A Study of the Interaction Between Malachite Green and Lysozyme by Steady-state Fluorescence

Overview

Journal J Fluoresc

Specialties Biophysics
Chemistry

Date 2009 Apr 1

PMID 19333739

Citations 9

Authors

Fei Ding

Wei Liu

Feng Liu

Zhi-Yuan Li

Ying Sun

Affiliations

Soon will be listed here.

Abstract

The interaction of a N-methylated diaminotriphenylmethane dye, malachite green, with lysozyme was investigated by fluorescence spectroscopic techniques under physiological conditions. The binding parameters have been evaluated by fluorescence quenching methods. The results revealed that malachite green caused the fluorescence quenching of lysozyme through a static quenching procedure. The thermodynamic parameters like DeltaH and DeltaS were calculated to be -15.33 kJ mol(-1) and 19.47 J mol(-1) K(-1) according to van't Hoff equation, respectively, which proves main interaction between malachite green and lysozyme is hydrophobic forces and hydrogen bond contact. The distance r between donor (lysozyme) and acceptor (malachite green) was obtained to be 3.82 nm according to Frster's theory. The results of synchronous fluorescence, UV/vis and three-dimensional fluorescence spectra showed that binding of malachite green with lysozyme can induce conformational changes in lysozyme. In addition, the effects of common ions on the constants of lysozyme-malachite green complex were also discussed.

Citing Articles

Interactions between tetrahydroisoindoline-1,3-dione derivatives and human serum albumin via multiple spectroscopy techniques.

Zhu M, Wang L, Zhang H, Fan S, Wang Z, Li Q Environ Sci Pollut Res Int. 2018; 25(18):17735-17748.

PMID: 29671232 DOI: 10.1007/s11356-018-1955-9.

Fluorescent component and complexation mechanism of extracellular polymeric substances during dye wastewater biotreatment by anaerobic granular sludge.

Li N, Wei D, Sun Q, Han X, Du B, Wei Q R Soc Open Sci. 2018; 5(2):171445.

PMID: 29515863 PMC: 5830752. DOI: 10.1098/rsos.171445.

Fluorescence Behavior of Schiff Base-N, N'-bis(salicylidene) Trans 1, 2-Diaminocyclohexane in Proteinous and Micellar Environments.

Roy N, Nath S, Paul P, Singh T J Fluoresc. 2017; 27(6):2295-2311.

PMID: 28831629 DOI: 10.1007/s10895-017-2171-6.

Conformational modulation of the farnesoid X receptor by prenylflavonoids: Insights from hydrogen deuterium exchange mass spectrometry (HDX-MS), fluorescence titration and molecular docking studies.

Yang L, Broderick D, Campbell Y, Gombart A, Stevens J, Jiang Y Biochim Biophys Acta. 2016; 1864(12):1667-1677.

PMID: 27596062 PMC: 5071164. DOI: 10.1016/j.bbapap.2016.08.019.

Interaction mechanism of Trp-Arg dipeptide with calf thymus DNA.

Lin J, Gao C, Liu R J Fluoresc. 2013; 23(5):921-7.

PMID: 23604815 DOI: 10.1007/s10895-013-1217-7.

References

Shaikh S, Seetharamappa J, Kandagal P, Manjunatha D . In vitro study on the binding of anti-coagulant vitamin to bovine serum albumin and the influence of toxic ions and common ions on binding. Int J Biol Macromol. 2007; 41(1):81-6. DOI: 10.1016/j.ijbiomac.2007.01.004. View

Cha C, Doerge D, Cerniglia C . Biotransformation of malachite green by the fungus Cunninghamella elegans. Appl Environ Microbiol. 2001; 67(9):4358-60. PMC: 93171. DOI: 10.1128/AEM.67.9.4358-4360.2001. View

Lakowicz J, Weber G . Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules. Biochemistry. 1973; 12(21):4161-70. PMC: 6959846. DOI: 10.1021/bi00745a020. View

Chen C, Lu C, Chung Y, Jan J . UV light induced photodegradation of malachite green on TiO2 nanoparticles. J Hazard Mater. 2006; 141(3):520-8. DOI: 10.1016/j.jhazmat.2006.07.011. View

Oevermann A, Engels M, Thomas U, Pellegrini A . The antiviral activity of naturally occurring proteins and their peptide fragments after chemical modification. Antiviral Res. 2003; 59(1):23-33. PMC: 7125565. DOI: 10.1016/s0166-3542(03)00010-x. View

Gorbenko G, Ioffe V, Kinnunen P . Binding of lysozyme to phospholipid bilayers: evidence for protein aggregation upon membrane association. Biophys J. 2007; 93(1):140-53. PMC: 1914450. DOI: 10.1529/biophysj.106.102749. View

PARROT J, NICOT G . Antihistaminic action of lysozyme. Nature. 1963; 197:496. DOI: 10.1038/197496a0. View

Zhu J, Li D, Jin J, Wu L . Binding analysis of farrerol to lysozyme by spectroscopic methods. Spectrochim Acta A Mol Biomol Spectrosc. 2007; 68(2):354-9. DOI: 10.1016/j.saa.2006.11.045. View

Lee-Huang S, Sun Y, Huang P, Kung H, Blithe D, Chen H . Lysozyme and RNases as anti-HIV components in beta-core preparations of human chorionic gonadotropin. Proc Natl Acad Sci U S A. 1999; 96(6):2678-81. PMC: 15828. DOI: 10.1073/pnas.96.6.2678. View

10.

Ogundele M . A novel anti-inflammatory activity of lysozyme: modulation of serum complement activation. Mediators Inflamm. 1999; 7(5):363-5. PMC: 1781862. DOI: 10.1080/09629359890893. View

11.

Blake C, KOENIG D, Mair G, North A, Phillips D, Sarma V . Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution. Nature. 1965; 206(4986):757-61. DOI: 10.1038/206757a0. View

12.

Ran D, Wu X, Zheng J, Yang J, Zhou H, Zhang M . Study on the interaction between florasulam and bovine serum albumin. J Fluoresc. 2007; 17(6):721-6. DOI: 10.1007/s10895-007-0226-9. View

13.

Zhang Y, Zhou B, Liu Y, Zhou C, Ding X, Liu Y . Fluorescence study on the interaction of bovine serum albumin with p-aminoazobenzene. J Fluoresc. 2007; 18(1):109-18. DOI: 10.1007/s10895-007-0247-4. View

14.

Lakowicz J, Weber G . Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry. 1973; 12(21):4171-9. PMC: 6945976. DOI: 10.1021/bi00745a021. View

15.

Henderson A, Schmitt T, Heinze T, Cerniglia C . Reduction of malachite green to leucomalachite green by intestinal bacteria. Appl Environ Microbiol. 1997; 63(10):4099-101. PMC: 168723. DOI: 10.1128/aem.63.10.4099-4101.1997. View

16.

Srivastava S, Sinha R, Roy D . Toxicological effects of malachite green. Aquat Toxicol. 2004; 66(3):319-29. DOI: 10.1016/j.aquatox.2003.09.008. View

17.

Zhang Y, Zhou B, Zhang X, Huang P, Li C, Liu Y . Interaction of malachite green with bovine serum albumin: determination of the binding mechanism and binding site by spectroscopic methods. J Hazard Mater. 2008; 163(2-3):1345-52. DOI: 10.1016/j.jhazmat.2008.07.132. View

18.

Xiao J, Chen X, Jiang X, Hilczer M, Tachiya M . Probing the interaction of trans-resveratrol with bovine serum albumin: a fluorescence quenching study with Tachiya model. J Fluoresc. 2008; 18(3-4):671-8. DOI: 10.1007/s10895-008-0346-x. View

19.

Imoto T, FORSTER L, Rupley J, Tanaka F . Fluorescence of lysozyme: emissions from tryptophan residues 62 and 108 and energy migration. Proc Natl Acad Sci U S A. 1972; 69(5):1151-5. PMC: 426651. DOI: 10.1073/pnas.69.5.1151. View

20.

Lehrer S . Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry. 1971; 10(17):3254-63. DOI: 10.1021/bi00793a015. View