RT Journal Article
T1 Conformational binding mechanism of lysozyme induced by interactions with penicillin antibiotic drugs
A1 Rial Silva, Ramón
A1 González Durruthy, Michael
A1 Liu, Zhen
A1 Ruso Beiras, Juan Manuel
K1 Lysozyme
K1 Antibiotic
K1 Molecular docking
K1 Protein interactions
AB In this study we present an in-depth and detailed analysis of the binding process between two antibiotics (cloxacillin and dicloxacillin) and a blood serum protein (lysozyme). Our objectives have been several: to determine, at the atomic level, the structural and conformational changes that take place in both molecular structures once the complex is formed; to investigate the effect that the substitution of a hydrogen atom for a chlorine atom has on the bonding process; and to relate these local modifications with macromolecular parameters. Achieving these goals requires a multi-pronged approach and effective resource management. In our case, we have combined different experimental (isothermal titration calorimetry, UV–vis and fluorescence spectroscopy) and computational techniques (molecular docking and network models), in order to obtain comprehensive and contrasted information of the interaction process. Both approaches have showed an excellent correlation, confirming that there is a single binding site, that both penicillins are moderate binders and hydrogen bond and van der Waals forces are predominant. On the other hand, the small discrepancies between the two techniques highlighted the pressing need to approach the study of these systems from both atomic and macromolecular perspectives.
PB Elsevier
YR 2022
FD 2022
LK http://hdl.handle.net/10347/29937
UL http://hdl.handle.net/10347/29937
LA eng
NO Journal of Molecular Liquids  358 (2022) 119081
NO The authors acknowledge Ministerio de Ciencia e Innovación (PID2019-111327GB-100)
DS Minerva
RD 24 abr 2026