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Study · Not a test of the peptide alone · 2015

2 results

Production of cell-penetrating peptides in Escherichia coli using an intein-mediated system.

Rodríguez V, Lascani J, Asenjo JA, Andrews BA

Applied biochemistry and biotechnology14 Jan 2015Cited by 6 (Europe PMC)

PMID25586490 (opens in a new tab)DOI10.1007/s12010-015-1484-7 (opens in a new tab)PepBankPUB-25586490
Publisher pagePubMedAsk about this study
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Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study2

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone2

In this study, PNC-27 was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking PNC-27.

  1. 01LabNot a test of PNC-27 aloneIn vitro (cells)Other

    In Escherichia coli, pTXB1 and pTYB11 vectors were suitable for recombinant production of PNC27 and p53pAnt peptides.

    In plain wordsIn lab tests, both vector systems were suitable for producing PNC27 and p53pAnt peptides in bacteria.

    Peptide
    PNC-27
    Outcome
    Not applicableRecombinant production suitability
    Study

    Escherichia colin: not reported in source

    recombinant Escherichia coli production system
    Outcome group
    Synthesis and manufacturing · Pharmacology

    Source sentences

    Summary
    It was demonstrated that the pTXB1 and the pTYB11 vector systems are suitable for production of this kind of peptides.
    1 context sentence
    Summary · context
    In this work, an intein-mediated system was used to evaluate Escherichia coli recombinant production of p53pAnt and PNC27 anticancer cell-penetrating peptides.

    In this study, PNC-27 was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking PNC-27.

  2. 02LabNot a test of PNC-27 aloneIn vitro (cells)Other

    In recombinant production, low-temperature induction and on-column intein-mediated cleavage allowed effective recovery of PNC27 and p53pAnt peptides in one chromatographic step.

    In plain wordsIn lab tests, the production process recovered PNC27 and p53pAnt peptides using one chromatography step.

    Peptide
    PNC-27
    Outcome
    Not applicablePeptide recovery
    Study

    Escherichia colin: not reported in source

    recombinant Escherichia coli production system
    Outcome group
    Synthesis and manufacturing · Pharmacology

    Source sentences

    Summary
    The production process involves a low-temperature induction process and an efficient on-column intein-mediated cleavage, which allowed an effective peptide recovery using a single chromatographic step.
    1 context sentence
    Summary · context
    In this work, an intein-mediated system was used to evaluate Escherichia coli recombinant production of p53pAnt and PNC27 anticancer cell-penetrating peptides.

    In this study, PNC-27 was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking PNC-27.

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Version 2Current

    21 Oct 2026, 15:58 UTC

    Study results updated

  2. Version 1

    21 Oct 2026, 12:50 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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