Affinity of human growth hormone-releasing factor (1-29)NH2 analogues for GRF binding sites in rat adenopituitary.

Gaudreau P, Boulanger L, Abribat T

Journal of medicinal chemistry1 May 1992Cited by 14 (Europe PMC)

PMID1534126DOI10.1021/jm00088a023PepBankPUB-01534126

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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

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

Studies that did not test the peptide alone6

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.

01LabNot a test of Sermorelin aloneIn vitro (cell-free)Activity measurement
Acylation of the N-terminus of hGRF(1-29)NH2 generally decreased its binding affinity to rat adenopituitary GRF binding sites.
In plain wordsIn lab tests, adding an acyl group to the start of the GRF peptide generally lowered its binding to the GRF receptor.
Peptide
Sermorelin
Outcome
DecreaseAffinity of N-terminal acylated analogues
Study
ratn: not reported in source
GRF binding assay, rat adenopituitary
Comparator
hGRF(1-29)NH2
Outcome group
Receptor activity and mechanism · Endocrine and hormones
Measurements
Relative affinity
26 to 85%
N-terminal acylated analogues
Source sentences
Summary
Acylation of the N-terminus of hGRF(1-29)NH2 generally decreased its affinity (relative affinity to hGRF(1-29)NH2 (RA), 26-85%).
1 context sentence(design, population, supporting numbers)
Summary · context
Since we have recently developed a sensitive GRF binding assay with [125I-Tyr10]hGRF(1-44)NH2, this method was applied to structure-affinity studies as a first step of screening GRF analogues.
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.
Report a problemFND-0153412601
02LabNot a test of Sermorelin aloneIn vitro (cell-free)Activity measurement
Replacing the C-terminal carboxamide by a free carboxylic function decreased affinity.
In plain wordsIn lab tests, changing the end of the GRF peptide to a free acid lowered its binding.
Peptide
Sermorelin
Outcome
DecreaseAffinity of C-terminal free acid analogue
Study
ratn: not reported in source
GRF binding assay, rat adenopituitary
Comparator
hGRF(1-29)NH2
Outcome group
Receptor activity and mechanism · Endocrine and hormones
Measurements
Relative affinity
57%
free carboxylic C-terminus
Source sentences
Summary
Replacement of the C-terminal carboxamide by a free carboxylic function decreased affinity likely by diminishing its proteolytic stability (RA, 57%).
1 context sentence(design, population, supporting numbers)
Summary · context
Since we have recently developed a sensitive GRF binding assay with [125I-Tyr10]hGRF(1-44)NH2, this method was applied to structure-affinity studies as a first step of screening GRF analogues.
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.
Report a problemFND-0153412602
03LabNot a test of Sermorelin aloneIn vitro (cell-free)Activity measurement
Removal of Tyr1, Ser9, Lys12, Val13, Gly15, Gln16 or Lys21 drastically decreased affinity.
In plain wordsIn lab tests, removing any of seven single amino acids from the GRF peptide sharply lowered its binding.
Peptide
Sermorelin
Outcome
DecreaseAffinity after removal of Tyr1, Ser9, Lys12, Val13, Gly15, Gln16 or Lys21
Study
ratn: not reported in source
GRF binding assay, rat adenopituitary
Comparator
hGRF(1-29)NH2
Outcome group
Receptor activity and mechanism · Endocrine and hormones
Measurements
Relative affinity
< 3%
single residue deletions
Source sentences
Summary
Removal of Tyr1, Ser9, Lys12, Val13, Gly15, Gln16, or Lys21 drastically decreased its affinity (RA, less than 3%).
1 context sentence(design, population, supporting numbers)
Summary · context
Since we have recently developed a sensitive GRF binding assay with [125I-Tyr10]hGRF(1-44)NH2, this method was applied to structure-affinity studies as a first step of screening GRF analogues.
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.
Report a problemFND-0153412603
04LabNot a test of Sermorelin aloneIn vitro (cell-free)Activity measurement
Multiple deletions in segment 13-21, or replacing segment 13-15, 16-18 or 19-21 by an octanoyl moiety, led to a loss of affinity.
In plain wordsIn lab tests, removing or replacing several amino acids in the middle of the GRF peptide cost almost all binding.
Peptide
Sermorelin
Outcome
DecreaseAffinity after multiple deletions in segment 13-21
Study
ratn: not reported in source
GRF binding assay, rat adenopituitary
Comparator
hGRF(1-29)NH2
Outcome group
Receptor activity and mechanism · Endocrine and hormones
Measurements
Relative affinity
< 1%
segment 13-21 changes
Source sentences
Summary
Multiple amino acid deletions in the segment 13-21 of hGRF(1-29)NH2 also led to a loss of affinity as did replacing segment 13-15, 16-18, or 19-21 by an octanoyl moiety (RA, less than 1%).
1 context sentence(design, population, supporting numbers)
Summary · context
Since we have recently developed a sensitive GRF binding assay with [125I-Tyr10]hGRF(1-44)NH2, this method was applied to structure-affinity studies as a first step of screening GRF analogues.
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.
Report a problemFND-0153412604
05LabNot a test of Sermorelin aloneIn vitro (cell-free)Activity measurement
Removal of Asn8, Gln24, Asp25, Ile26, Met27, and Ser28 or Arg29 had less effect on GRF receptor affinity.
In plain wordsIn lab tests, removing amino acids near the ends of the GRF peptide lowered its binding less.
Peptide
Sermorelin
Outcome
DecreaseAffinity after removal of Asn8, Gln24, Asp25, Ile26, Met27, Ser28 or Arg29
Study
ratn: not reported in source
GRF binding assay, rat adenopituitary
Comparator
hGRF(1-29)NH2
Outcome group
Receptor activity and mechanism · Endocrine and hormones
Measurements
Relative affinity
5 to 33%
terminal residue deletions
Source sentences
Summary
Removal of Asn8, Gln24, Asp25, Ile26, Met27, and Ser28 or Arg29 had less effect on GRF receptor affinity (RA, 5-33%).
1 context sentence(design, population, supporting numbers)
Summary · context
Since we have recently developed a sensitive GRF binding assay with [125I-Tyr10]hGRF(1-44)NH2, this method was applied to structure-affinity studies as a first step of screening GRF analogues.
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.
Report a problemFND-0153412605
06LabNot a test of Sermorelin aloneIn vitro (cell-free)Activity measurement
Removal of Met27 or Ser28 only slightly affected hGRF(1-29)NH2 affinity.
In plain wordsIn lab tests, removing Met27 or Ser28 changed binding of the GRF peptide only slightly.
Peptide
Sermorelin
Outcome
DecreaseAffinity after removal of Met27 or Ser28
Study
ratn: not reported in source
GRF binding assay, rat adenopituitary
Comparator
hGRF(1-29)NH2
Outcome group
Receptor activity and mechanism · Endocrine and hormones
Measurements
Relative affinity
62 to 78%
Met27 or Ser28 removal
Source sentences
Summary
Removal of Met27 or Ser28 only slightly affected hGRF(1-29)NH2 affinity (RA, 62-78%).
1 context sentence(design, population, supporting numbers)
Summary · context
Since we have recently developed a sensitive GRF binding assay with [125I-Tyr10]hGRF(1-44)NH2, this method was applied to structure-affinity studies as a first step of screening GRF analogues.
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.
Report a problemFND-0153412606

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.

Version 2Current
10 Oct 2026, 10:21 UTC
Study results updated
Version 1
9 Oct 2026, 03:13 UTC
First added · source update from Europe PMC

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