Stereospecific control of peptide gas-phase ion chemistry with cis and trans cyclo ornithine residues

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F18%3A00489619" target="_blank" >RIV/61388963:_____/18:00489619 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.1002/jms.4047" target="_blank" >http://dx.doi.org/10.1002/jms.4047</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/jms.4047" target="_blank" >10.1002/jms.4047</a>

Result language

angličtina

Original language name

Stereospecific control of peptide gas-phase ion chemistry with cis and trans cyclo ornithine residues

Original language description

We report non-chiral amino acid residues cis- and trans-1,4-diaminocyclohexane-1-carboxylic acid (cyclo-ornithine, cO) that exhibit unprecedented stereospecific control of backbone dissociations of singly charged peptide cations and hydrogen-rich cation radicals produced by electron-transfer dissociation. Upon collision-induced dissociation (CID) in the slow heating regime, peptide cations containing trans-cO residues undergo facile backbone cleavages of amide bonds C-terminal to trans-cO. By contrast, peptides with cis-cO residues undergo dissociations at several amide bonds along the peptide ion backbone. Diastereoisomeric cO-containing peptides thus provide remarkably distinct tandem mass spectra. The stereospecific effect in CID of the trans-cO residue is explained by syn-facially directed proton transfer from the 4-ammonium group at cO to the C-terminal amide followed by neighboring group participation in the cleavage of the CO-NH bond, analogous to the aspartic acid and ornithine effects. Backbone dissociations of diastereoisomeric cO-containing peptide ions generate distinct [b(n)](+)-type fragment ions that were characterized by CID-MS3 spectra. Stereospecific control is also reported for electron-transfer dissociation of cis- and trans-cO containing doubly charged peptide ions. The stereospecific effect upon electron transfer is related to the different conformations of doubly charged peptide ions that affect the electron attachment sites and ensuing N-C alpha bond dissociations.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10406 - Analytical chemistry

Project

—

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2018

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Mass Spectrometry

ISSN

1076-5174

e-ISSN

—

Volume of the periodical

53

Issue of the periodical within the volume

2

Country of publishing house

GB - UNITED KINGDOM

Number of pages

14

Pages from-to

124-137

UT code for WoS article

000425189400004

EID of the result in the Scopus database

2-s2.0-85040721260