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isoAsp-Quest: workflow development for isoAsp identification using database searches.

Hiroaki Sakaue1, Atsushi Kuno1

  • 1Molecular and Cellular Glycoproteomics Research Group, Cellular and Molecular Biotechnology Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Central 5, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8565, Japan.

Journal of Biochemistry
|October 23, 2024
PubMed
Summary
This summary is machine-generated.

A new method, isoAsp-Quest, identifies aspartyl isomerization in proteins. This technique uses enzymatic conversion and mass spectrometry to detect subtle changes, aiding protein quality control and biomarker discovery.

Keywords:
aspartic acidisoAsp-Questisomerizationprotein L-isoaspartyl-O-methyltransferaseproteomics

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Area of Science:

  • Biochemistry
  • Proteomics
  • Analytical Chemistry

Background:

  • Aspartyl residue isomerization is a common post-translational modification in vivo.
  • Standard mass spectrometry struggles to detect Asp isomerization due to unchanged molecular weight.

Purpose of the Study:

  • To develop a novel mass spectrometry-based method for identifying aspartyl isomerization (isoAsp).
  • To establish a straightforward and rapid workflow for analyzing isoAsp modifications.

Main Methods:

  • Developed isoAsp-Quest, a database search-oriented method.
  • Utilized protein L-isoaspartyl-O-methyltransferase (PIMT) for enzymatic conversion to 18O-labelled Lα-Asp.
  • Employed AspN degradation to remove endogenous Lα-Asp before PIMT reaction for enhanced detection.

Main Results:

  • Successfully identified several Asp isomerization sites in bovine lens α-crystallin.
  • Results were consistent with findings in human αA-crystallin, validating the method's effectiveness.
  • Demonstrated the utility of isoAsp-Quest for analyzing Lβ-Asp in biological samples.

Conclusions:

  • The isoAsp-Quest strategy provides a robust method for analyzing aspartyl isomerization.
  • This approach is valuable for protein product quality control and biomarker discovery.
  • The method enables straightforward and rapid identification of isoAsp modifications.