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J Proteome Res. 2016 Dec 2;15(12):4403-4411. Epub 2016 Oct 11.

Examination of Endogenous Peptides in Medicago truncatula Using Mass Spectrometry Imaging.

Author information

1
Department of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.
2
Department of Agronomy, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.
3
Department of Biochemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.
4
Department of Bacteriology, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.
5
School of Pharmacy, University of Wisconsin-Madison , Madison, Wisconsin 53705, United States.

Abstract

Plant science is an important, rapidly developing area of study. Within plant science, one area of study that has grown tremendously with recent technological advances, such as mass spectrometry, is the field of plant-omics; however, plant peptidomics is relatively underdeveloped in comparison with proteomics and metabolomics. Endogenous plant peptides can act as signaling molecules and have been shown to affect cell division, development, nodulation, reproduction, symbiotic associations, and defense reactions. There is a growing need to uncover the role of endogenous peptides on a molecular level. Mass spectrometric imaging (MSI) is a valuable tool for biological analyses as it allows for the detection of thousands of analytes in a single experiment and also displays spatial information for the detected analytes. Despite the prediction of a large number of plant peptides, their detection and imaging with spatial localization and chemical specificity is currently lacking. Here we analyzed the endogenous peptides and proteins in Medicago truncatula using matrix-assisted laser desorption/ionization (MALDI)-MSI. Hundreds of endogenous peptides and protein fragments were imaged, with interesting peptide spatial distribution changes observed between plants in different developmental stages.

KEYWORDS:

MALDI; Medicago truncatula; imaging; mass spectrometry; orbitrap; peptides; peptidomics; plant science; proteins

PMID:
27726374
DOI:
10.1021/acs.jproteome.6b00471
[Indexed for MEDLINE]

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