Synthesis of 6, desGly10>GnRH-Et without Side-Chain Protection
Masiukiewicz, E.,Rzeszotarska, B.,Wiejak, S.
, p. 674 - 680 (2007/10/02)
A gonadoliberin superagonist, 6, desGly1>GnRH-Et* (5), was obtained in solution by connecting segments, Glp-His-Trp-Ser-Tyr-N2H3 (1) and Z-DSer(tBu)-LeuArg(AcOH)-Pro-NHEt (4) (Scheme 1), which were produced witho
