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Related Concept Videos

Peptide Bonds02:43

Peptide Bonds

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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
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Microtubule Associated Proteins (MAPs)01:42

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Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
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Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
Neutralization
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Plotting of Topographic Maps01:29

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Topographic maps represent the Earth's surface features using contour lines, which connect points of equal elevation to create a two-dimensional representation of three-dimensional terrain. Creating a topographic map requires a systematic approach.Begin by plotting a scaled grid and marking intersections corresponding to the survey's elevation data points. Assign elevation values at these intersections to build the base map. Next, determine contour levels using a consistent contour interval,...
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Coordinates and map projections are essential tools in accurately representing the Earth's surface for various applications, ranging from navigation to spatial analysis. The latitude and longitude coordinate system is a universally recognized framework for defining locations. Latitude specifies the distance of a point north or south of the equator, measured in degrees from 0° at the equator to 90° at the poles. Longitude indicates a location's position east or west of the prime meridian,...
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Analysis of Histone Antibody Specificity with Peptide Microarrays
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Antibody characterization using novel ERLIC-MS/MS-based peptide mapping.

Jing Zhen1, John Kim1, Ying Zhou1

  • 1a Department of Analytical Sciences and Operations , Biologics CMC, Teva Pharmaceutical Industries , West Chester , PA , USA.

Mabs
|August 22, 2018
PubMed
Summary
This summary is machine-generated.

Electrostatic repulsion hydrophilic interaction chromatography (ERLIC) coupled with mass spectrometry (MS) offers a novel peptide mapping method for biologic therapeutics. This technique provides superior sequence coverage and characterization of challenging modifications like asparagine deamidation.

Keywords:
ERLICantibodycharacterizationdeamidationmethionine oxidationpeptide mapping

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Proteomics

Background:

  • Electrostatic repulsion hydrophilic interaction chromatography (ERLIC) coupled with mass spectrometry (MS) is gaining traction in proteomics.
  • ERLIC is utilized for glycopeptide/phosphorylated peptide enrichment and sample fractionation.

Purpose of the Study:

  • To introduce a novel ERLIC-MS/MS peptide mapping method for biologic therapeutics characterization.
  • To evaluate ERLIC's performance against traditional reversed-phase liquid chromatography (RPLC)-MS/MS.

Main Methods:

  • Development and application of an ERLIC-MS/MS based peptide mapping strategy.
  • Characterization of denosumab, focusing on sequence coverage, terminal peptides, methionine oxidation, asparagine deamidation, and glycopeptides.

Main Results:

  • Achieved 100% sequence coverage for denosumab light and heavy chains, outperforming RPLC-MS/MS for small peptides.
  • Demonstrated superior separation and characterization of asparagine deamidated peptides, a known RPLC-MS/MS challenge.
  • Successfully extended ERLIC applications from sample preparation to direct characterization of biologic therapeutics.

Conclusions:

  • The developed ERLIC-MS/MS method is effective for denosumab characterization, offering complete sequence coverage.
  • ERLIC-MS/MS serves as a valuable standalone or orthogonal method to RPLC-MS/MS for monoclonal antibody characterization.
  • This approach enhances the reliability and confidence in bottom-up peptide mapping for biologic therapeutics analysis.