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Study · In vitro (cell-free) · rat · 2004

6 results

[The binding of Semax, ACTH 4-10 heptapeptide, to plasma membranes of the rat forebrain basal nuclei and its biodegradation].

Dolotov OV, Zolotarev IuA, Dorokhova EM, Andreeva LA, Alfeeva LIu, Grivennikov IA, Miasoedov NF

Bioorganicheskaia khimiia1 May 2004Cited by 11 (Europe PMC)

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 study6

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

  1. 01LabIn vitro (cell-free)Activity measurement

    In plasma membranes of rat forebrain basal nuclei, binding of labeled semax was time-dependent, specific and reversible.

    In plain wordsIn lab tests on rat brain membranes, semax bound in a time-dependent, specific and reversible way.

    Peptide
    Semax
    Outcome
    Not applicableBinding to plasma membranes
    Study

    ratn: not reported in source

    Plasma membranes of rat forebrain basal nuclei
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Binding of the homogeneously labeled [G-3H]Semax was shown to be time-dependent, specific, and reversible.
    1 context sentence
    Summary · context
    The binding characteristics of the peptide Semax (Met-Glu-His-Phe-Pro-Gly-Pro) to plasma membranes of basal nuclei of the rat forebrain and the dynamics of its degradation during its incubation with these membranes were studied.
  2. 02LabIn vitro (cell-free)Activity measurement

    In plasma membranes of rat forebrain basal nuclei, specific binding of semax depended on calcium ions.

    In plain wordsIn lab tests on rat brain membranes, semax binding needed calcium ions.

    Peptide
    Semax
    Outcome
    Not applicableCalcium dependence of binding
    Study

    ratn: not reported in source

    Plasma membranes of rat forebrain basal nuclei
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Specific binding of the heptapeptide depended on calcium ions
    1 context sentence
    Summary · context
    The binding characteristics of the peptide Semax (Met-Glu-His-Phe-Pro-Gly-Pro) to plasma membranes of basal nuclei of the rat forebrain and the dynamics of its degradation during its incubation with these membranes were studied.
  3. 03LabIn vitro (cell-free)Activity measurement

    In plasma membranes of rat forebrain basal nuclei, the dissociation constant of the semax ligand-receptor complex was 2.41 +/- 1.02 x 10(-9) M.

    In plain wordsIn lab tests on rat brain membranes, semax bound with a measured binding strength (Kd) in the nanomolar range.

    Peptide
    Semax
    Outcome
    Not applicableDissociation constant (Kd)
    Study

    ratn: not reported in source

    Plasma membranes of rat forebrain basal nuclei
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Measurements

    Kd
    2.41 x 10(-9) M
    rat forebrain basal nuclei plasma membranes

    Source sentences

    Summary
    characterized by the dissociation constant of the ligand-receptor complex Kd = 2.41 +/- 1.02 x 10(-9) M
    1 context sentence
    Summary · context
    The binding characteristics of the peptide Semax (Met-Glu-His-Phe-Pro-Gly-Pro) to plasma membranes of basal nuclei of the rat forebrain and the dynamics of its degradation during its incubation with these membranes were studied.
  4. 04LabIn vitro (cell-free)Activity measurement

    In plasma membranes of rat forebrain basal nuclei, the concentration of semax binding sites was 33.5 +/- 7.9 x 10(-15) mol/mg of protein.

    In plain wordsIn lab tests on rat brain membranes, a measured number of semax binding sites was found per mg of protein.

    Peptide
    Semax
    Outcome
    Not applicableConcentration of binding sites (Bmax)
    Study

    ratn: not reported in source

    Plasma membranes of rat forebrain basal nuclei
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Measurements

    Bmax
    33.5 x 10(-15) mol/mg protein
    rat forebrain basal nuclei plasma membranes

    Source sentences

    Summary
    by the concentration of binding sites Bmax = 33.5 +/- 7.9 x 10(-15) mol/mg of protein.
    1 context sentence
    Summary · context
    The binding characteristics of the peptide Semax (Met-Glu-His-Phe-Pro-Gly-Pro) to plasma membranes of basal nuclei of the rat forebrain and the dynamics of its degradation during its incubation with these membranes were studied.
  5. 05LabIn vitro (cell-free)Pharmacokinetics

    In the presence of rat brain plasma membranes, the half-life of semax was longer than 1 h.

    In plain wordsIn lab tests with rat brain membranes, semax broke down slowly, with a half-life of more than 1 hour.

    Peptide
    Semax
    Outcome
    Not applicableHalf-life with plasma membranes
    Study

    ratn: not reported in source

    Plasma membranes of rat forebrain basal nuclei
    Outcome group
    Pharmacokinetics · Pharmacology
    Studied dose
    Dose not stated

    Measurements

    half-life
    > 1 h
    rat brain plasma membranes

    Source sentences

    Summary
    The half-life of Semax in the presence of the plasma membranes was demonstrated to be longer than 1 h.
    1 context sentence
    Summary · context
    The binding characteristics of the peptide Semax (Met-Glu-His-Phe-Pro-Gly-Pro) to plasma membranes of basal nuclei of the rat forebrain and the dynamics of its degradation during its incubation with these membranes were studied.
  6. 06LabIn vitro (cell-free)Mechanism

    Dipeptidylaminopeptidases are considered the main enzymes that cleave semax in rat brain membranes, first to the HFPGP pentapeptide and then to the PGP tripeptide.

    In plain wordsIn lab tests with rat brain membranes, enzymes are thought to cut semax stepwise into smaller pieces.

    Peptide
    Semax
    Outcome
    Not applicableBiodegradation pathway
    Study

    ratn: not reported in source

    Plasma membranes of rat forebrain basal nuclei
    Outcome group
    Pharmacokinetics · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Dipeptidylaminopeptidases are considered to be the main enzymes responsible for its biodegradation; they successively cleave Semax to the HFPGP pentapeptide and the PGP tripeptide.
    1 context sentence
    Summary · context
    The binding characteristics of the peptide Semax (Met-Glu-His-Phe-Pro-Gly-Pro) to plasma membranes of basal nuclei of the rat forebrain and the dynamics of its degradation during its incubation with these membranes were studied.

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

    12 Oct 2026, 17:28 UTC

    Study results updated

  2. Version 1

    9 Oct 2026, 03:04 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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