Structure and antibacterial activity relationships of native and amyloid fibril lysozyme loaded on layered double hydroxide

Colloids and Surfaces B: Biointerfaces

Volumn 157, Issue , 2017, Pages 10-17

  Bouaziz, Zaineb ^a,b   Soussan, Laurence ^a   Janot, Jean Marc ^a   Lepoitevin, Mathilde ^a   Bechelany, Mikhael ^a   Djebbi, Mohamed Amine ^b,c   Amara, Abdesslem Ben Haj ^b   Balme, Sebastien ^a  

^a CNRS   (France)

^b University of Carthage   (Tunisia)

^c UNIVERSITÉ LYON 1   (France)

Author keywords

Adsorption; Amyloid fibrils; Antibacterial activity; Layered double hydroxide (LDH); Lysozyme; Time resolved fluorescence

Indexed keywords

ADSORPTION; AMINO ACIDS; BACTERIA; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; FOURIER TRANSFORM INFRARED SPECTROSCOPY; GLYCOPROTEINS; X RAY DIFFRACTION;

AMYLOID FIBRIL; ANTI-BACTERIAL ACTIVITY; ANTIBACTERIAL PROPERTIES; GRAM-POSITIVE BACTERIUM; LAYERED DOUBLE HYDROXIDES; PSEUDO-SECOND ORDER MODEL; TIME-RESOLVED FLUORESCENCE; TIME-RESOLVED FLUORESCENCE SPECTROSCOPY;

ENZYMES;

AMYLOID; LAYERED DOUBLE HYDROXIDE; LYSOZYME; NANOCOMPOSITE; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT;

ADSORPTION KINETICS; ANTIBACTERIAL ACTIVITY; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME IMMOBILIZATION; ENZYME LOCALIZATION; ENZYME MODIFICATION; INFRARED SPECTROSCOPY; NONHUMAN; PRIORITY JOURNAL; SPECTROFLUOROMETRY; STAPHYLOCOCCUS EPIDERMIDIS; STRUCTURE ACTIVITY RELATION; X RAY DIFFRACTION; ADSORPTION; CHEMISTRY; KINETICS;

ADSORPTION; AMYLOID; ANTI-BACTERIAL AGENTS; KINETICS; MURAMIDASE; SPECTROMETRY, FLUORESCENCE; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; STRUCTURE-ACTIVITY RELATIONSHIP; X-RAY DIFFRACTION;

EID: 85019868222     PISSN: 09277765     EISSN: 18734367     Source Type: Journal    
DOI: 10.1016/j.colsurfb.2017.05.050     Document Type: Article

References (40)

1. Weiss, M.S., Palm, G.J., Hilgenfeld, R., Crystallization, structure solution and refinement of hen egg-white lysozyme at pH 8.0 in the presence of MPD. Acta Crystallogr. Sect. D: Biol. Crystallogr. 56 (2000), 952–958.
2. Balme, S., et al. Structure, orientation and stability of lysozyme confined in layered materials. Soft Matter 9:11 (2013), 3188–3196.
3. Lepoitevin, M., et al. BSA and lysozyme adsorption on homoionic montmorillonite: influence of the interlayer cation. Appl. Clay Sci. 95 (2014), 396–402.
4. Bhattacharyya, M.S., et al. Lysozyme adsorption and release from ordered mesoporous materials. J. Phys. Chem. C 114:47 (2010), 19928–19934.
5. Kiersnowski, A., et al. Delamination of montmorillonite in serum—a new approach to obtaining clay-based biofunctional hybrid materials. Appl. Clay Sci. 44:3–4 (2009), 225–229.
6. Luckarift, H.R., et al. Rapid, room-temperature synthesis of antibacterial bionanocomposites of lysozyme with amorphous silica or titania. Small 2:5 (2006), 640–643.
7. Cheng, Y.H., et al. Effects of metal oxide nanoparticles on the structure and activity of lysozyme. Colloids Surf. B: Biointerfaces 151 (2017), 344–353.
8. Jahn, T.R., Radford, S.E., The Yin and Yang of protein folding. FEBS J. 272:23 (2005), 5962–5970.
9. Hartl, F.U., Hayer-Hartl, M., Converging concepts of protein folding in vitro and in vivo. Nat. Struct. Mol. Biol. 16:6 (2009), 574–581.
10. Goda, S., et al. Amyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution. Protein Sci. 9:2 (2000), 369–375.
11. Swaminathan, R., et al. Lysozyme: a model protein for amyloid research. Adv. Protein Chem. Struct. Biol. 84 (2011), 63–111.
12. Booth, D.R., et al. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 385:6619 (1997), 787–793.
13. Li, C.X., Bolisetty, S., Mezzenga, R., Hybrid nanocomposites of gold single-crystal platelets and amyloid fibrils with tunable fluorescence, conductivity, and sensing properties. Adv. Mater. 25:27 (2013), 3694–3700.
14. Li, C.X., Mezzenga, R., The interplay between carbon nanomaterials and amyloid fibrils in bio-nanotechnology. Nanoscale 5:14 (2013), 6207–6218.
15. Li, C.X., Adamcik, J., Mezzenga, R., Biodegradable nanocomposites of amyloid fibrils and graphene with shape-memory and enzyme-sensing properties. Nat. Nanotechnol. 7:7 (2012), 421–427.
16. Bolisetty, S., Mezzenga, R., Amyloid-carbon hybrid membranes for universal water purification. Nat. Nanotechnol., 11(4), 2016, 365.
17. Knowles, T.P.J., et al. Nanostructured films from hierarchical self-assembly of amyloidogenic proteins. Nat. Nanotechnol. 5:3 (2010), 204–207.
18. Adamcik, J., Berquand, A., Mezzenga, R., Single-step direct measurement of amyloid fibrils stiffness by peak force quantitative nanomechanical atomic force microscopy. Appl. Phys. Lett., 98(19), 2011.
19. Li, C.X., et al. Amyloid-hydroxyapatite bone biomimetic composites. Adv. Mater., 26(20), 2014, 3207.
20. Wang, Q., O'Hare, D., Recent advances in the synthesis and application of layered double hydroxide (LDH) nanosheets. Chem. Rev. 112:7 (2012), 4124–4155.
21. Kong, X.G., et al. Layer-by-layer assembly of bi-protein/layered double hydroxide ultrathin film and its electrocatalytic behavior for catechol. Biosens. Bioelectron. 26:2 (2010), 549–554.
22. Rao, C.N.R., Novel materials, materials design and synthetic strategies: recent advances and new directions. J. Mater. Chem. 9:1 (1999), 1–14.
23. Bouaziz, Z., et al. Adsorption of nisin into layered double hydroxide nanohybrids and in-vitro controlled release. Mater. Sci. Eng.: C, 2017.
24. Yang, Q.Z., et al. Synthesis and characterization of polyoxyethylene sulfate intercalated Mg-Al-nitrate layered double hydroxide. Langmuir 19:14 (2003), 5570–5574.
25. Kwak, S.Y., et al. Inorganic delivery vector for intravenous injection. Biomaterials 25:28 (2004), 5995–6001.
26. Hill, S.E., et al. Amyloid protofibrils of lysozyme nucleate and grow via oligomer fusion. Biophys. J. 96:9 (2009), 3781–3790.
27. Krieger, J., Langowski, J., QuickFit 3.0: A Data Evaluation Application for Biophysics. 2005 http://www.dkfz.de/Macromol/quickfit/index.html.
28. Balme, S., et al. Highly efficient fluorescent label unquenched by protein interaction to probe the avidin rotational motion. J. Photochem. Photobiol. A: Chem. 184:1–2 (2006), 204–211.
29. Tangaraj, V., et al. Fluorescent quenching of sulforhodamine dye over graphene oxide and graphene-like boron nitride. Eur. J. Inorg. Chem. 2016:13–14 (2016), 2125–2130.
30. Arnaudov, L.N., de Vries, R., Thermally induced fibrillar aggregation of hen egg white lysozyme. Biophys. J. 88:1 (2005), 515–526.
31. Antonio, P., Iha, K., Suarez-Iha, M.E.V., Kinetic modeling of adsorption of di-2-pyridylketone salicyloylhydrazone on silica gel. J. Colloid Interface Sci. 307:1 (2007), 24–28.
32. Cowgill, R.W., Fluorescence and protein structure. 11. Fluorescence quenching by disulfide and sulfhydryl groups. Biochim. Biophys. Acta, 140(1), 1967, 37.
33. Nishimoto, E., et al. Internal motion of lysozyme studied by time-resolved fluorescence depolarization of tryptophan residues. Biochemistry 37:16 (1998), 5599–5607.
34. Nishimoto, E., et al. Resolution and characterization of tryptophyl fluorescence of hen egg-white lysozyme by quenching- and time-resolved spectroscopy. Biosci. Biotechnol. Biochem. 63:2 (1999), 329–336.
35. Narayanan, J., Liu, X.Y., Protein interactions in undersaturated and supersaturated solutions: a study using light and X-ray scattering. Biophys. J. 84:1 (2003), 523–532.
36. Pastor, I., et al. Structure and dynamics of lysozyme encapsulated in a silica sol-gel matrix. J. Phys. Chem. B 111:39 (2007), 11603–11610.
37. Chaari, A., et al. Insights into kinetics of agitation-induced aggregation of hen lysozyme under heat and acidic conditions from various spectroscopic methods. PLOS ONE, 10(11), 2015.
38. Frare, E., et al. Identification of the core structure of lysozyme amyloid fibrils by proteolysis. J. Mol. Biol. 361:3 (2006), 551–561.
39. Yang, Q.Z., Chang, Y.Y., Zhao, H.Z., Preparation and antibacterial activity of lysozyme and layered double hydroxide nanocomposites. Water Res. 47:17 (2013), 6712–6718.
40. Hawiger, J., Purification and properties of lysozyme produced by Staphylococcus aureus. J. Bacteriol., 95(2), 1968, 376.