Exploring the Diversity of Cysteine-Rich Natural Product Peptides via MS/MS Fingerprint Ions.
Exploring the Diversity of Cysteine-Rich Natural Product Peptides via MS/MS Fingerprint Ions.
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DOI:
10.1021/jasms.0c00078
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发表时间:
2020-09-02
影响因子:
3.2
通讯作者:
Hicks LM
中科院分区:
文献类型:
--
作者:
Parsley NC;Williams OL;Hicks LM
Natural product extracts present inherently complex matrices in which the identification of novel bioactive peptide species is challenged by low abundance masses and significant structural and sequence diversity. Additionally, discovery efforts often result in the re-identification of known compounds, where modifications derived in vivo or during sample handling may obscure true sequence identity. Herein, we identify mass spectral (MS2) “fingerprint” ions characteristic of cyclotides, a diverse and biologically active family of botanical cysteine-rich peptides, based on regions of high sequence homology. We couple mass shift analysis with MS2 spectral fingerprint ions cross referenced with CyBase - a cyclotide database - to discern unique mass species in Viola communis extracts from mass species that are likely already characterized and those with common modifications. The approach is extended to a related class of cysteine-rich peptide, the trypsin inhibitors, using the characterized botanical species Lagenaria siceraria. Coupling the observation of highly abundant MS2 ions with mass shift analysis, we identify a new set of small, highly disulfide bound cysteine-rich L. siceraria peptides. We identify mass spectral (MS2) “fingerprint” ions characteristic of cyclotides, a diverse and biologically active family of botanical cysteine-rich peptides, based on regions of high sequence homology. Mass shift analysis is coupled with MS2 spectral fingerprint ions to discern unique mass species in Viola extracts from mass species that are likely already characterized and those with common modifications.
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影响因子:
5.6
作者:
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通讯作者:
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DOI:
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