Related Experiment Video

Updated: Jul 17, 2025

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

6.2K

Phenol-soluble modulins form amyloids in contact with multiple surface chemistries

Laurent Marichal1, Lucie Bagnard1, Olivier Sire2

  • 1Université Grenoble Alpes, CNRS, Grenoble-INP LMGP, Grenoble F-38000, France.

Biochimica Et Biophysica Acta. General Subjects
|August 28, 2023
PubMed

Insights

Phenol-soluble modulins (PSMs) from Staphylococcus aureus readily adsorb to surfaces and form amyloids. This adaptability suggests a role in biofilm adhesion and structural integrity.

Area of Science:

  • Microbiology
  • Biomaterials Science
  • Biophysics

Background:

  • Functional amyloids are crucial in microbial communities.
  • Staphylococcus aureus secretes phenol-soluble modulins (PSMs) that form amyloid structures within biofilms.
  • The precise function of these PSM amyloids remains unclear.

Purpose of the Study:

  • To investigate the bioadhesive and biofilm stabilization potential of PSM amyloids.
  • To analyze PSM adsorption and amyloid formation on various abiotic surfaces.

Main Methods:

  • Surface plasmon resonance imaging
  • Fluorescence aggregation kinetics
  • Fourier-transform infrared (FTIR) spectroscopy
  • Evaluation of PSM interactions with diverse surface chemistries.

Main Results:

  • PSMs demonstrate significant adsorption capabilities, even on low-binding surfaces.
  • Surface chemistries do not impede the aggregation potential of PSMs into amyloids.
  • PSM adsorption and amyloid formation are versatile across different tested surfaces.

Conclusions:

  • PSMs exhibit high adaptability for bioadhesion due to their surface adsorption properties.
  • The inherent amyloidogenic potential of PSMs is maintained irrespective of surface interactions.
  • These findings suggest a potential role for PSMs in enhancing biofilm adhesion and structural integrity.
Keywords:
AdsorptionAmyloidFTIRMaterial surfacePhenol-soluble modulinsSPRi

More Related Videos

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils00:15

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

6.0K
A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis06:17

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

Published on: May 22, 2018

12.0K

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,...
9.6K
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
2.9K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
7.9K
Protein Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
7.0K
Proteoglycans01:05

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
3.9K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
6.8K