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Amplifying Signals via Enzymatic Cascade01:22

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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
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In 1923, G. N. Lewis proposed a generalized definition of acid-base behavior in which acids and bases are identified by their ability to accept or to donate a pair of electrons and form a coordinate covalent bond.
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Some compounds produce hydroxide ions when dissolved by chemically reacting with water molecules. In all cases, these compounds react only partially and so are classified as weak bases. These types of compounds are also abundant in nature and important commodities in various technologies. For example, global production of the weak base ammonia is typically well over 100 metric tons annually, being widely used as an agricultural fertilizer, a raw material for chemical synthesis of other...
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One of the common DNA damages is the chemical alteration of single bases by alkylation, oxidation, or deamination. The altered bases cause mispairing and strand breakage during replication. This type of damage causes minimal change to the DNA double helix structure and can be repaired by the base excision repair (BER) pathways. BER corrects damaged DNA sequences by removing the damaged base and restoring the original base sequence using the complementary strand as a template.
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Salts with Acidic Ions
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Light-driven Enzymatic Decarboxylation
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CCMV-Based Enzymatic Nanoreactors.

Mark V de Ruiter1, Rindia M Putri1, Jeroen J L M Cornelissen2

  • 1Laboratory of Biomolecular Nanotechnology, MESA+ Institute for Nanotechnology, University of Twente, Enschede, The Netherlands.

Methods in Molecular Biology (Clifton, N.J.)
|June 6, 2018
PubMed
Summary
This summary is machine-generated.

Researchers developed three noncovalent methods to encapsulate enzymes within cowpea chlorotic mottle virus (CCMV) protein cages, creating novel protein-based nanoreactors for various applications.

Keywords:
Cowpea chlorotic mottle virus (CCMV)Enzyme encapsulationFunctional cargoLeucine zippersNanoreactorsVirus-like particlespH-responsive assembly

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Area of Science:

  • Biotechnology
  • Nanotechnology
  • Biochemistry

Background:

  • Protein-based nanoreactors offer unique platforms for biocatalysis.
  • Cowpea chlorotic mottle virus (CCMV) capsids serve as versatile viral protein cages.
  • Efficient enzyme encapsulation is crucial for nanoreactor functionality.

Purpose of the Study:

  • To describe three distinct noncovalent methods for enzyme encapsulation into CCMV capsids.
  • To demonstrate the applicability of these methods for specific enzymes and potentially others.
  • To advance the development of protein-based nanoreactors.

Main Methods:

  • Enzyme encapsulation using pH-driven interactions.
  • Enzyme encapsulation utilizing leucine zipper interactions.
  • Enzyme encapsulation driven by electrostatic interactions.

Main Results:

  • Successfully incorporated enzymes into CCMV capsids using three different noncovalent strategies.
  • Demonstrated efficient encapsulation for horseradish peroxidase, glucose oxidase, and Pseudozyma antarctica lipase B.
  • Validated the versatility of the methods for various enzymes.

Conclusions:

  • Developed efficient and versatile noncovalent methods for creating enzyme-loaded CCMV nanoreactors.
  • These methods provide a robust platform for protein-based nanoreactor design.
  • The described techniques are applicable to a broad range of enzymes for diverse applications.