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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, normally used to...
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, normally used to...
Amino Acid Catabolism01:18

Amino Acid Catabolism

Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...

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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

Unzipping a functional microbial amyloid.

David Alsteens1, Caleen B Ramsook, Peter N Lipke

  • 1Institute of Life Sciences & Institute of Condensed Matter and Nanosciences, Université Catholique de Louvain, Croix du Sud, 1 bte L7.04.01, B-1348 Louvain-la-Neuve, Belgium.

ACS Nano
|August 29, 2012
PubMed
Summary
This summary is machine-generated.

Functional amyloids from Candida albicans strengthen cell adhesion. Atomic force microscopy reveals how amyloid interactions provide mechanical strength to these microbial adhesion proteins.

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Area of Science:

  • Microbiology and Nanotechnology
  • Biophysics

Background:

  • Functional amyloids are crucial for microbial adhesion and biofilm formation.
  • The molecular basis of their mechanical strength is not well understood.
  • Als proteins from Candida albicans are key adhesion proteins.

Purpose of the Study:

  • To investigate the mechanical properties of amyloids formed by Als proteins.
  • To elucidate the molecular mechanisms underlying the mechanical strength of these functional amyloids.
  • To explore the implications for microbial adhesion and nanotechnology.

Main Methods:

  • Single-molecule atomic force microscopy (AFM) was employed.
  • Mechanical stretching of Als proteins was performed.
  • Force signatures were analyzed to understand β-sheet unzipping.

Main Results:

  • Stretching Als proteins revealed characteristic force signatures.
  • These signatures correspond to the mechanical unzipping of β-sheet interactions.
  • Unzipping probability increased with contact time, indicating time-dependent association.

Conclusions:

  • Amyloid interactions confer cohesive strength to Als cell adhesion proteins.
  • This mechanism enhances microbial cell adhesion.
  • Functional amyloids may offer a general strategy for strengthening cell adhesion proteins and in nanostructures.