Interaction of hen egg white lysozyme with cefpiramide sodium: multi-spectroscopic and computational simulations. Issue 8 (14th September 2019)

• Record Type: Journal Article
• Authors: Zhang, Hong-Cai; Liu, Bao-Sheng
• Is Part Of: Spectroscopy letters. Volume 52:Issue 8(2019)
• Page Start: 447
• Page End: 455
• Publication Date: 2019-09-14
• Subjects: Cefpiramide sodium -- hen egg white lysozyme -- fluorescence spectroscopy -- interaction -- molecular docking; Spectrum analysis -- Periodicals; 543.5
• DOI: 10.1080/00387010.2019.1660684
• Languages: English
• ISSNs: 0038-7010

Abstract

Abstract: Under simulated physiological conditions (pH = 7.40), the interaction between cefpiramide sodium and hen egg white lysozyme was studied with multi-spectroscopy and molecular docking. The results showed that cefpiramide sodium quenched the fluorescence of hen egg white lysozyme by static quenching, and the number of binding site n was about 1. The binding distance ( r ) between cefpiramide sodium and hen egg white lysozyme was obtained based on the Förster nonradioactive resonance energy transfer and r was less than 7 nm, which indicated that there was a non-radiative energy transition in the system. The thermodynamic parameters were obtained from the van't Hoff equation, and the Gibbs free energy Δ G < 0, indicating that the reaction was spontaneous; Δ H < 0, Δ S > 0, indicating hydrophobic interaction played a major role in forming the cefpiramide sodium-hen egg white lysozyme complex. Synchronous spectra, circular dichroism spectra and UV-Vis spectra showed that cefpiramide sodium changed the conformation of hen egg white lysozyme. The molecular docking results showed that the binding position of cefpiramide sodium was close to the active center composed of Asp52 and Glu35 residues, suggesting that cefpiramide sodium could change the microenvironment of amino acid residues at the catalytic active center of hen egg white lysozyme.