Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8328855 | International Journal of Biological Macromolecules | 2018 | 7 Pages |
Abstract
Present work reports the inhibition of Bacillus cereus EMB20 β-lactamase by a deep eutectic solvent, maline in an uncompetitive manner. Far-UV CD and intrinsic fluorescence spectroscopy revealed a disrupted secondary as well as tertiary structure as a function of maline concentration. The effect of individual components of maline on β-lactamase inhibition showed that malonic acid was mainly responsible for inhibiting the β-lactamase. Structural and docking studies found that malonic acid led to major perturbations in the secondary and tertiary structure of the enzyme while H-bonding with the active site residues. Further the antibacterial and cytotoxic studies also confirmed the potential of maline as a potent growth inhibitor of β-lactamase producing B. cereus EMB20.
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Ayesha Sadaf, Arti Kumari, S.K. Khare,