alexa Unusual Peptide Fragment Ions In Low-energy CID Process By Charge-remote Fragmentation Pathways
ISSN: 2157-7064

Journal of Chromatography & Separation Techniques
Open Access

Like us on:
OMICS International organises 3000+ Global Conferenceseries Events every year across USA, Europe & Asia with support from 1000 more scientific Societies and Publishes 700+ Open Access Journals which contains over 50000 eminent personalities, reputed scientists as editorial board members.

Open Access Journals gaining more Readers and Citations

700 Journals and 15,000,000 Readers Each Journal is getting 25,000+ Readers

This Readership is 10 times more when compared to other Subscription Journals (Source: Google Analytics)

Share This Page

Additional Info

Loading Please wait..

4th World Congress on MASS SPECTROMETRY
June 19-21, 2017 London, UK

Xinhua Guo
Jilin University, China
ScientificTracks Abstracts: J Chromatogr Sep Tech
DOI: 10.4172/2157-7064-C1-025
Several unusual peptide fragment ions including bn-44, cn and bn+H2O ions are initially observed in the MS/MS spectrum of a singly charged deuterohemine N-terminated peptide (DhHP-6, deuterohemine-βAHTVEK-NH2). A detailed investigation on formation pathways of these characteristic ions are performed by using high resolution mass determination, H/D exchange, isotope labeling and density functional theory (DFT). Results indicate that the production of these ions is related to the presence of threonine (Thr) residue in the peptide. Also the N-terminal fixed charge carried by deuterohemine group may play a critical role for the activation of the hydrogen connecting with carbon, and McLafferty-type rearrangement reactions are proposed as the potential mechanism for explaining the generation of the bn-CH3CHO and cn ions. In this study, we also propose a rearrangement fragmentation pathway for the production of bn+H2O ions from the Thr/Ser residue. In that case, the N→O acyl shift occurs to generate an ester intermediate which is the first and the most critical step, following that a further fragmentation of the ester isomer leads to the formation of bn+H2O ions. Detections of these diagnostic ions from the MS/MS spectra of sodiated Thr containing peptides further support the proposed charge-remote fragmentation pathways. Present work provides mechanism insights into the production of special ions, such as cn and bn+H2O ions, in the low energy collision-induced dissociation (CID) process.

Xinhua Guo completed her PhD in 2004 at University of the Sciences, US. Currently, she is a Full Professor at College of Chemistry, Jilin University, China. Her research interests include “The development of various methods for structural studies and assemblies of DNA strands, new matrixes and materials for sensitive MALDI-MS analysis and studies of peptide fragmentation mechanism”. She has published more than 30 scientific articles. She was a member of council of Chinese Mass Spectrometry Society (CMSS) from 2008-2016.

Email: [email protected]

image PDF   |   image HTML
Peer Reviewed Journals
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version