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. [Article]

Documents
31412:613619
[thumbnail of Chunetal teicoplanin 2023.pdf]
Preview
PDF
Chunetal teicoplanin 2023.pdf - Published Version
Available under License Creative Commons Attribution.

Download (1MB) | Preview
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.
More Information
Statistics

Downloads

Downloads per month over past year

Metrics

Altmetric Badge

Dimensions Badge

Share
Add to AnyAdd to TwitterAdd to FacebookAdd to LinkedinAdd to PinterestAdd to Email

Actions (login required)

View Item View Item