Kahne D, Leimkuhler C, Lu W, Walsh C (2005) Glycopeptide and lipoglycopeptide antibiotics. Chem Rev 105:425–448. https://doi.org/10.1021/cr030103a
Article CAS PubMed Google Scholar
McComas CC, Crowley BM, Boger DL (2003) Partitioning the loss in vancomycin binding affinity for D-Ala-D-Lac into lost H-bond and repulsive lone pair contributions. J Am Chem Soc 125:9314–9315. https://doi.org/10.1021/ja035901x
Article CAS PubMed Google Scholar
Sarkar P, Yarlagadda V, Ghosh C, Haldar J (2017) A review on cell wall synthesis inhibitors with an emphasis on glycopeptide antibiotics. Medchemcomm. 8:516–533. https://doi.org/10.1039/C6MD00585C
Article CAS PubMed PubMed Central Google Scholar
Dhanda G, Sarkar P, Samaddar S, Haldar J (2018) Battle against vancomycin-resistant bacteria: recent developments in chemical strategies. J Med Chem 62:3184–3205. https://doi.org/10.1021/acs.jmedchem.8b01093
Article CAS PubMed Google Scholar
Acharya Y, Dhanda G, Sarkar P, Haldar J (2022) Pursuit of next-generation glycopeptides: a journey with vancomycin. Chem Commun 58:1881–1897. https://doi.org/10.1039/D1CC06635H
Kociolek LK, Gerding DN (2016) Breakthroughs in the treatment and prevention of Clostridium difficile infection. Nat Rev Gastroenterol Hepatol 13:150–160. https://doi.org/10.1038/nrgastro.2015.220
Article CAS PubMed Google Scholar
Jenkins C, Meyer D, Dreyfus M, Larreu MJ (1974) Willebrand factor and ristocetin I. Mechanism of ristocetin-induced platelet aggregation. Br J Haematol 28:561–578. https://doi.org/10.1111/j.1365-2141.1974.tb06675.x
Article CAS PubMed Google Scholar
Meyer D, Jenkins C, Dreyflis M, Fressinaud E, Lariueu MJ (1974) Willebrand factor and ristocetin II. Relationship between willebrand factor, willebrand antigen and factor-VIII activity. Br J Haematol 28:579–599. https://doi.org/10.1111/j.1365-2141.1974.tb06676.x
Article CAS PubMed Google Scholar
Bager F et al (1997) Avoparcin used as a growth promoter is associated with the occurrence of vancomycin-resistant Enterococcus faecium on Danish poultry and pig farms. Prev Vet Med 31:95–112. https://doi.org/10.1016/S0167-5877(96)01119-1
Article CAS PubMed Google Scholar
Nicolaou K, Boddy CN, Bräse S, Winssinger N (1999) Chemistry, biology, and medicine of the glycopeptide antibiotics. Angew Chem 38:2096–2152. https://doi.org/10.1002/(SICI)1521-3773(19990802)38:15%3C2096::AID-ANIE2096%3E3.0.CO;2-F
Griffith RSJJOAC (1984) Vancomycin use—an historical review. J Antimicrob Chemother 14:1–5. https://doi.org/10.1093/jac/14.suppl_D1
Article CAS PubMed Google Scholar
Blaskovich MA, Hansford KA, Butler MS, Jia Z, Mark AE, Cooper MA (2018) Developments in glycopeptide antibiotics. ACS Infect Dis 4:715–735. https://doi.org/10.1021/acsinfecdis.7b00258
Article CAS PubMed PubMed Central Google Scholar
Williams DH, Kalman JR (1977) Structural and mode of action studies on the antibiotic vancomycin. Evidence from 270-MHz proton magnetic resonance. J Am Chem Soc 99:2768–2774. https://doi.org/10.1021/ja00450a058
Article CAS PubMed Google Scholar
Barna J, Williams DH (1984) The structure and mode of action of glycopeptide antibiotics of the vancomycin group. Ann Rev Microbiol 38:339–357
Westwell MS, Bardsley B, Dancer RJ, Try AC, Williams DH (1996) Cooperativity in ligand binding expressed at a model cell membrane by the vancomycin group antibiotics. Chem Commun 5:589–590. https://doi.org/10.1039/cc9960000589
Mackay JP et al (1994) Glycopeptide antibiotic activity and the possible role of dimerization: a model for biological signaling. J Am Chem Soc 116:4581–4590. https://doi.org/10.1021/ja00090a006
Groves P, Searle MS, Mackay JP, Williams DH (1994) The structure of an asymmetric dimer relevant to the mode of action of the glycopeptide antibiotics. Structure 2:747–754. https://doi.org/10.1016/s0969-2126(94)00075-1
Article CAS PubMed Google Scholar
Mackay JP, Gerhard U, Beauregard DA, Maplestone RA, Williams DH (1994) Dissection of the contributions toward dimerization of glycopeptide antibiotics. J Am Chem Soc 116:4573–4580. https://doi.org/10.1021/ja00090a005
Kannan R, Harris CM, Harris TM, Waltho JP, Skelton NJ, Williams DH (1988) Function of the amino sugar and N-terminal amino acid of the antibiotic vancomycin in its complexation with cell wall peptides. J Am Chem Soc 110:2946–2953. https://doi.org/10.1021/ja00217a042
Butler MS, Blaskovich MA, Cooper MA (2013) Antibiotics in the clinical pipeline in 2013. J Antibiot 66:571–591
Beauregard DA, Williams DH, Gwynn MN (1995) Knowles Dimerization and membrane anchors in extracellular targeting of vancomycin group antibiotics. Antimicrob Agents Chemother 39:781–785. https://doi.org/10.1128/aac.39.3.781
Article CAS PubMed PubMed Central Google Scholar
Economou NJ et al (2013) Structure of the complex between teicoplanin and a bacterial cell-wall peptide: use of a carrier-protein approach. Acta Cryst 69:520–533. https://doi.org/10.1107/S0907444912050469
Barna JC, Williams DH, Williamson MP (1985) Structural features that affect the binding of teicoplanin, ristocetin A, and their derivatives to the bacterial cell-wall model N-acetyl-D-alanyl-D-alanine. J Chem Soc Chem Commun. https://doi.org/10.1039/c39850000254
Charneski L, Patel PN, Sym DJAOP (2009) Telavancin: a novel lipoglycopeptide antibiotic. Ann Pharmacother 43:928–938. https://doi.org/10.1345/aph.1G417
Article CAS PubMed Google Scholar
Higgins DL, Chang R, Debabov DV (2005) Telavancin, a multifunctional lipoglycopeptide, disrupts both cell wall synthesis and cell membrane integrity in methicillin-resistant Staphylococcus aureus. Antimicrob Agents Chemother 49:1127–1134. https://doi.org/10.1128/aac.49.3.1127-1134.2005
Article CAS PubMed PubMed Central Google Scholar
Karlowsky JA, Nichol K, Zhanel GG (2015) Telavancin: mechanisms of action, in vitro activity, and mechanisms of resistance. Clin Infect Dis 61:S58–S68. https://doi.org/10.1093/cid/civ534
Article CAS PubMed Google Scholar
Leadbetter MR, Adams SM, Bazzini B (2004) Hydrophobic vancomycin derivatives with improved ADME properties discovery of telavancin (TD-6424). J Antibiot 57:326–336. https://doi.org/10.7164/antibiotics.57.326
Judice JK, Pace JL (2003) Semi-synthetic glycopeptide antibacterials. Biorg Med Chem Lett 13:4165–4168. https://doi.org/10.1016/j.bmcl.2003.08.067
Lunde CS et al (2009) Telavancin disrupts the functional integrity of the bacterial membrane through targeted interaction with the cell wall precursor lipid II. Antimicrob Agents Chemother 53:3375–3383. https://doi.org/10.1128/aac.01710-08
Article CAS PubMed PubMed Central Google Scholar
Pfaller M, Rhomberg P, Sader H, Mendes R, Jones RN (2010) Telavancin activity against Gram-positive bacteria isolated from patients with skin and skin-structure infections. J Chemother 22:304–311. https://doi.org/10.1179/joc.2010.22.5.304
Article CAS PubMed Google Scholar
Malabarba A, Goldstein BP (2005) Origin, structure, and activity in vitro and in vivo of dalbavancin. J Antimicrob Chemother 55:ii15–ii20. https://doi.org/10.1093/jac/dki005
Article CAS PubMed Google Scholar
Pace JL, Krause K, Johnston D (2003) In vitro activity of TD-6424 against Staphylococcus aureus. Antimicrob Agents Chemother 47:3602–3604. https://doi.org/10.1128/aac.47.11.3602-3604.2003
Article CAS PubMed PubMed Central Google Scholar
Economou NJ, Nahoum V, Weeks SD (2012) A carrier protein strategy yields the structure of dalbavancin. J Am Chem Soc 134:4637–4645. https://doi.org/10.1128/aac.47.11.3602-3604.2003
Article CAS PubMed PubMed Central Google Scholar
Lu W, Oberthür M, Leimkuhler C, Tao J, Kahne D, Walsh CT (2004) Characterization of a regiospecific epivancosaminyl transferase GtfA and enzymatic reconstitution of the antibiotic chloroeremomycin. PNAS 101:4390–4395. https://doi.org/10.1073/pnas.0400277101
Article CAS PubMed PubMed Central Google Scholar
Bouza E, Burillo A (2010) Oritavancin: a novel lipoglycopeptide active against Gram-positive pathogens including multiresistant strains. Int J Antimicrob Agents 36:401–407.
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