Repozytorium

Hydrogen-deuterium exchange of α-carbon protons and fragmentation pathways in N-methylated glycine and alanine-containing peptides derivatized by quaternary ammonium salts.

Autorzy

Remigiusz Bąchor

Magdalena Rudowska

Alicja Kluczyk

Piotr Stefanowicz

Zbigniew Szewczuk

Rok wydania

2014

Czasopismo

Journal of Mass Spectrometry

Numer woluminu

49

Strony

529-536

DOI

10.1002/jms.3371

Kolekcja

Naukowa

Język

Angielski

Typ publikacji

Artykuł

Streszczenie

Recently, we developed a selective and efficient method of hydrogen‐deuterium exchange (HDX) at the α‐carbon (α‐C) of sarcosine residue (N‐methylglycine) in model peptides [Bąchor et al. J . Mass Spectrom . 2014, 49 , 43]. Here, we report the influence of quaternary ammonium (QA) group on HDX at the α‐C of sarcosine and N‐methylalanine in peptides. The obtained results suggest a significant acceleration of the HDX in sarcosine residue caused by the presence of QA. The effect depends on the distance between the sarcosine residue and QA moiety. The deuterons, introduced at α‐C, are resistant to the back‐exchange in acidic aqueous solution. The collision induced dissociation of the deuterium‐labeled analogs of QA‐tagged oligosarcosine peptides without mobile hydrogen revealed the mobilization of the hydrogens localized at α‐C of sarcosine residue.

Słowa kluczowe

HDX of peptides, quaternary ammonium salts, ESI‐MS/MS, sarcosine, charge-remote fragmentation

Adres publiczny

http://dx.doi.org/10.1002/jms.3371

Strona internetowa wydawcy

onlinelibrary.wiley.com

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