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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Microbial Biosensors01:17

Microbial Biosensors

Microbial biosensors are analytical devices that utilize living microbes to detect specific substances through measurable signals. These devices consist of two main components: biosensing organisms and signal-transducing elements. Biosensing organisms, such as Escherichia coli or Saccharomyces cerevisiae, are typically housed in multiwell plates connected to transducers, enabling rapid, real-time detection of target analytes.Signal Generation MechanismWhen a target analyte—such as...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
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...

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Carbohydrate-protein interactions and their biosensing applications.

Xiangqun Zeng1, Cesar A S Andrade, Maria D L Oliveira

  • 1Department of Chemistry, Oakland University, 2200 Squirrel Road, Rochester, MI 48309, USA. zeng@oakland.edu

Analytical and Bioanalytical Chemistry
|December 28, 2011
PubMed
Summary

Carbohydrate recognition offers a promising alternative to antibodies for biosensors. This review explores using carbohydrate-protein interactions and immobilization methods for developing label-free carbohydrate and lectin sensors.

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Area of Science:

  • Biochemistry
  • Biomaterials Science
  • Sensor Technology

Background:

  • Carbohydrate recognition is crucial in biological interactions, particularly for initial attachment.
  • Current biosensor technology predominantly relies on antibodies or nucleic acids for detection.
  • The use of carbohydrates in biological detection systems is limited due to challenges in affinity, scaffold design, and assay technology.

Purpose of the Study:

  • To explore the potential of carbohydrate-protein interactions as a viable alternative to antibodies and nucleic acids in biosensor development.
  • To discuss methods for carbohydrate immobilization for creating carbohydrate- and lectin-based label-free sensors.
  • To demonstrate the feasibility of using carbohydrates and lectins as recognition elements in real-world biosensor applications.

Main Methods:

  • Reviewing the characteristics of natural carbohydrate-protein interactions.
  • Analyzing carbohydrate immobilization techniques based on surface coupling chemistry.
  • Examining innovative designs of multivalent carbohydrate-protein interactions for sensor applications.
  • Presenting representative cases of carbohydrate- and lectin-based label-free sensor development.

Main Results:

  • Carbohydrate-protein interactions exhibit unique characteristics relevant to biosensing.
  • Surface coupling chemistry provides versatile methods for carbohydrate immobilization.
  • Multivalent interactions can enhance the affinity and specificity of carbohydrate-based recognition.
  • Several cases demonstrate the feasibility of carbohydrate and lectin recognition elements in label-free sensors.

Conclusions:

  • Carbohydrate and lectin recognition elements offer a flexible platform for developing label-free biosensors.
  • Overcoming challenges in affinity, scaffold design, and assay technology is key to broader adoption.
  • This approach presents a viable alternative for detection and identification in various biosensor applications.