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Study · Not a test of the peptide alone · 1987

3 results

Structure, solubility and reactivity of peptides. A conformational study of two protected key intermediates from a large-scale synthesis of thymosin alpha 1.

Toniolo C, Bonora GM, Heimer EP, Felix AM

International journal of peptide and protein research1 Aug 1987Cited by 3 (Europe PMC)

PMID3679672 (opens in a new tab)DOI10.1111/j.1399-3011.1987.tb03331.x (opens in a new tab)PepBankPUB-03679672
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, Thymosin alpha-1 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 Thymosin alpha-1.

  1. 01LabNot a test of Thymosin alpha-1 aloneIn vitro (cell-free)Mechanism

    Infrared absorption and circular dichroism showed random coil, self-associated beta-structure and alpha-helix conformations in protected thymosin alpha‑1 segments, with the helix only in the longer segment.

    In plain wordsIn lab tests, protected pieces of thymosin alpha‑1 took several shapes depending on the solvent.

    Peptide
    Thymosin alpha-1
    Outcome
    Not applicableConformation of protected thymosin alpha 1 segments
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    By using infrared absorption and circular dichroism techniques the occurrence of the random coil conformation, the self-associated beta-structure, and the alpha-helix (the latter adopted only by the longer peptide) was established.

    In this study, Thymosin alpha-1 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 Thymosin alpha-1.

  2. 02LabNot a test of Thymosin alpha-1 aloneIn vitro (cell-free)Mechanism

    The tendency of the protected thymosin alpha‑1 segments to aggregate is paralleled by a decrease in their solubility.

    In plain wordsIn lab tests, protected pieces of thymosin alpha‑1 that clumped together were less soluble.

    Peptide
    Thymosin alpha-1
    Outcome
    Not applicableAggregation and solubility of protected thymosin alpha 1 segments
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    The tendency of these peptides to aggregate is paralleled by a decrease in their solubility.

    In this study, Thymosin alpha-1 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 Thymosin alpha-1.

  3. 03LabNot a test of Thymosin alpha-1 aloneIn vitro (cell-free)Mechanism

    The self-associated species of the two protected thymosin alpha‑1 segments were disrupted by adding hexamethylphosphoramide or by dilution.

    In plain wordsIn lab tests, clumped pieces of protected thymosin alpha‑1 came apart when a solvent was added or when they were diluted.

    Peptide
    Thymosin alpha-1
    Outcome
    Not applicableDisruption of self-associated protected thymosin alpha 1 segments
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    The self-associated species of the two peptide segments were disrupted either by adding increasing amounts of hexamethylphosphoramide or by dilution.

    In this study, Thymosin alpha-1 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 Thymosin alpha-1.

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 3Current

    10 Oct 2026, 08:55 UTC

    Study results updated

  2. Version 2

    9 Oct 2026, 03:03 UTC

    Study data updated · source update from Europe PMC

  3. Version 1

    9 Oct 2026, 03:02 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

Publication types

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