GHK-CU Serum Research Standard
GHK-CU Serum is a co-formulated topical-grade research solution supplying copper tripeptide-1 (GHK-Cu) at 20 mg/mL and nicotinamide adenine dinucleotide (NAD+) at 7.5 mg/mL in an aqueous sodium hyaluronate and glycerin base, in a 30 mL bottle. It is supplied for in vitro and ex vivo laboratory work on extracellular matrix biology, copper coordination chemistry and cellular bioenergetics. The two actives are well characterised individually in the literature; they are supplied together here as a single research matrix, not because a combined effect has been demonstrated.
Mechanism of Action & Research Context
The formulation brings together two independent and separately documented biochemical systems.
GHK-Cu is a defined copper coordination complex. Glycyl-L-histidyl-L-lysine is an endogenous Cu(II)-binding tripeptide present in human plasma. It forms characterised Cu(II) complexes, and ternary complexes with other physiological ligands such as urocanic acid, established by potentiometry, circular dichroism and EPR.[3]
Bound copper is redox-attenuated. Cu(II) held by GHK shows reduced redox activity compared with free copper, and in a CNS cell model this prevented copper- and zinc-driven protein aggregation and cell death. The relevant chemistry is sequestration and redox silencing, not general radical scavenging.[4]
Collagen synthesis in fibroblast culture. GHK-Cu raises collagen synthesis in cultured fibroblasts, with the effect emerging between 10−12 and 10−11 M and peaking around 10−9 M, independent of cell number.[1]
Matrix remodelling runs in both directions. GHK-Cu increases MMP-2 protein and mRNA in dermal fibroblast conditioned media, and raises TIMP-1 and TIMP-2 secretion alongside it. The net effect is bidirectional matrix turnover rather than one-way collagen accumulation. Copper ions alone reproduced the MMP-2 effect while GHK alone did not, so activity in this assay cannot be attributed to the peptide moiety by itself.[2]
NAD+ is both a redox coenzyme and a consumed substrate. NAD+ carries the redox chemistry of dehydrogenase-driven catabolism and is separately consumed stoichiometrically by sirtuins, PARPs and CD38.[5] Its availability couples cellular energy status to mitochondrial function and is rate-limiting for sirtuin activity.[6] Removing PARP-1, a major NAD+-consuming enzyme, raises tissue NAD+ and SIRT1 activity — the direct demonstration that the pool is drawn down, not merely recycled.[7]
What is not established. No study cited here tests GHK-Cu and NAD+ in combination, so no synergy between them should be assumed. None of these references examined dermal penetration of either active; NAD+ in particular is a large, charged, phosphorylated dinucleotide, and its permeation is not something this literature supports. The stability of the two actives co-formulated in an aqueous base is likewise untested here: NAD+ hydrolyses in aqueous solution and Cu(II) is a plausible catalyst for that. Treat delivery and co-formulation stability as open experimental questions, which is part of what makes the matrix useful to work on.
Research Applications
Primary fields of in vitro and ex vivo laboratory investigation include:
Dermal fibroblast assays. Collagen and glycosaminoglycan synthesis, and dose-response characterisation across the picomolar-to-nanomolar range.[1]
Matrix metalloproteinase profiling. MMP-2 and TIMP-1/TIMP-2 quantification in conditioned media, with copper-only and peptide-only arms to separate the contributions.[2]
Copper speciation and coordination chemistry. Potentiometric, CD and EPR characterisation of binary and ternary Cu(II) complexes.[3,4]
Bioenergetic profiling. Sirtuin and PARP activity, NAD+/NADH ratio measurement, and mitochondrial function readouts in cultured cells.[5,6,7]
Permeability and formulation studies. Ex vivo skin tissue work mapping penetration and stability of peptide-cofactor co-formulations — an open question rather than a settled one.
Analytical Documentation
Purity, identity and composition vary by manufacturing lot. Kimera Chems does not publish a single fixed purity figure for this item; refer to the batch-specific Certificate of Analysis (COA) issued for the lot received, which reflects third-party analytical testing for that lot.
References
- Maquart FX, Pickart L, Laurent M, et al. Stimulation of collagen synthesis in fibroblast cultures by the tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+. FEBS Lett. 1988;238(2):343–346. doi:10.1016/0014-5793(88)80509-x
- Siméon A, Emonard H, Hornebeck W, Maquart FX. The tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+ stimulates matrix metalloproteinase-2 expression by fibroblast cultures. Life Sci. 2000;67(18):2257–2265. doi:10.1016/s0024-3205(00)00803-1
- Bossak-Ahmad K, Wiśniewska MD, Bal W, Drew SC, Frączyk T. Ternary Cu(II) complex with GHK peptide and urocanic acid as a potential physiologically functional copper chelate. Int J Mol Sci. 2020;21(17):6190. doi:10.3390/ijms21176190
- Min JH, Sarlus H, Harris RA. Glycyl-L-histidyl-L-lysine prevents copper- and zinc-induced protein aggregation and central nervous system cell death in vitro. Metallomics. 2024;16(5):mfae019. doi:10.1093/mtomcs/mfae019
- Covarrubias AJ, Perrone R, Grozio A, Verdin E. NAD+ metabolism and its roles in cellular processes during ageing. Nat Rev Mol Cell Biol. 2021;22(2):119–141. doi:10.1038/s41580-020-00313-x
- Cantó C, Menzies KJ, Auwerx J. NAD+ metabolism and the control of energy homeostasis: a balancing act between mitochondria and the nucleus. Cell Metab. 2015;22(1):31–53. doi:10.1016/j.cmet.2015.05.023
- Bai P, Cantó C, Oudart H, et al. PARP-1 inhibition increases mitochondrial metabolism through SIRT1 activation. Cell Metab. 2011;13(4):461–468. doi:10.1016/j.cmet.2011.03.004
Storage & Handling
Store at controlled room temperature. Keep tightly closed.
Storage guidance is a house recommendation. Analytical documentation is per-lot release testing.
