Binding of the growth factor glycyl-L-histidyl-L-lysine by heparin.

Rabenstein DL, Robert JM, Hari S

FEBS letters1 Dec 1995Cited by 4 (Europe PMC)

PMID7498545DOI10.1016/0014-5793(95)01286-5PepBankPUB-07498545

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 study7

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

Studies that did not test the peptide alone7

In this study, GHK (glycyl-L-histidyl-L-lysine) 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 GHK (glycyl-L-histidyl-L-lysine).

01LabNot a test of GHK (glycyl-L-histidyl-L-lysine) aloneIn vitro (cell-free)Mechanism
In NMR experiments, GHK bound to heparin.
In plain wordsIn lab tests, GHK bound to heparin.
Peptide
GHK (glycyl-L-histidyl-L-lysine)
Outcome
Not applicableHeparin binding
Study
n: not reported in source
GHK-heparin NMR binding experiments
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
Evidence is presented that the growth factor glycyl-histidyl-lysine (GHK) binds to heparin, and the interaction has been characterized by [1H]NMR spectroscopy.
In this study, GHK (glycyl-L-histidyl-L-lysine) 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 GHK (glycyl-L-histidyl-L-lysine).
Report a problemFND-0749854501
02LabNot a test of GHK (glycyl-L-histidyl-L-lysine) aloneIn vitro (cell-free)Mechanism
In NMR experiments, GHK interacted with both carboxylic acid and carboxylate forms of heparin.
In plain wordsIn lab tests, GHK interacted with both acid and carboxylate forms of heparin.
Peptide
GHK (glycyl-L-histidyl-L-lysine)
Outcome
Not applicableHeparin acid and carboxylate interaction
Study
n: not reported in source
GHK-heparin NMR binding experiments
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
1H chemical shifts indicate that GHK interacts with both the carboxylic acid and the carboxylate forms of heparin.
In this study, GHK (glycyl-L-histidyl-L-lysine) 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 GHK (glycyl-L-histidyl-L-lysine).
Report a problemFND-0749854502
03LabNot a test of GHK (glycyl-L-histidyl-L-lysine) aloneIn vitro (cell-free)Mechanism
In NMR experiments, chemical shifts supported weak delocalized binding of triprotonated GHK by the carboxylic acid form of heparin.
In plain wordsIn lab tests, chemical shifts supported weak binding of triprotonated GHK to the acid form of heparin.
Peptide
GHK (glycyl-L-histidyl-L-lysine)
Outcome
Not applicableTriprotonated GHK binding
Study
n: not reported in source
GHK-heparin NMR binding experiments
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
The chemical shift data are consistent with a weak delocalized binding of the triprotonated (ImH+, GlyNH3+, LysNH3+) form of GHK by the carboxylic acid form of heparin.
In this study, GHK (glycyl-L-histidyl-L-lysine) 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 GHK (glycyl-L-histidyl-L-lysine).
Report a problemFND-0749854503
04LabNot a test of GHK (glycyl-L-histidyl-L-lysine) aloneIn vitro (cell-free)Mechanism
In NMR experiments at increased pD, GHK ammonium groups hydrogen bonded to heparin carboxylate groups.
In plain wordsIn lab tests at increased pD, GHK ammonium groups hydrogen bonded to heparin carboxylate groups.
Peptide
GHK (glycyl-L-histidyl-L-lysine)
Outcome
Not applicableAmmonium hydrogen bonding
Study
n: not reported in source
GHK-heparin NMR binding experiments
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
As the pD is increased and the carboxylic acid groups are titrated, chemical shift data indicate that ammonium groups of GHK are hydrogen bonded to heparin carboxylate groups, while the histidyl imidazolium ring occupies the imidazolium-binding site of heparin.
In this study, GHK (glycyl-L-histidyl-L-lysine) 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 GHK (glycyl-L-histidyl-L-lysine).
Report a problemFND-0749854504
05LabNot a test of GHK (glycyl-L-histidyl-L-lysine) aloneIn vitro (cell-free)Mechanism
In NMR experiments at increased pD, chemical shifts indicated that the GHK histidyl imidazolium ring occupied the heparin imidazolium-binding site.
In plain wordsIn lab tests at increased pD, chemical shifts indicated that the GHK histidyl ring occupied a specific heparin binding site.
Peptide
GHK (glycyl-L-histidyl-L-lysine)
Outcome
Not applicableImidazolium binding site occupancy
Study
n: not reported in source
GHK-heparin NMR binding experiments
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
As the pD is increased and the carboxylic acid groups are titrated, chemical shift data indicate that ammonium groups of GHK are hydrogen bonded to heparin carboxylate groups, while the histidyl imidazolium ring occupies the imidazolium-binding site of heparin.
In this study, GHK (glycyl-L-histidyl-L-lysine) 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 GHK (glycyl-L-histidyl-L-lysine).
Report a problemFND-0749854505
06LabNot a test of GHK (glycyl-L-histidyl-L-lysine) aloneIn vitro (cell-free)Mechanism
In NMR experiments, titration shifts and proton shielding supported site-specific GHK-heparin binding.
In plain wordsIn lab tests, titration shifts and proton shielding supported site-specific GHK-heparin binding.
Peptide
GHK (glycyl-L-histidyl-L-lysine)
Outcome
Not applicableSite-specific binding evidence
Study
n: not reported in source
GHK-heparin NMR binding experiments
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
Evidence for site-specific binding includes displacement of chemical shift titration curves for heparin to lower pD, increased shielding of specific heparin protons by the imidazolium ring current and displacement of chemical shift titration curves for GHK to higher pD.
In this study, GHK (glycyl-L-histidyl-L-lysine) 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 GHK (glycyl-L-histidyl-L-lysine).
Report a problemFND-0749854506
07LabNot a test of GHK (glycyl-L-histidyl-L-lysine) aloneIn vitro (cell-free)Mechanism
In NMR experiments, specific GHK-heparin binding constants were determined, but the abstract did not report their values.
In plain wordsIn lab tests, GHK-heparin binding constants were determined, but their values were not reported.
Peptide
GHK (glycyl-L-histidyl-L-lysine)
Outcome
Direction not reportedSpecific binding constants
Study
n: not reported in source
GHK-heparin NMR binding experiments
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
Specific binding constants were determined for binding of the (ImH+, GlyNH3+), LysNH3+) forms of GHK by the carboxylate form of heparin from chemical shift vs. pD titration data.
In this study, GHK (glycyl-L-histidyl-L-lysine) 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 GHK (glycyl-L-histidyl-L-lysine).
Report a problemFND-0749854507

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
14 Oct 2026, 05:02 UTC
Study results updated
Version 1
14 Oct 2026, 01:46 UTC
First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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MeSH terms

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