Abstract:
:The interaction between TEM-1 β-lactamase and antibiotics is very important in the hydrolysis of antibiotics. In the present study, the recognition and binding of TEM-1 β-lactamase with three β-lactam antibiotics, including penicillin G, cefalexin and cefoxitin, was investigated by fluorescence and ultraviolet-visible absorption spectra in combination with molecular docking in the temperature range of 278-288 K and under simulated physiological conditions. The results demonstrated that the fluorescence emissions of TEM-1 β-lactamase were extinguished by static quenching and the energy of TEM-1 β-lactamase was transferred in a non-radioactive manner. The binding of TEM-1 β-lactamase with the three antibiotics was a spontaneously exothermic process, with binding constants of 1.41×107, 7.81×106 and 5.43×104 at 278 K. Furthermore, binding was driven by enthalpy change and the binding forces between them were mainly hydrogen bonding and Van der Waals forces. A TEM-1 β-lactamase only bound with one antibiotic at a time and the binding capacity between them was closely associated with the functional groups and flexibility in the antibiotics. In addition, a conformational change occurred in the TEM-1 β-lactamases when they bound with the three antibiotics and TEM-1 β-lactamase-antibiotic complexes were formed. The present study provided an insight into the recognition and binding of TEM-1 β-lactamase with β-lactam antibiotics, which may be helpful for designing a novel substrate for TEM-1 β-lactamase and developing novel antibiotics that are resistant to the enzyme.
journal_name
Exp Ther Medjournal_title
Experimental and therapeutic medicineauthors
Yang J,Li Q,Bian Ldoi
10.3892/etm.2017.4853subject
Has Abstractpub_date
2017-10-01 00:00:00pages
3288-3298issue
4eissn
1792-0981issn
1792-1015pii
ETM-0-0-4853journal_volume
14pub_type
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