Enzymatic semisynthesis of a superpotent analog of human growth hormone-releasing factor.

Bongers J, Lambros T, Liu W, Ahmad M, Campbell RM, Felix AM, Heimer EP

Journal of medicinal chemistry1 Oct 1992Cited by 7 (Europe PMC)

PMID1433202DOI10.1021/jm00099a022PepBankPUB-01433202

Publisher page PubMedAsk about this study

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 study3

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

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.

01LabNot a test of Sermorelin aloneIn vitro (cell-free)Other
With the alpha-ethyl ester of the acyl component, conversion of segment 2 to the analog was limited to about 60% by competing proteolysis at Asp25-Ile26.
In plain wordsIn lab chemistry, with one ester, about 60% of the peptide piece became product because the peptide was cut at an unwanted site.
Peptide
Sermorelin
Outcome
Not applicableConversion with the alpha-ethyl ester
Study
n: not reported in source
enzymatic semisynthesis
Outcome group
Synthesis and manufacturing · Pharmacology
Measurements
Conversion
≈ 60%
alpha-ethyl ester 3a
Source sentences
Summary
Conversion of 2 to 4 in couplings employing the alpha-ethyl ester of the acyl component 3a was limited to about 60% by competing proteolysis at Asp25-Ile26.
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-0143320201
02LabNot a test of Sermorelin aloneIn vitro (cell-free)Other
The 4-nitrobenzyl ester gave 90% conversion of segment 2 to the analog with no detectable loss to proteolysis.
In plain wordsIn lab chemistry, a different ester gave 90% conversion with no detectable unwanted cutting.
Peptide
Sermorelin
Outcome
Not applicableConversion with the 4-nitrobenzyl ester
Study
n: not reported in source
enzymatic semisynthesis
Outcome group
Synthesis and manufacturing · Pharmacology
Measurements
Conversion
90%
4-nitrobenzyl ester 3b
Source sentences
Summary
The 4-nitrobenzyl ester 3b proved to be a superior substrate, resulting in 90% conversion of 2 to 4 with no detectable loss to proteolysis
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-0143320202
03LabNot a test of Sermorelin aloneIn vitro (cell-free)Other
The 4-nitrobenzyl ester required significantly lesser amounts of catalyst.
In plain wordsIn lab chemistry, the second ester needed much less enzyme.
Peptide
Sermorelin
Outcome
Not applicableCatalyst amount with the 4-nitrobenzyl ester
Study
n: not reported in source
enzymatic semisynthesis
Outcome group
Synthesis and manufacturing · Pharmacology
Source sentences
Summary
requiring significantly lesser amounts of catalyst.
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-0143320203

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

Subjects

Terms as the source lists them.

Publication types

Journal Article

MeSH terms

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