Characterizing the D-Amino Acid Position in Peptide Epimers by Using Higher-Energy Collisional Dissociation Tandem Mass Spectrometry: A Case Study of Liraglutide
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) fragmentat...
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| Format: | Article |
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MDPI AG
2024-01-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/25/3/1379 |
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| author | Yuan-Chih Chen Hsin-Yi Wu Lung-Cheng Lin Chih-Wei Chang Pao-Chi Liao |
| author_facet | Yuan-Chih Chen Hsin-Yi Wu Lung-Cheng Lin Chih-Wei Chang Pao-Chi Liao |
| author_sort | Yuan-Chih Chen |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-08T03:56:14Z |
| format | Article |
| id | doaj.art-0c446af51719465990e80fec6bbbd37b |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-08T03:56:14Z |
| publishDate | 2024-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-0c446af51719465990e80fec6bbbd37b2024-02-09T15:13:02ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672024-01-01253137910.3390/ijms25031379Characterizing the D-Amino Acid Position in Peptide Epimers by Using Higher-Energy Collisional Dissociation Tandem Mass Spectrometry: A Case Study of LiraglutideYuan-Chih Chen0Hsin-Yi Wu1Lung-Cheng Lin2Chih-Wei Chang3Pao-Chi Liao4Department of Environmental and Occupational Health, College of Medicine, National Cheng Kung University, Tainan 704, TaiwanInstrumentation Center, National Taiwan University, Taipei 106, TaiwanScinoPharm Taiwan, Ltd., Tainan 741, TaiwanDepartment of Environmental and Occupational Health, College of Medicine, National Cheng Kung University, Tainan 704, TaiwanDepartment of Environmental and Occupational Health, College of Medicine, National Cheng Kung University, Tainan 704, TaiwanD-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.https://www.mdpi.com/1422-0067/25/3/1379chiralityhigh-resolution mass spectrometryD-amino acid-containing peptidehigher-energy collisional dissociation |
| spellingShingle | Yuan-Chih Chen Hsin-Yi Wu Lung-Cheng Lin Chih-Wei Chang Pao-Chi Liao Characterizing the D-Amino Acid Position in Peptide Epimers by Using Higher-Energy Collisional Dissociation Tandem Mass Spectrometry: A Case Study of Liraglutide International Journal of Molecular Sciences chirality high-resolution mass spectrometry D-amino acid-containing peptide higher-energy collisional dissociation |
| title | Characterizing the D-Amino Acid Position in Peptide Epimers by Using Higher-Energy Collisional Dissociation Tandem Mass Spectrometry: A Case Study of Liraglutide |
| title_full | Characterizing the D-Amino Acid Position in Peptide Epimers by Using Higher-Energy Collisional Dissociation Tandem Mass Spectrometry: A Case Study of Liraglutide |
| title_fullStr | Characterizing the D-Amino Acid Position in Peptide Epimers by Using Higher-Energy Collisional Dissociation Tandem Mass Spectrometry: A Case Study of Liraglutide |
| title_full_unstemmed | Characterizing the D-Amino Acid Position in Peptide Epimers by Using Higher-Energy Collisional Dissociation Tandem Mass Spectrometry: A Case Study of Liraglutide |
| title_short | Characterizing the D-Amino Acid Position in Peptide Epimers by Using Higher-Energy Collisional Dissociation Tandem Mass Spectrometry: A Case Study of Liraglutide |
| title_sort | characterizing the d amino acid position in peptide epimers by using higher energy collisional dissociation tandem mass spectrometry a case study of liraglutide |
| topic | chirality high-resolution mass spectrometry D-amino acid-containing peptide higher-energy collisional dissociation |
| url | https://www.mdpi.com/1422-0067/25/3/1379 |
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