Enzymatic Ligation of Disulfide-Rich Animal Venom Peptides: Using Sortase A to Form Double-Knotted Peptides.

Poanna Tran, Christina I Schroeder

Open access · greenAbstract read

In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

–field-weighted citation impact, top 87% of its field

1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Poanna TranInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, Australia.

Christina I SchroederInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, Australia. christina.schroeder@nih.gov.

University of Queensland · AU

Funding

Discovery and development of voltage-gated sodium channel inhibitorsZIABC012003 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SCHROEDER, INGRID · 2020 to 2022

$291k

Intramural NIH HHS ZIA BC012003

6 · The paper itself

Abstract

Sortase A is a thiol transpeptidase expressed by Gram-positive bacteria. This enzyme is capable of site-specifically ligating peptides containing the C-terminal recognition motif LPXTG to peptides containing an N-terminal polyglycine sequence, forming a native peptide bond. Here, we describe the preparation and application of sortase A to the ligation of two individually folded disulfide-rich animal venom peptides in order to form a heterodimeric double-knotted peptide with a native peptide linker. This method is mild enough to preserve the structures and disulfide connectivities of the peptides during ligation. We employed a highly efficient sortase A pentamutant (SrtA5°), which brings the reaction to completion within 15 min with a ~50-80% yield of ligated peptide.

Indexed as

VenomsAminoacyltransferasesAnimalsBacterial ProteinsCysteine EndopeptidasesDisulfidesPeptidesAminoacyltransferasesBacterial ProteinsCysteine EndopeptidasesDisulfidesPeptidessortase AVenomsDisulfide-rich peptideDouble-knotted peptideEnzymatic ligationSite-specific ligationSortase ATranspeptidase

Identifiers

PMID34386952

DOI10.1007/978-1-0716-1617-8_8

PMCPMC10795843

OpenAlexW3187466039

What OpenQuestion holds

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LicenceTDM

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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.