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

CHUN, Taewoo, PATTEM, Jacob, GILLIS, Richard B., DINU, Vlad T., YAKUBOV, Gleb E., CORFIELD, 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.

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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
Identification Number:	https://doi.org/10.1038/s41598-023-28740-8
SWORD Depositor:	Symplectic Elements
Depositing User:	Symplectic Elements
Date Deposited:	06 Feb 2023 11:40
Last Modified:	11 Oct 2023 12:31
URI:	https://shura.shu.ac.uk/id/eprint/31412

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