Proteomics

Dataset Information

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PepSAVI-MS reveals proline-rich antimicrobial peptide in Amaranthus tricolor


ABSTRACT: PepSAVI-MS, a mass spectrometry-based peptidomics pipeline, was implemented for antimicrobial peptide (AMP) discovery in the medicinal plant Amaranthus tricolor. This investigation revealed a novel 1.7 kDa AMP, deemed Atr-AMP1. Initial efforts to determine the sequence of Atr-AMP1 utilized chemical derivatization and enzymatic digestion to provide information about specific residues and post-translational modifications. EThcD (electron-transfer/higher-energy collision dissociation) produced extensive backbone fragmentation and facilitated de novo sequencing, the results of which were consistent with orthogonal characterization experiments. Additionally, multistage HCD (higher-energy collisional dissociation) facilitated discrimination between isobaric leucine and isoleucine. These results revealed a positively-charged proline-rich peptide present in a heterogeneous population of multiple peptidoforms, possessing several post-translational modifications including a disulfide bond, methionine oxidation, and proline hydroxylation.

INSTRUMENT(S): Orbitrap Fusion Lumos, TripleTOF 5600

ORGANISM(S): Amaranthus Tricolor

TISSUE(S): Leaf

SUBMITTER: Tessa Bartges  

LAB HEAD: Leslie Hicks

PROVIDER: PXD014547 | Pride | 2020-05-26

REPOSITORIES: Pride

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Publications

PepSAVI-MS Reveals a Proline-rich Antimicrobial Peptide in <i>Amaranthus tricolor</i>.

Moyer Tessa B TB   Heil Lilian R LR   Kirkpatrick Christine L CL   Goldfarb Dennis D   Lefever William A WA   Parsley Nicole C NC   Wommack Andrew J AJ   Hicks Leslie M LM  

Journal of natural products 20190926 10


Traditional medicinal plants are a rich source of antimicrobials; however, the bioactive peptide constituents of most ethnobotanical species remain largely unexplored. Herein, PepSAVI-MS, a mass spectrometry-based peptidomics pipeline, was implemented for antimicrobial peptide (AMP) discovery in the medicinal plant <i>Amaranthus tricolor</i>. This investigation revealed a novel 1.7 kDa AMP with strong activity against <i>Escherichia coli</i> ATCC 25922, deemed Atr-AMP1. Initial efforts to determ  ...[more]

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