A Glycopeptide Dendrimer Inhibitor of the Galactose-Specific Lectin LecA and of Pseudomonas aeruginosa Biofilms

被引:150
作者
Kadam, Rameshwar U. [1 ]
Bergmann, Myriam [1 ]
Hurley, Matthew [2 ,3 ]
Garg, Divita [4 ,5 ]
Cacciarini, Martina [6 ]
Swiderska, Magdalena A. [1 ]
Nativi, Cristina [6 ]
Sattler, Michael [4 ,5 ]
Smyth, Alan R. [3 ]
Williams, Paul [2 ]
Camara, Miguel [2 ]
Stocker, Achim [1 ]
Darbre, Tamis [1 ]
Reymond, Jean-Louis [1 ]
机构
[1] Univ Bern, Dept Chem & Biochem, CH-3012 Bern, Switzerland
[2] Univ Nottingham, Sch Mol Med Sci, Nottingham NG7 2UH, England
[3] Univ Nottingham, Sch Clin Sci, Nottingham NG7 2UH, England
[4] Tech Univ Munich, Inst Biol Struct, Helmholtz Zentrum Munchen, D-85747 Garching, Germany
[5] Tech Univ Munich, Ctr Integrated Prot Sci Munich, Dept Chem, D-85747 Garching, Germany
[6] Univ Florence, Dipartimento Chim Polo Sci & Tecnol, I-50019 Sesto Fiorentino, Firenze, Italy
基金
英国惠康基金;
关键词
biofilms; dendrimers; glycopeptides; lectins; multivalency; STRUCTURAL BASIS; PA-IL; BACTERIAL LECTIN; HIGH-AFFINITY; BINDING; RECOGNITION; ADHESION;
D O I
10.1002/anie.201104342
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Inhibiting factors: Biofilm inhibition is achieved with a phenylgalactosyl peptide dendrimer (see picture) that binds to the galactose-specific lectin LecA of P. aeruginosa. The multivalency of the ligands is critical for biofilm inhibition, although the nature of the linker between the peptide dendrimer and the galactose can provide additional contacts to the lectin and also has an effect on the interaction. Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
引用
收藏
页码:10631 / 10635
页数:5
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