lyophilised powder raises a handful of sensible questions. This page answers them in order, starting with the fundamentals and moving to applications.
This page was last updated on 2026-08-01 and is reviewed periodically as new material appears.
The sequence now called GHK was first reported in the early 1970s after isolation from human plasma, where it was noted to influence liver cell behavior in laboratory preparations. Later work described a copper-binding form and its activity in fibroblast and wound-model experiments. Review articles frequently group the substance with other copper peptides. Concentrations in blood appear to fall with age in several small surveys, although the reason for this trend is not settled. Whether such a decline carries functional consequences remains an open question.
Published work on GHK-Cu concentrates largely on cell culture systems rather than whole organisms. Frequently used endpoints include collagen synthesis, expression of matrix metalloproteinases, and migration of fibroblasts. Some reports describe antioxidant behavior, while others stress delivery of copper into cells. These mechanisms are proposed rather than demonstrated, and the relative weight of each pathway is unclear. Human trials are few and generally small, so laboratory findings should not be read as confirmed clinical results.
GHK-Cu is a coordination complex formed between the tripeptide glycyl-L-histidyl-L-lysine and a copper(II) ion. The peptide backbone consists of glycine, histidine, and lysine joined in that order. Copper is held through the imidazole nitrogen of histidine and the alpha-amino group at the N-terminus, which together produce a square-planar arrangement around the metal center. The solid appears blue to violet, a color that originates from d-d electronic transitions within the copper coordination sphere. The complex is indexed under CAS number 89030-95-5.
Solutions of GHK-Cu respond strongly to pH, redox conditions, and the presence of competing chelators such as EDTA. Below roughly pH 4 the copper tends to dissociate, because the amide nitrogen donors become protonated and can no longer coordinate. Strongly alkaline conditions instead favour hydrolysis and precipitation of copper hydroxide. Dissolved oxygen and light accelerate breakdown of the peptide backbone, and the copper released during that process can catalyse further oxidation, so dry, cold, dark storage is the usual recommendation.
Routine characterisation relies on reversed-phase high-performance liquid chromatography for peptide purity, paired with mass spectrometry for identity confirmation. Ultraviolet-visible spectroscopy detects the metal centre through its absorption band in the visible region, and inductively coupled plasma mass spectrometry quantifies total copper so that a metal-to-peptide ratio can be calculated. Amino acid analysis confirms the expected residue composition. Together these techniques establish concentration, identity, and stoichiometry, but none of them directly reports biological activity.
| Property | Value | Notes |
|---|---|---|
| Chemical class | Copper(II) peptide complex | Peptide chain coordinated to a single metal ion |
| CAS number | 89030-95-5 | Indexed for the peptide-copper complex |
| Molecular formula | C14H22CuN6O4 | Approximate formula for a one-to-one complex |
| Appearance | Blue to violet solid | Color from copper d-d transitions |
| Solubility class | Freely soluble in water | Also dispersible in some polar solvents |
Identity and purity are commonly assessed by reversed-phase high-performance liquid chromatography, frequently paired with mass spectrometry to confirm the molecular ion. Copper content is measured separately, typically by inductively coupled plasma mass spectrometry or atomic absorption spectroscopy, because the chromatographic signal reports the peptide rather than the metal. Ultraviolet-visible spectroscopy provides a fast check on complex formation, since copper(II) peptide complexes absorb in the visible region. Elemental analysis and amino acid analysis are used less often but remain useful for reference standards. A gap between reported peptide purity and measured copper content is a recurring source of confusion.
Material described as GHK-Cu appears in several distinct markets, including cosmetic ingredients, laboratory reagents, and consumer products, and the quality expectations attached to each differ. A certificate of analysis generally reports peptide purity by chromatography, copper content, appearance, and residual solvents or counterions. Counterion identity matters, because the complex is usually supplied as an acetate or a similar salt, and the counterion contributes to the measured mass. Independent verification of sequence and metal stoichiometry is advisable when a material is used for quantitative work. Batch-to-batch variation is common and should be documented rather than assumed negligible.
Identity and purity are usually assessed with reversed-phase high-performance liquid chromatography, often paired with mass spectrometry. Copper content is measured separately by techniques such as inductively coupled plasma mass spectrometry or atomic absorption. Amino acid analysis confirms the peptide sequence after hydrolysis. Because the metal and the peptide can be quantified independently, a complete certificate of analysis normally reports both values rather than a single purity figure. This separation of measurements is important when comparing suppliers.
Solid GHK-Cu appears as a blue to blue-violet powder, and the colour is a direct consequence of copper coordination. The complex dissolves readily in water and in many polar solvents, while the free peptide behaves differently. Solubility in nonpolar media is low, which limits its use in oil-based systems. Solutions are typically prepared fresh because the dissolved form is more exposed to hydrolysis and to loss of the metal ion than the dry powder. Working concentrations are usually low, and preparation notes often specify the solvent and the order of addition.
Identity and purity are normally checked by reversed-phase high-performance liquid chromatography, often coupled to mass spectrometry. The peptide absorbs in the ultraviolet region, and the copper complex also shows a broad visible absorption band that can be followed spectroscopically. Copper content is measured separately, for example by inductively coupled plasma mass spectrometry or atomic absorption spectroscopy, because the peptide assay alone does not confirm how much metal is bound. Purity figures therefore need a stated basis: peptide peak area, copper content, or both.
Aqueous GHK-Cu solutions are less stable than the dry powder. Light, dissolved oxygen and elevated temperature all accelerate loss of the intact complex, and the main observable changes are fading of the blue colour and the appearance of peptide fragments. Acidic conditions protonate the histidine imidazole and weaken copper binding, while strongly alkaline conditions promote hydrolysis of the peptide backbone. Because several degradation routes operate at once, a single shelf-life figure does not describe all storage conditions.
Endogenous GHK occurs in blood plasma, saliva, and urine, and reported plasma concentrations decline with age in several studies. Researchers have proposed that the peptide acts as a copper carrier that delivers the metal to cells and to sites of injury. That transport role is a hypothesis supported by binding measurements and tissue-distribution data rather than a settled mechanism, and the peptide is generally described as a minor contributor to total plasma copper transport. Values reported in wound fluid and certain tissue extracts are higher than in circulating plasma.
The sequence carries three residues in the order glycine, histidine, lysine, which places a small, flexible chain around a single metal centre. Compared with larger copper-binding proteins, the complex is compact and its coordination chemistry can be reproduced with synthetic peptide in a laboratory. Published structural work agrees on the nitrogen donor set but differs in the exact geometry assigned under some conditions, so the arrangement is best treated as well characterised in outline rather than fixed in every detail.
GHK-Cu is a coordination complex formed between the tripeptide glycyl-L-histidyl-L-lysine and a copper(II) ion. The peptide was isolated from human plasma in the early 1970s by Loren Pickart, who observed that a plasma fraction from young donors stimulated growth in cultured liver cells. The copper-bound form is abbreviated GHK-Cu, while the metal-free peptide is written simply as GHK. In the research literature the complex also appears as copper tripeptide-1 and as glycyl-histidyl-lysine copper complex.
== Grundlagen == Durch eine supramaximale elektrische Stimulation eines peripheren Nervs (z. B. Nervus tibialis) kann, während einer maximalen, willkürlichen Kontraktion neben der direkten Muskelantwort (M-Welle), ein zweites Potential im OEMG beobachtet werden. Diese elektrophysiologische Variation der H-Welle wird als V-Welle bezeichnet. Ab einer bestimmten Stimulationsintensität kommt es zum Rückgang der H-Welle aufgrund der Kollision des afferenten Aktionspotentials mit dem antidromen Aktionspotential. Die Kollision findet aufgrund der unterschiedlichen Leitungsgeschwindigkeiten von Ia-afferenten Nervenfasern und efferenten Nervenfasern in den efferenten Nervenfasern statt. Unter maximaler, willkürlicher Kontraktion können natürliche efferente Aktionspotentiale mit den künstlich evozierten antidromen Aktionspotentialen kollidieren. Dadurch wird es dem peripher evozierten Signal ermöglicht über die monosynaptische Verschaltung im Rückenmark über das ɑ-Motoneuron zurück zum homonymen Muskel zu gelangen. Dieses Muskelaktionspotential entspricht dem der H-Welle, wird aber, da es unter maximaler Kontraktion hervorgerufen wurde, als V-Welle definiert. Mit steigender motoneuronaler Aktivität, wird das antidrome Aktionspotential zunehmend stärker unterdrückt. Dies führt zu einem Anstieg der peak-to-peak Amplitude der V-Welle. Aus dem Verhältnis von maximaler M-Welle und der V-Welle (V/M) könnten demnach Rückschlüsse auf das Ausmaß des efferenten, ɑ-motoneuronalen Outputs gezogen werden.
Vibrationstraining, auch Whole Body Vibration (WBV), Beschleunigungstraining, Schwingungstraining, Mechanostimulation oder stochastisches Resonanztraining genannt, ist eine Trainingsmethode, bei der die übende Person auf einer vibrierenden Platte steht, die in einem Frequenzbereich von etwa 5 bis 60 Hz vibriert. Dabei sollen Dehnreflexe der Muskulatur ausgelöst und Muskelkontraktionen hervorgerufen werden. Bei der verwandten Methoden der biomechanischen Stimulation (BMS) oder der biomechanischen Oszillation werden hingegen lokale Muskelgruppen direkt oder über die zugehörigen Sehnen mittels spezieller Vibrationsgeräte stimuliert. Vibrationstraining wird in einer Vielzahl von Bereichen (Leistungssport, Fitness, Rehabilitation, Medizin, Vorsorge, Beauty) angeboten und zur Leistungssteigerung der Muskulatur und zur Verbesserung von Koordination und Gleichgewicht eingesetzt.
Vibrierende Massagehilfsmittel wurden in der Medizin schon lange erprobt. 1869 setzte der US-Amerikaner George Taylor ein Gerät zur Vibrationstherapie von Arm und Rücken ein. Jean-Martin Charcot experimentierte um 1880 mit einem vibrierenden Stuhl zur Behandlung der Parkinson-Krankheit. Gustav Zander (Schweden) entwickelte über 70 verschiedene dampfbetriebene Geräte zur Mechano-Therapy. John Harvey Kellogg setzte in seinem Battle Creek Sanatorium vibrierende Stühle und vibrierende Manipulatoren für Arme und Beine ein. 1960 veröffentlichte der Ostdeutsche W. Biermann den Effekt von sogenannten „zyklischen Oszillationen“ auf den menschlichen Körper. Um 1970 versuchte Wladimir Nasarow, Mitglied des sowjetischen Turnerteams, die Übertragung der Biermannschen Idee in praktikable Trainingsmethoden für welche sich seither die Begriffe biomechanische Stimulation (BMS), biomechanische Oszillation etabliert haben. In den 1960er bis 1980er Jahren waren in Österreich in vielen Bahnhöfen und Geschäftspassagen „Fußmassage“-Automaten aufgestellt. Eine Person konnte sich auf die Rüttelplatte stellen und durch Münzeinwurf von typisch 1 Schilling die Vibrationsbewegung in Gang setzen. Mit dem etwa 1,5 m hohen abgerundet quaderförmigen Korpus aus robustem Aluguss war ein solcher Automat meist an einer Wand aufgestellt. Eine Leuchtfläche bewarb die Erfrischung müder Beine im Umfeld stehend wartender Menschen.
Seit 1996 werden Geräte im freien Handel angeboten, auf denen der Trainierende stehen kann und die somit ein ganzheitliches Training sowohl der Extremitäten als auch der Rumpfmuskulatur ermöglichen. Für das Training mit dieser Gerätegruppe haben sich die Begriffe Whole Body Vibration (WBV), Vibrationstraining, Beschleunigungstraining und stochastisches Resonanztraining etabliert. Der Begriff Whole Body Vibration (WBV) ist jedoch mehrfach belegt, da er ursprünglich im Bereich der Arbeitssicherheit die Effekte von auf einen Körper wirkenden Vibrationen beispielsweise von Fahrzeugen oder Baumaschinen umfasst. Im Zusammenhang mit Training wurde der begriff erstmals in einer Publikation von 1998 erwähnt, die der Trainingsmethode ihren Namen gab.
Sources: de.wikipedia.org
It is the copper complex of the tripeptide glycyl-L-histidyl-lysine. The metal ion is held by the histidine imidazole group and the peptide N-terminus. Most research on it concerns skin and wound models.
The tripeptide was first isolated from human plasma and has also been reported in saliva and urine. Plasma levels appear to decline with age in some small studies. Those observations rest on limited sample sizes.
It is not authorized as a systemic medicine in most countries. Cosmetic preparations list it as an ingredient rather than an active pharmaceutical substance. Legal status therefore differs by jurisdiction.
Inductively coupled plasma mass spectrometry or atomic absorption spectroscopy gives total copper after acid digestion. Combining that value with a peptide concentration from chromatography or amino acid analysis yields the metal-to-peptide ratio.