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Study · Animal study (in vivo) · rat · 2005

6 results

Interactions of GRF(1-29)NH2 with plasma proteins and their effects on the release of the peptide from a PLAGA matrix.

Mariette B, Coudane J, Vert M

Journal of controlled release : official journal of the Controlled Release Society1 Sept 2005

PMID15987661 (opens in a new tab)DOI10.1016/j.jconrel.2005.05.008 (opens in a new tab)PepBankPUB-15987661
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 study6

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

  1. 01AnimalAnimal study (in vivo)Pharmacokinetics

    In rats with subcutaneously implanted bioresorbable pellets holding a large quantity of GRF(1-29)NH2, the peptide was slowly released despite complexation with plasma proteins.

    In plain wordsIn rats, the peptide was released slowly from implanted pellets, even though it bound to blood proteins.

    Peptide
    Sermorelin
    Outcome
    Not applicableRelease of GRF(1-29)NH2 from bioresorbable pellets
    Study

    Ratn: not reported in source

    Subcutaneous implantation of bioresorbable PLAGA pellets
    Outcome group
    Pharmacokinetics · Pharmacology
    Studied dose
    Dose not stated · subcutaneous implantationAs given in this study (Rat).

    Source sentences

    Summary
    When a rather large quantity of GRF(1-29)NH2 was entrapped in bioresorbable pellets working at a percolating regime after subcutaneous implantation in rats, the peptide was slowly released despite the complexation with plasma proteins.
  2. 02AnimalAnimal study (in vivo)Pharmacokinetics

    In rats with implanted pellets, only a very small part of GRF(1-29)NH2 was found in blood.

    In plain wordsIn rats, only a very small part of the implanted peptide reached the blood.

    Peptide
    Sermorelin
    Outcome
    Not applicablePeptide level in blood after pellet implantation
    Study

    Ratn: not reported in source

    Subcutaneous implantation of bioresorbable PLAGA pellets
    Outcome group
    Pharmacokinetics · Pharmacology
    Studied dose
    Dose not stated · subcutaneous implantationAs given in this study (Rat).

    Source sentences

    Summary
    However only a very small part of the peptide was found in blood, this small part being still large enough to cause a detectable increase of the circulating growth hormone concentration.
  3. 03AnimalAnimal study (in vivo)Activity measurement

    In rats with implanted pellets, the small amount of GRF(1-29)NH2 in blood was enough to cause a detectable increase in circulating growth hormone.

    In plain wordsIn rats, the small amount of peptide that reached the blood still raised growth hormone levels.

    Peptide
    Sermorelin
    Outcome
    IncreaseCirculating growth hormone concentration
    Study

    Ratn: not reported in source

    Subcutaneous implantation of bioresorbable PLAGA pellets
    Outcome group
    Growth hormone and IGF-1 · Endocrine and hormones
    Studied dose
    Dose not stated · subcutaneous implantationAs given in this study (Rat).

    Source sentences

    Summary
    However only a very small part of the peptide was found in blood, this small part being still large enough to cause a detectable increase of the circulating growth hormone concentration.

Studies that did not test the peptide alone3

In this study, Sermorelin 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 Sermorelin.

  1. 04LabNot a test of Sermorelin aloneIn vitro (cell-free)Other

    In protein-free salted media, precipitation of GRF(1-29)NH2 is due to a salting out phenomenon, complemented by neutralization of solubilizing electrostatic charges in isotonic buffer.

    In plain wordsIn lab tests, the peptide fell out of salty solutions because of salting out and loss of electric charge, not because of proteins.

    Peptide
    Sermorelin
    Outcome
    Not applicableCause of GRF(1-29)NH2 precipitation in protein-free salted media
    Study

    n: not reported in source

    Protein-free salt solution and isotonic phosphate buffer (pH 7.4)
    Outcome group
    Formulation, delivery and stability · Pharmacology

    Source sentences

    Summary
    It is shown that precipitation in protein-free salted media is due to a salting out phenomenon complemented by the neutralization of the solubilizing electrostatic charges in the isotonic buffer.

    In this study, Sermorelin 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 Sermorelin.

  2. 05LabNot a test of Sermorelin aloneIn vitro (cell-free)Other

    In plasma, precipitation of GRF(1-29)NH2 is due to polyelectrolyte-type complexation with polyanionic proteins of low isoelectric point, such as albumin, transferin, haptoglobulin and IgG immunoglobulins.

    In plain wordsIn lab tests, the peptide fell out of plasma because it bound to proteins such as albumin and immunoglobulins.

    Peptide
    Sermorelin
    Outcome
    Not applicableCause of GRF(1-29)NH2 precipitation in plasma
    Study

    n: not reported in source

    Plasma
    Outcome group
    Formulation, delivery and stability · Pharmacology

    Source sentences

    Summary
    In contrast, the precipitation in plasma is due to inter polyelectrolyte-type complexation that involved polyanionic proteins having a rather low isoelectric point like albumin, transferin, haptoglobulin and IgG immunoglobulins.

    In this study, Sermorelin 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 Sermorelin.

  3. 06LabNot a test of Sermorelin aloneIn vitro (cell-free)Other

    Combining GRF(1-29)NH2 with arginine increased the solubility of the peptide in plasma.

    In plain wordsIn lab tests, adding the amino acid arginine made the peptide dissolve better in plasma.

    Peptide
    Sermorelin
    Outcome
    IncreaseSolubility of GRF(1-29)NH2 in plasma with arginine
    Study

    n: not reported in source

    Plasma
    Outcome group
    Formulation, delivery and stability · Pharmacology

    Source sentences

    Summary
    Attempts made to increase the solubility of the peptide in plasma were successful when the peptide was combined with arginine, an amino acid known to promote the poor hormonal activity of injected GRF(1-29)NH2 solutions under clinical conditions.

    In this study, Sermorelin 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 Sermorelin.

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

    9 Oct 2026, 19:08 UTC

    Study results updated

  2. Version 1

    9 Oct 2026, 03:13 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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