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.
A glycopeptide dendrite inhibitor of the galactose-specific lectin LecA and of Pseudomonas Aeruginosa biofilm / R. U. Kadam; M. Bergmann; M. Hurley; D. Garg; M. Cacciarini; M. A. Swiderska; C. Nativi; M. Sattler; A. R. Smith; P. Williams; M. Càmara; A. Stocker; T. Darbre; J. L. Reymond. - In: ANGEWANDTE CHEMIE. INTERNATIONAL EDITION. - ISSN 1433-7851. - STAMPA. - 50:(2011), pp. 10613-10635. [10.1002/anie.201104342]
A glycopeptide dendrite inhibitor of the galactose-specific lectin LecA and of Pseudomonas Aeruginosa biofilm
CACCIARINI, MARTINA;NATIVI, CRISTINA;
2011
Abstract
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.
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