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Study · Not a test of the peptide alone · 1998

5 results

The conformation of peptide thymosin alpha 1 in solution and in a membrane-like environment by circular dichroism and NMR spectroscopy. A possible model for its interaction with the lymphocyte membrane.

Grottesi A, Sette M, Palamara T, Rotilio G, Garaci E, Paci M

Peptides1 Jan 1998Cited by 28 (Europe PMC)

PMID9880079 (opens in a new tab)DOI10.1016/s0196-9781(98)00132-6 (opens in a new tab)PepBankPUB-09880079
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 study5

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

Studies that did not test the peptide alone5

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

    In water solution, circular dichroism showed that thymosin alpha1 does not assume a preferred conformation.

    In plain wordsIn lab tests, thymosin alpha1 had no fixed shape in plain water.

    Peptide
    Thymosin alpha-1
    Outcome
    Not applicableConformation in water
    Study

    n: not reported in source

    Peptide in solution, circular dichroism and NMR
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Circular dichroism indicates that thymosin alpha1 in water solution does not assume a preferred conformation
    1 context sentence
    Summary · context
    The 28-residue peptide thymosin alpha1 was studied by circular dichroism and two-dimensional NMR.

    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

    In lab tests with phospholipid vesicles and sodium dodecyl sulphate, thymosin alpha1 assumed a partly structured conformation.

    In plain wordsIn lab tests, thymosin alpha1 took a partly ordered shape with membrane-like vesicles or detergent.

    Peptide
    Thymosin alpha-1
    Outcome
    Not applicableConformation with vesicles and SDS
    Study

    n: not reported in source

    Peptide in solution, circular dichroism and NMR
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    while in the presence of small unilamellar vesicles of dimiristoylphosphatidylcholine and dimiristoylphosphatidic acid (10:1) and in sodium dodecyl sulphate, it assumes a partly structured conformation.
    1 context sentence
    Summary · context
    The 28-residue peptide thymosin alpha1 was studied by circular dichroism and two-dimensional NMR.

    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

    In lab tests, zinc ions produced similar conformational effects on thymosin alpha1.

    In plain wordsIn lab tests, zinc ions had a similar effect on the shape of thymosin alpha1.

    Peptide
    Thymosin alpha-1
    Outcome
    Not applicableConformation with zinc ions
    Study

    n: not reported in source

    Peptide in solution, circular dichroism and NMR
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Presence of zinc ions produces similar effects.
    1 context sentence
    Summary · context
    The 28-residue peptide thymosin alpha1 was studied by circular dichroism and two-dimensional NMR.

    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.

  4. 04LabNot a test of Thymosin alpha-1 aloneIn vitro (cell-free)Mechanism

    In a water-2,2,2 trifluoroethanol mixed solvent, thymosin alpha1 adopted a structured conformation.

    In plain wordsIn lab tests, thymosin alpha1 took an ordered shape in a water-trifluoroethanol mixture.

    Peptide
    Thymosin alpha-1
    Outcome
    Not applicableConformation in water-trifluoroethanol
    Study

    n: not reported in source

    Peptide in solution, circular dichroism and NMR
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    In a more hydrophobic environment like a solution of a mixed solvent water-2,2,2 trifluoroethanol, it adopts a structured conformation.
    1 context sentence
    Summary · context
    The 28-residue peptide thymosin alpha1 was studied by circular dichroism and two-dimensional NMR.

    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.

  5. 05LabNot a test of Thymosin alpha-1 aloneIn vitro (cell-free)Mechanism

    NMR showed that thymosin alpha1 in the water-trifluoroethanol mixture has a beta-turn at residues 5 to 8 and an alpha helix at residues 17 to 24.

    In plain wordsIn lab tests, NMR showed thymosin alpha1 has a turn near residues 5 to 8 and a helix near residues 17 to 24.

    Peptide
    Thymosin alpha-1
    Outcome
    Not applicableNMR secondary structure
    Study

    n: not reported in source

    Peptide in solution, circular dichroism and NMR
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Measurements

    beta-turn start residue
    5 residue
    water-TFE
    beta-turn end residue
    8 residue
    water-TFE
    alpha helix start residue
    17 residue
    water-TFE
    alpha helix end residue
    24 residue
    water-TFE

    Source sentences

    Summary
    NMR spectra indicated that in this mixture as solvent, thymosin alpha1 has a structure characterized by two regions. A beta-turn is present between residue 5 and residue 8, while the region between residues 17 and 24 shows an alpha helix conformation.
    1 context sentence
    Summary · context
    The 28-residue peptide thymosin alpha1 was studied by circular dichroism and two-dimensional NMR.

    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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