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Related Concept Videos

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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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.
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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.
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Glycoform Differentiation by a Targeted, Self-Assembled, Pattern-Generating Protein Surface Sensor.

Ronny Peri-Naor1, Zohar Pode1, Naama Lahav-Mankovski1

  • 1Department of Organic Chemistry, Weizmann Institute of Science, Rehovot 7610001, Israel.

Journal of the American Chemical Society
|August 14, 2020
PubMed
Summary
This summary is machine-generated.

Researchers developed self-assembling DNA (oligodeoxynucleotide) sensors for precise protein analysis. These novel sensors can differentiate glycoforms and detect specific protein tags, showcasing diagnostic potential.

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Area of Science:

  • Biomolecular Engineering
  • Supramolecular Chemistry
  • Analytical Chemistry

Background:

  • Therapeutic protein glycosylation is critical for efficacy and safety.
  • Existing methods for glycoform analysis can be complex and time-consuming.
  • Developing versatile molecular sensors is essential for advanced diagnostics.

Purpose of the Study:

  • To present a novel method for creating pattern-generating protein surface sensors using self-assembling modified oligodeoxynucleotides (ODNs).
  • To demonstrate the sensor's ability to discriminate between distinct glycoform populations and identify glycosylation states of therapeutic proteins.
  • To showcase the integration of supramolecular receptors and sensors into advanced molecular analytical devices.

Main Methods:

  • Self-assembly of modified oligodeoxynucleotides (ODNs) to create protein surface sensors.
  • Integration of anthracene-boronic acid (An-BA) probe for enhanced glycoform differentiation via photophysical properties.
  • Modification with trinitrilotriacetic acid (tri-NTA)-Ni2+ complex for selective binding to hexa-histidine tags (His-tags).

Main Results:

  • Successfully developed ODN-based sensors capable of discriminating between distinct glycoform populations.
  • Demonstrated the diagnostic potential by identifying glycosylation states of a therapeutic protein.
  • Validated the sensor's selectivity towards His-tag-labeled proteins, confirming the mechanism of function.

Conclusions:

  • The described self-assembly method offers a simple yet powerful approach for generating targeted protein surface sensors.
  • These sensors exhibit significant diagnostic potential for analyzing therapeutic proteins and differentiating glycoforms.
  • The modularity of the system allows for integration with various molecular probes and receptors, enabling the development of sophisticated analytical devices.