Related Experiment Video

Updated: Mar 1, 2026

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
08:53

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Published on: March 21, 2025

1.2K

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

Zaineb Bouaziz1, Laurence Soussan2, Jean-Marc Janot2

  • 1Institut Européen des Membranes, UMR5635, UM, ENSM, CNRS, Place Eugène Bataillon, 34095 Montpellier cedex 5, France; Laboratoire de Physique des Matériaux lamellaires et Nanomatériaux hybrides, Faculté des Sciences de Bizerte Université de Carthage, Tunisia.

Colloids and Surfaces. B, Biointerfaces
|May 30, 2017
PubMed

Insights

Lysozyme's antibacterial properties are retained even when it forms amyloid fibrils and adsorbs onto layered double hydroxides. The enzyme's active site remains accessible, preserving its function against Gram-positive bacteria.

Area of Science:

  • Biochemistry
  • Materials Science
  • Microbiology

Background:

  • Lysozyme, a 129-amino acid enzyme from hen egg white, exhibits antibacterial activity against Gram-positive bacteria.
  • Lysozyme is known to form amyloid fibrils under specific conditions (low pH, <75°C).
  • Layered double hydroxides (LDHs) are materials with potential applications in biomaterial science.

Purpose of the Study:

  • To investigate the impact of lysozyme fibrillation and adsorption onto LDHs on its antibacterial efficacy.
  • To characterize the adsorption behavior and structural integrity of lysozyme on LDHs.
  • To assess the accessibility of the lysozyme active site after adsorption and fibrillation.

Main Methods:

  • Kinetic analysis of lysozyme adsorption onto LDHs.
  • X-ray diffraction (XRD) and Fourier transform infrared spectroscopy (FTIR) for material characterization.
  • Time-resolved fluorescence spectroscopy to study tryptophan accessibility and enzyme denaturation.

Main Results:

  • Lysozyme adsorption onto LDHs follows a pseudo-second-order kinetic model.
  • XRD and FTIR confirm that lysozyme adsorbs exclusively on the external surface of the LDH material.
  • Adsorbed lysozyme amyloid fibrils retain partial antibacterial activity, indicating the active site remains accessible.

Conclusions:

  • Lysozyme fibrillation and adsorption onto LDHs do not completely abolish its antibacterial properties.
  • The layered double hydroxide material provides a platform for immobilizing lysozyme while maintaining partial enzymatic activity.
  • Further studies can explore optimizing LDH-lysozyme composites for enhanced antibacterial applications.
Keywords:
AdsorptionAmyloid fibrilsAntibacterial activityLayered double hydroxide (LDH)LysozymeTime resolved fluorescence

More Related Videos

Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis08:49

Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis

Published on: June 20, 2025

1.4K
Au-Interaction of Slp1 Polymers and Monolayer from Lysinibacillus sphaericus JG-B53 - QCM-D, ICP-MS and AFM as Tools for Biomolecule-metal Studies08:29

Au-Interaction of Slp1 Polymers and Monolayer from Lysinibacillus sphaericus JG-B53 - QCM-D, ICP-MS and AFM as Tools for Biomolecule-metal Studies

Published on: January 19, 2016

11.8K

Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
12.2K
Amyloid Fibrils03:03

Amyloid Fibrils

6.8K
Archaeal Cell Wall01:29

Archaeal Cell Wall

Archaeal cell walls are structurally and compositionally distinct from their bacterial counterparts, lacking the characteristic peptidoglycan layer found in most bacteria. Instead, archaeal cell walls exhibit remarkable diversity, utilizing materials such as pseudomurein, polysaccharides, and proteins to construct their protective outer layers. This structural flexibility is closely tied to archaea's ecological adaptability.S-Layers: The Common Archaeal Cell WallThe S-layer is the most...
1.4K
Outer Layers of the Cell Envelope01:18

Outer Layers of the Cell Envelope

The outermost layers of prokaryotic cells play a critical role in their survival, virulence, and interaction with the environment. These layers, often composed of polysaccharides, polypeptides, or proteins, form protective and adhesive structures that vary in organization and function.Capsules and Slime LayersCapsules are highly organized, tightly bound layers that firmly attach to the bacterial cell wall. Capsules are usually made of polysaccharides, though some are made of polypeptides. These...
1.4K
Lysosomal Hydrolases01:22

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
4.7K