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Study · Not a test of the peptide alone · 2004

3 results

NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein that is selectively cytotoxic to cancer cells.

Rosal R, Pincus MR, Brandt-Rauf PW, Fine RL, Michl J, Wang H

Biochemistry1 Feb 2004Cited by 28 (Europe PMC)

PMID14967026 (opens in a new tab)DOI10.1021/bi035718g (opens in a new tab)PepBankPUB-14967026
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 study3

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

Studies that did not test the peptide alone3

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 (cell-free)Other

    In aqueous solution, PNC‑27 formed an S-shaped structure with three helical domains and another similar, less helical structure.

    In plain wordsIn lab tests, PNC‑27 formed an S-shaped structure and a similar structure with less helix in water.

    Peptide
    PNC-27
    Outcome
    Not applicableAqueous solution conformation
    Study

    n: not reported in source

    Outcome group
    Peptide structure and chemistry · Pharmacology

    Source sentences

    Summary
    In an aqueous milieu, PNC-27 contains three alpha-helical domains connected by loop structures, forming an S shape, and another similar structure with less helical structure.
    1 context sentence
    Summary · context
    To determine the role of solution structure in this peptide's selective and rapid tumor membrane disruptive behavior, we have performed two-dimensional NMR on a 32-residue sequence called PNC-27, in both an aqueous cytosolic-like and a mixed organic membrane-mimetic solution environment.

    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 (cell-free)Other

    In membrane-mimetic solution, PNC‑27 helical domains lengthened and formed three classes of U-shaped helix-coil-helix structures.

    In plain wordsIn lab tests, PNC‑27 helices became longer in membrane-like solution and formed U-shaped structures.

    Peptide
    PNC-27
    Outcome
    IncreaseMembrane-mimetic conformation
    Study

    n: not reported in source

    Outcome group
    Peptide structure and chemistry · Pharmacology

    Source sentences

    Summary
    In a solution environment simulating a membrane, the helical domains found in water increase in length, forming three classes of structures, all of which form a U-shaped helix-coil-helix ensemble.
    1 context sentence
    Summary · context
    To determine the role of solution structure in this peptide's selective and rapid tumor membrane disruptive behavior, we have performed two-dimensional NMR on a 32-residue sequence called PNC-27, in both an aqueous cytosolic-like and a mixed organic membrane-mimetic solution environment.

    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.

  3. 03LabNot a test of PNC-27 aloneIn vitro (cell-free)Other

    In both solvent systems, PNC‑27 formed amphipathic structures with hydrophobic and polar residues on opposite faces.

    In plain wordsIn lab tests, PNC‑27 placed water-repelling and water-attracting residues on opposite faces in both solutions.

    Peptide
    PNC-27
    Outcome
    Not applicableAmphipathic residue arrangement
    Study

    n: not reported in source

    Outcome group
    Peptide structure and chemistry · Pharmacology

    Source sentences

    Summary
    In both solvent systems, this peptide forms amphipathic structures such that its hydrophobic residues coalesce on one face while the polar residues aggregate on the opposite face.
    1 context sentence
    Summary · context
    To determine the role of solution structure in this peptide's selective and rapid tumor membrane disruptive behavior, we have performed two-dimensional NMR on a 32-residue sequence called PNC-27, in both an aqueous cytosolic-like and a mixed organic membrane-mimetic solution environment.

    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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