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Self-association of the glycopeptide antibiotic teicoplanin A2 in aqueous solution studied by molecular hydrodynamics

The natural glycopeptide antibiotic teicoplanin is used for the treatment of serious Gram-positive related bacterial infections and can be administered intravenously, intramuscularly, topically (ocular infections), or orally. It has also been considered for targeting viral infection by SARS-CoV-2. T...

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Published in:Scientific reports 2023-02, Vol.13 (1), p.1969-1969, Article 1969
Main Authors: Chun, Taewoo, Pattem, Jacob, Gillis, Richard B., Dinu, Vlad T., Yakubov, Gleb E., Corfield, Anthony P., Harding, Stephen E.
Format: Article
Language:English
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Summary:The natural glycopeptide antibiotic teicoplanin is used for the treatment of serious Gram-positive related bacterial infections and can be administered intravenously, intramuscularly, topically (ocular infections), or orally. It has also been considered for targeting viral infection by SARS-CoV-2. The hydrodynamic properties of teicoplanin A2 ( M 1  = 1880 g/mol) were examined in phosphate chloride buffer (pH 6.8, I  = 0.10 M) using sedimentation velocity and sedimentation equilibrium in the analytical ultracentrifuge together with capillary (rolling ball) viscometry. In the concentration range, 0–10 mg/mL teicoplanin A2 was found to self-associate plateauing > 1 mg/mL to give a molar mass of (35,400 ± 1000) g/mol corresponding to ~ (19 ± 1) mers, with a sedimentation coefficient s 20, w  =  ~ 4.65 S. The intrinsic viscosity [ η ] was found to be (3.2 ± 0.1) mL/g: both this, the value for s 20,w and the hydrodynamic radius from dynamic light scattering are consistent with a globular macromolecular assembly, with a swelling ratio through dynamic hydration processes of ~ 2.
ISSN:2045-2322
2045-2322
DOI:10.1038/s41598-023-28740-8