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Title: Improving peptide fragmentation by N-terminal derivatization with high proton affinity.
Authors: Miyashita, Masahiro  kyouindb  KAKEN_id
Hanai, Yosuke
Awane, Hiroyuki
Yoshikawa, Toru
Miyagawa, Hisashi  kyouindb  KAKEN_id  orcid (unconfirmed)
Author's alias: 宮下, 正弘
Issue Date: 15-May-2011
Publisher: wiley
Journal title: Rapid communications in mass spectrometry
Volume: 25
Issue: 9
Start page: 1130
End page: 1140
Abstract: An improved method of de novo peptide sequencing based on mass spectrometry using novel N-terminal derivatization reagents with high proton affinity has been developed. The introduction of a positively charged group into the N-terminal amino group of a peptide is known to enhance the relative intensity of b-ions in product ion spectra, allowing the easy interpretation of the spectra. However, the physicochemical properties of charge derivatization reagents required for efficient fragmentation remain unclear. In this study, we prepared several derivatization reagents with high proton affinity, which are thought to be appropriate for peptide fragmentation under low-energy collision-induced dissociation (CID) conditions, and examined their usefulness in de novo peptide sequencing. Comparison of the effects on fragmentation among three derivatization reagents having a guanidino or an amidino moiety, which differ in proton affinity, clearly indicated that there was an optimal proton affinity for efficient fragmentation of peptides. Among reagents tested in this study, derivatization with 4-amidinobenzoic acid brought about the most effective fragmentation. This derivatization approach will offer a novel de novo peptide sequencing method under low-energy CID conditions.
Description: Article first published online: 12 APR 2011
Rights: This is the peer reviewed version of the following article: Miyashita, M., Hanai, Y., Awane, H., Yoshikawa, T. and Miyagawa, H. (2011), Improving peptide fragmentation by N-terminal derivatization with high proton affinity. Rapid Commun. Mass Spectrom., 25: 1130–1140, which has been published in final form at This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.
This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。
DOI(Published Version): 10.1002/rcm.4962
PubMed ID: 21488112
Appears in Collections:Journal Articles

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