Characterizing the D-Amino Acid Position in Peptide Epimers by Using Higher-Energy Collisional Dissociation Tandem Mass Spectrometry: A Case Study of Liraglutide.

Yuan-Chih Chen, Hsin-Yi Wu, Lung-Cheng Lin, Chih-Wei Chang, Pao-Chi Liao

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Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 authors at 3 institutions in 1 country.

Yuan-Chih ChenDepartment of Environmental and Occupational Health, College of Medicine, National Cheng Kung University, Tainan 704, Taiwan.

Hsin-Yi WuInstrumentation Center, National Taiwan University, Taipei 106, Taiwan.ORCID 0000-0003-0722-0201

Lung-Cheng LinScinoPharm Taiwan, Ltd., Tainan 741, Taiwan.

Chih-Wei ChangDepartment of Environmental and Occupational Health, College of Medicine, National Cheng Kung University, Tainan 704, Taiwan.

Pao-Chi LiaoDepartment of Environmental and Occupational Health, College of Medicine, National Cheng Kung University, Tainan 704, Taiwan.ORCID 0000-0001-8510-9870

National Cheng Kung University · TWNational Taiwan University · TWScinoPharm Taiwan (Taiwan) · TW

Funding

National Science and Technology Council MOST110-2113-M-006-014National Science and Technology Council MOST111-2113-M-006-011National Science and Technology Council NSTC112-2113-M-006-002Southern Taiwan Science Park 110CB-1-01

6 · The paper itself

Abstract

D-amino acid-containing peptides (DAACPs) occur in biological and artificial environments. Since the importance of DAACPs has been recognized, various mass spectrometry-based analytical approaches have been developed. However, the capability of higher-energy collisional dissociation (HCD) fragmentation to characterize DAACP sites has not been evaluated. In this study, we compared the normalized spectra intensity under different conditions of HCD and used liraglutide along with its DAACPs as examples. Our results indicated that the difference in the intensity of y ions between DAACPs and all-L liraglutide could not only distinguish them but also localize the sites of D-amino acids in the DAACPs. Our data demonstrate the potential of using HCD for the site characterization of DAACPs, which may have great impact in biological studies and peptide drug development.

Indexed as

LiraglutideTandem Mass SpectrometryAmino AcidsPeptidesAmino AcidsLiraglutidePeptideschiralityD-amino acid-containing peptidehigher-energy collisional dissociationhigh-resolution mass spectrometry

Identifiers

PMID38338662

DOI10.3390/ijms25031379

PMCPMC10855602

OpenAlexW4391133928

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LicenceCC BY

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.