617688-33-2Relevant academic research and scientific papers
Novel antibiotics: C-2 symmetrical macrocycles inhibiting Holliday junction DNA binding by E. coli RuvC
Pan, Po-Shen,Curtis, Fiona A.,Carroll, Chris L.,Medina, Irene,Liotta, Lisa A.,Sharples, Gary J.,McAlpine, Shelli R.
, p. 4731 - 4739 (2007/10/03)
Holliday junctions (HJs) are formed as transient DNA intermediates during site-specific and homologous recombination. Both of these genetic exchange pathways are critical for normal DNA metabolism and repair. Trapping HJs leads to bacterial cell death by
A progressive synthetic strategy for class B synergimycins
Robinson, Jennifer L.,Taylor, Rachel E.,Liotta, Lisa A.,Bolla, Megan L.,Azevedo, Enrique V.,Medina, Irene,McAlpine, Shelli R.
, p. 2147 - 2150 (2007/10/03)
Described are the syntheses of four macrocyclic peptides that are the core structure of class B synergimycins, and the synthesis of a final class B derivative. Our synthetic route to these synergimycin derivatives allows the incorporation of amino acid su
Novel antibiotics: Second generation macrocyclic peptides designed to trap Holliday junctions
Liotta, Lisa A.,Medina, Irene,Robinson, Jennifer L.,Carroll, Chris L.,Pan, Po-Shen,Corral, Ricardo,Johnston, Jennifer V.C.,Cook, Kristina M.,Curtis, Fiona A.,Sharples, Gary J.,McAlpine, Shelli R.
, p. 8447 - 8450 (2007/10/03)
Described are the syntheses of 15 macrocyclic peptides designed to trap Holliday junctions (HJs) in bacteria during site-specific and homologous recombination. This leads to inhibiting bacterial growth. These second generation macrocycles were based on th
Novel antibiotics: macrocyclic peptides designed to trap Holliday junctions.
Bolla, Megan L,Azevedo, Enrique V,Smith, Jason M,Taylor, Rachel E,Ranjit, Dev K,Segall, Anca M,McAlpine, Shelli R
, p. 109 - 112 (2007/10/03)
[reaction: see text] Described are the syntheses of eight macrocyclic peptides designed to trap Holliday junctions in bacteria, thereby inhibiting bacterial growth. These macrocycles were designed from linear dimerized hexapeptides that bind to the C-2 sy
