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

Chun, Taewoo, Pattem, Jacob ORCID: https://orcid.org/0000-0003-0276-7996, Gillis, Richard B., Dinu, Vlad T., Yakubov, Gleb E., Corfeld, Anthony P. and Harding, Stephen E. 2023. Self-association of the glycopeptide antibiotic teicoplanin A2 in aqueous solution studied by molecular hydrodynamics. Scientific Reports 13 (1) , 1969. 10.1038/s41598-023-28740-8

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Abstract

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 (M1 = 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 s20, w =  ~ 4.65 S. The intrinsic viscosity [η ] was found to be (3.2 ± 0.1) mL/g: both this, the value for s20,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.

Item Type:	Article
Date Type:	Published Online
Status:	Published
Schools:	Schools > Dentistry
Publisher:	Nature Research
ISSN:	2045-2322
Date of First Compliant Deposit:	15 September 2023
Date of Acceptance:	24 January 2023
Last Modified:	16 Sep 2023 07:54
URI:	https://orca.cardiff.ac.uk/id/eprint/162534

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