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Study · In vitro (cell-free) · 2016

2 results

Thymosin α1 Interacts with Exposed Phosphatidylserine in Membrane Models and in Cells and Uses Serum Albumin as a Carrier.

Mandaliti W, Nepravishta R, Sinibaldi Vallebona P, Pica F, Garaci E, Paci M

Biochemistry3 Mar 2016Cited by 18 (Europe PMC)

PMID26909491 (opens in a new tab)DOI10.1021/acs.biochem.5b01345 (opens in a new tab)PepBankPUB-26909491
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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

2 results from studies that gave the peptide. No result from this study comes from people.

  1. 01LabIn vitro (cell-free)Mechanism

    By NMR, Thymosin α1 interacted with mixed phospholipid membranes when the membrane was negatively charged by exposed phosphatidylserine.

    In plain wordsIn lab tests, thymosin alpha‑1 bound to membranes only when they carried a negative charge from phosphatidylserine.

    Peptide
    Thymosin alpha-1
    Outcome
    Not applicableInteraction with phosphatidylserine-exposing membranes
    Study

    n: not reported in source

    Mixed phosphatidylcholine and phosphatidylserine membranes (NMR)
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    The results indicate that interaction occurs when the membrane is negatively charged by exposing phosphatidylserine.
    1 context sentence
    Summary · context
    This study reports on Thymosin α1's interaction with mixed phospholipids phosphatidylcholine and phosphatidylserine, the negative component of the membranes, by ¹H and natural abundance ¹⁵N nuclear magnetic resonance (NMR).
  2. 02LabIn vitro (cell-free)Mechanism

    By NMR, the C-terminal region of Thymosin α1 was involved in the interaction with human serum albumin.

    In plain wordsIn lab tests, the end part of thymosin alpha‑1 took part in binding to human serum albumin.

    Peptide
    Thymosin alpha-1
    Outcome
    Not applicableInteraction with human serum albumin
    Study

    n: not reported in source

    Human serum albumin (NMR)
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Steady-state saturation transfer, transfer nuclear Overhauser effect spectroscopy, and diffusion-ordered spectroscopy methodologies all reveal that the C-terminal region of Thymosin α1 is involved in the interaction with serum albumin.
    1 context sentence
    Summary · context
    This study reports on Thymosin α1's interaction with mixed phospholipids phosphatidylcholine and phosphatidylserine, the negative component of the membranes, by ¹H and natural abundance ¹⁵N nuclear magnetic resonance (NMR).

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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