Fingerprinting desmosine-containing elastin peptides

Christoph U Schräder; Andrea Heinz; Petra Majovsky; Christian E H Schmelzer

doi:10.1007/s13361-014-1075-9

Fingerprinting desmosine-containing elastin peptides

Christoph U Schräder, Andrea Heinz, Petra Majovsky, Christian E H Schmelzer

10 Citations (Scopus)

Abstract

Abstract Elastin is a vital protein of the extracellular matrix of jawed vertebrates and provides elasticity to numerous tissues. It is secreted in the form of its soluble precursor tropoelastin, which is subsequently cross-linked in the course of the elastic fiber assembly. The process involves the formation of the two tetrafunctional amino acids desmosine (DES) and isodesmosine (IDES), which are unique to elastin. The resulting high degree of cross-linking confers remarkable properties, including mechanical integrity, insolubility, and long-term stability to the protein. These characteristics hinder the structural elucidation of mature elastin. However, MS² data of linear and cross-linked peptides released by proteolysis can provide indirect insights into the structure of elastin. In this study, we performed energy-resolved collision-induced dissociation experiments of DES, IDES, their derivatives, and DES-/IDES-containing peptides to determine characteristic product ions. It was found that all investigated compounds yielded the same product ion clusters at elevated collision energies. Elemental composition determination using the exact masses of these ions revealed molecular formulas of the type C_xH_yN, suggesting that the pyridinium core of DES/IDES remains intact even at relatively high collision energies. The finding of these specific product ions enabled the development of a similarity-based scoring algorithm that was successfully applied on LC-MS/MS data of bovine elastin digests for the identification of DES-/IDES-cross-linked peptides. This approach facilitates the straightforward investigation of native cross-links in elastin.

Original language	English
Journal	Journal of the American Society for Mass Spectrometry
Volume	26
Issue number	5
Pages (from-to)	762-73
Number of pages	12
ISSN	1044-0305
DOIs	https://doi.org/10.1007/s13361-014-1075-9
Publication status	Published - 1 May 2015

Keywords

Animals
Cattle
Chromatography, High Pressure Liquid
Cross-Linking Reagents
Desmosine
Elastin
Humans
Isodesmosine
Models, Molecular
Molecular Structure
Molecular Weight
Oligopeptides
Peptide Fragments
Peptide Mapping
Protein Stability
Proteolysis
Spectrometry, Mass, Electrospray Ionization
Stereoisomerism
Tandem Mass Spectrometry
Tropoelastin
Journal Article
Research Support, Non-U.S. Gov't

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10.1007/s13361-014-1075-9

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Cite this

@article{332dec3004494e168c1fd64a657ce78f,

title = "Fingerprinting desmosine-containing elastin peptides",

abstract = "Abstract Elastin is a vital protein of the extracellular matrix of jawed vertebrates and provides elasticity to numerous tissues. It is secreted in the form of its soluble precursor tropoelastin, which is subsequently cross-linked in the course of the elastic fiber assembly. The process involves the formation of the two tetrafunctional amino acids desmosine (DES) and isodesmosine (IDES), which are unique to elastin. The resulting high degree of cross-linking confers remarkable properties, including mechanical integrity, insolubility, and long-term stability to the protein. These characteristics hinder the structural elucidation of mature elastin. However, MS2 data of linear and cross-linked peptides released by proteolysis can provide indirect insights into the structure of elastin. In this study, we performed energy-resolved collision-induced dissociation experiments of DES, IDES, their derivatives, and DES-/IDES-containing peptides to determine characteristic product ions. It was found that all investigated compounds yielded the same product ion clusters at elevated collision energies. Elemental composition determination using the exact masses of these ions revealed molecular formulas of the type CxHyN, suggesting that the pyridinium core of DES/IDES remains intact even at relatively high collision energies. The finding of these specific product ions enabled the development of a similarity-based scoring algorithm that was successfully applied on LC-MS/MS data of bovine elastin digests for the identification of DES-/IDES-cross-linked peptides. This approach facilitates the straightforward investigation of native cross-links in elastin.",

keywords = "Animals, Cattle, Chromatography, High Pressure Liquid, Cross-Linking Reagents, Desmosine, Elastin, Humans, Isodesmosine, Models, Molecular, Molecular Structure, Molecular Weight, Oligopeptides, Peptide Fragments, Peptide Mapping, Protein Stability, Proteolysis, Spectrometry, Mass, Electrospray Ionization, Stereoisomerism, Tandem Mass Spectrometry, Tropoelastin, Journal Article, Research Support, Non-U.S. Gov't",

author = "Schr{\"a}der, {Christoph U} and Andrea Heinz and Petra Majovsky and Schmelzer, {Christian E H}",

year = "2015",

month = may,

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doi = "10.1007/s13361-014-1075-9",

language = "English",

volume = "26",

pages = "762--73",

journal = "Journal of the American Society for Mass Spectrometry",

issn = "1044-0305",

publisher = "Springer Nature",

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TY - JOUR

T1 - Fingerprinting desmosine-containing elastin peptides

AU - Schräder, Christoph U

AU - Heinz, Andrea

AU - Majovsky, Petra

AU - Schmelzer, Christian E H

PY - 2015/5/1

Y1 - 2015/5/1

N2 - Abstract Elastin is a vital protein of the extracellular matrix of jawed vertebrates and provides elasticity to numerous tissues. It is secreted in the form of its soluble precursor tropoelastin, which is subsequently cross-linked in the course of the elastic fiber assembly. The process involves the formation of the two tetrafunctional amino acids desmosine (DES) and isodesmosine (IDES), which are unique to elastin. The resulting high degree of cross-linking confers remarkable properties, including mechanical integrity, insolubility, and long-term stability to the protein. These characteristics hinder the structural elucidation of mature elastin. However, MS2 data of linear and cross-linked peptides released by proteolysis can provide indirect insights into the structure of elastin. In this study, we performed energy-resolved collision-induced dissociation experiments of DES, IDES, their derivatives, and DES-/IDES-containing peptides to determine characteristic product ions. It was found that all investigated compounds yielded the same product ion clusters at elevated collision energies. Elemental composition determination using the exact masses of these ions revealed molecular formulas of the type CxHyN, suggesting that the pyridinium core of DES/IDES remains intact even at relatively high collision energies. The finding of these specific product ions enabled the development of a similarity-based scoring algorithm that was successfully applied on LC-MS/MS data of bovine elastin digests for the identification of DES-/IDES-cross-linked peptides. This approach facilitates the straightforward investigation of native cross-links in elastin.

AB - Abstract Elastin is a vital protein of the extracellular matrix of jawed vertebrates and provides elasticity to numerous tissues. It is secreted in the form of its soluble precursor tropoelastin, which is subsequently cross-linked in the course of the elastic fiber assembly. The process involves the formation of the two tetrafunctional amino acids desmosine (DES) and isodesmosine (IDES), which are unique to elastin. The resulting high degree of cross-linking confers remarkable properties, including mechanical integrity, insolubility, and long-term stability to the protein. These characteristics hinder the structural elucidation of mature elastin. However, MS2 data of linear and cross-linked peptides released by proteolysis can provide indirect insights into the structure of elastin. In this study, we performed energy-resolved collision-induced dissociation experiments of DES, IDES, their derivatives, and DES-/IDES-containing peptides to determine characteristic product ions. It was found that all investigated compounds yielded the same product ion clusters at elevated collision energies. Elemental composition determination using the exact masses of these ions revealed molecular formulas of the type CxHyN, suggesting that the pyridinium core of DES/IDES remains intact even at relatively high collision energies. The finding of these specific product ions enabled the development of a similarity-based scoring algorithm that was successfully applied on LC-MS/MS data of bovine elastin digests for the identification of DES-/IDES-cross-linked peptides. This approach facilitates the straightforward investigation of native cross-links in elastin.

KW - Animals

KW - Cattle

KW - Chromatography, High Pressure Liquid

KW - Cross-Linking Reagents

KW - Desmosine

KW - Elastin

KW - Humans

KW - Isodesmosine

KW - Models, Molecular

KW - Molecular Structure

KW - Molecular Weight

KW - Oligopeptides

KW - Peptide Fragments

KW - Peptide Mapping

KW - Protein Stability

KW - Proteolysis

KW - Spectrometry, Mass, Electrospray Ionization

KW - Stereoisomerism

KW - Tandem Mass Spectrometry

KW - Tropoelastin

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1007/s13361-014-1075-9

DO - 10.1007/s13361-014-1075-9

M3 - Journal article

C2 - 25604393

SN - 1044-0305

VL - 26

SP - 762

EP - 773

JO - Journal of the American Society for Mass Spectrometry

JF - Journal of the American Society for Mass Spectrometry

IS - 5

ER -