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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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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,...
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Protein Folding01:25

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Protein Folding Quality Check in the RER01:29

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Amino Acid Catabolism01:18

Amino Acid Catabolism

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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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Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
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Rapid Generation of Amyloid from Native Proteins In vitro
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Prebiotically Plausible Autocatalytic Peptide Amyloids.

Saroj K Rout1, David Rhyner1, Roland Riek1

  • 1Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, ETH Hönggerberg, Vladimir-Prelog-Weg 2, 8093, Zürich, Switzerland.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|November 23, 2021
PubMed
Summary

Researchers demonstrated self-replicating molecules, crucial for life's origin. Amyloid-templated reactions showed enhanced yield and stereoselectivity in amino acid condensation, supporting their role in prebiotic evolution.

Keywords:
aggregationamyloidsautocatalysisorigin of lifeself-replication

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Area of Science:

  • Biochemistry
  • Origin of Life Research
  • Molecular Evolution

Background:

  • The origin of life requires self-replicating molecules capable of storing information.
  • Prebiotic self-replication of biologically relevant molecules remains a significant challenge.
  • Amyloids are known for their templating capabilities.

Purpose of the Study:

  • To demonstrate a plausible prebiotic self-replication mechanism for biologically relevant molecules.
  • To investigate the role of amyloids in prebiotic molecular evolution.
  • To enhance the yield and stereoselectivity of amino acid condensation reactions.

Main Methods:

  • Utilized amyloid templating to facilitate peptide-bond-forming reactions.
  • Investigated two systems where reaction products acted as self-replicators.
  • Analyzed the autocatalytic nature of amino acid condensation.

Main Results:

  • Demonstrated self-replication of molecules formed through peptide-bond reactions.
  • Achieved enhanced yield and stereoselectivity in the formation of these self-replicators.
  • Reported the first instance of amino acid condensation undergoing autocatalysis.

Conclusions:

  • Amyloid-templated reactions provide a viable pathway for prebiotic self-replication.
  • Amyloids can function as environment-responsive, information-coding systems in early life evolution.
  • This study offers a potential mechanism for the emergence of self-replicating molecules crucial for life's origin.