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Related Experiment Video

Updated: May 25, 2026

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Published on: January 31, 2014

Deamidation of collagen.

Pilar Perez Hurtado¹, Peter B O'Connor

¹Department of Chemistry, University of Warwick, Coventry, UK.

Analytical Chemistry

|January 31, 2012

Summary

Researchers developed a new method using mass spectrometry to measure collagen deamidation, a process linked to aging. This technique offers a simpler, more accurate way to study collagen aging in fossils and biological samples.

Area of Science:

Biochemistry
Paleontology
Analytical Chemistry

Background:

Collagen is a crucial structural protein in animals, with Type I being abundant in bone.
Collagen deamidation, a post-translational modification, increases with age in mammals.
Existing methods for measuring collagen deamidation are complex and require large samples.

Purpose of the Study:

To develop a simpler and more accurate method for determining collagen deamidation at the whole protein level.
To investigate the potential role of collagen deamidation in the aging process of fossil materials.

Main Methods:

Utilized Fourier transform ion cyclotron resonance-mass spectrometry (FTICR-MS).
Employed collisionally activated dissociation (CAD) and electron capture dissociation (ECD) for analysis.

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Enrichment of Extracellular Matrix Proteins from Tissues and Digestion into Peptides for Mass Spectrometry Analysis

Enrichment of Extracellular Matrix Proteins from Tissues and Digestion into Peptides for Mass Spectrometry Analysis

Published on: July 23, 2015

Related Experiment Videos

Last Updated: May 25, 2026

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Published on: January 31, 2014

Enrichment of Extracellular Matrix Proteins from Tissues and Digestion into Peptides for Mass Spectrometry Analysis

Enrichment of Extracellular Matrix Proteins from Tissues and Digestion into Peptides for Mass Spectrometry Analysis

Published on: July 23, 2015

Analyzed deamidation extent in collagen Type I peptides.

Main Results:

Successfully determined the extent of deamidation in collagen using FTICR-MS, CAD, and ECD.
Measured deamidation half-life for collagen (I) tryptic peptides ranged from 2000 to 6000 s.
Established a novel method for whole protein deamidation analysis.

Conclusions:

The developed FTICR-MS method provides a more accurate and simpler approach to study collagen deamidation.
This method can be applied to assess collagen aging in both biological and fossil samples.
Further research can explore the role of collagen deamidation in fossil material aging.