Binaphthyl-anchored antibacterial tripeptide derivatives with hydrophobic C-terminal amino acid variations

• John B. Bremner,
• Paul A. Keller,
• Stephen G. Pyne,
• Mark J. Robertson,
• K. Sakthivel,
• Kittiya Somphol,
• Dean Baylis,
• Jonathan A. Coates,
• John Deadman,
• Dharshini Jeevarajah and
• David I. Rhodes

Beilstein J. Org. Chem. 2012, 8, 1265–1270, doi:10.3762/bjoc.8.142

• and Enterococci (VRE, VSE), and against Staphylococcus epidermidis. Keywords: antibacterials; binaphthyls; cationic peptides; peptides; resistance; VISA; VRE; Introduction Among the most pressing challenges in current healthcare is the resistance of bacterial human pathogenic organisms to

• promising initial activity profile, the tripeptide derivative 2c was subjected to further evaluation (Table 2). It was tested against methicillin-sensitive (MSSA), methicillin-resistant (MRSA) and vancomycin-intermediate (VISA) S. aureus, S. epidermis and vancomycin-resistant (VRE) and vancomycin-sensitive

• MSSA, MRSA, VISA and VRE organisms. Our results confirmed the positive contribution to good Gram-positive antibacterial activity, engendered by filling of a hydrophobic area close to the C-terminus of these acyclic tripeptide derivatives. Experimental General notes were those detailed previously in the