Palmitoyl AHK appears to be a palmitoylated derivative of a short tripeptide, AHK, which is composed of alanine, histidine, and lysine.(1) Preliminary data collected in laboratory settings findings suggest that AHK may be involved in several cellular processes within hair follicles and dermal cells, including cell growth, differentiation, and apoptosis. It is hypothesized that the addition of a palmitoyl group might impact the peptide’s lipophilicity. This may potentially support the peptide’s ability to traverse cellular membranes. Furthermore, Palmitoyl AHK is believed to exhibit an affinity for copper ions, which might theoretically alter the peptide’s conformation or stabilize its structure, potentially impacting its bioactivity.

Researchers understand copper to participate in redox reactions and enzymatic processes, so its association with AHK might, in principle, modulate the peptide’s role in processes like collagen synthesis and cellular repair. That said, further research is needed to confirm both the biological functions of AHK and the efficacy of its palmitoylated form in promoting cellular penetration and subsequent biological activity. Due to the lack of available research on Palmitoyl AHK, studies conducted using data collected in laboratory settings have focused mostly on the non-modified AHK version.

 

Research

Palmitoyl AHK and Hair Follicle Cells

Research by Sadgrove et al. has suggested that AHK may be linked to a possible impact on Transforming Growth Factor Beta 1 (TGF-β1).(2) TGF-β1, sometimes viewed as a critical cytokine, is studied for its role in cell growth, immune regulation, and wound repair. If AHK-Cu happens to lower TGF-β1 levels, it might modify certain cell processes or immune responses. Researchers have posited that a reduction in TGF-alpha by AHK may create a more favorable environment for the proliferation and survival of dermal papilla cells, which in turn might potentially promote hair follicle cell growth.

Scientists consider dermal papilla cells to be a specialized subset of fibroblasts located at the base of hair follicles. TGF-alpha, being a growth factor, might ordinarily act to modulate cellular differentiation and proliferation, so its reduction may potentially shift the balance toward better-supported cell proliferation in these cells. More in-depth research by Pyo et al. posits that the modulation of apoptosis-related proteins may be a key aspect of AHK’s potential. (3) The peptide is believed to increase the expression of Bcl-2, an anti-apoptotic protein, while concurrently decreasing the expression of Bax, a pro-apoptotic protein.

This shift in the Bcl-2/Bax ratio may favor cell survival by possibly inhibiting the mitochondrial pathway of apoptosis. Additionally, AHK appears to impact downstream effectors of apoptosis, as data indicates in numbers that reflect an apparent reduction in the levels of cleaved caspase-3—a biomarker of cell death. This may imply that the activation of this critical executioner caspase is potentially inhibited. Moreover, the researchers observed a corresponding decrease in poly (ADP-ribose) polymerase cleavage fragments, suggesting that the proteolytic processing associated with cell death may also be attenuated.

Poly (ADP-ribose) polymerase is a nuclear enzyme involved in DNA repair and the maintenance of genomic integrity, and its cleavage is typically considered a hallmark of apoptosis. These interactions with Bcl-2, Bax, caspase-3, and poly (ADP-ribose) polymerase collectively suggest a mechanism by which Palmitoyl AHK might modulate the apoptotic threshold of dermal papilla cells (DPCs) and possibly support their survival. Based on these observations, the authors concluded “that AHK-Cu promotes the growth of […] hair follicles, and this stimulatory effect may occur due to stimulation of the proliferation and the preclusion of the apoptosis of DPCs.”(3)

Palmitoyl AHK and Dermal Cells

Palmitoyl AHK may support the normal function and growth of dermal cells by interacting with dermal fibroblasts, the primary cells responsible for synthesizing the extracellular matrix and collagen. These cells are thought to provide structural integrity to the skin through the production and maintenance of collagen and other matrix proteins. A study by Patt et al. suggests that the addition of AHK may stimulate these fibroblasts, leading to increased proliferation and better-supported cell viability.

In cultured cells derived from murine models, experimentation with various concentrations of the complex apparently increased cell numbers, as determined by standard assays such as neutral red uptake and sulforhodamine B staining, which are commonly exposed to research models in laboratory settings to evaluate cellular viability and density. Furthermore, the data indicate that the peptide may impact the formation of collagen type I, with collagen production increasing by up to 300% compared to controls. This suggests that AHK might potentially accelerate the renewal of the extracellular matrix by promoting collagen synthesis through its action on fibroblasts. Consequently, Patt et al. concluded that the peptide “increases the growth and viability of dermal fibroblasts while stimulating the production of collagen.”

Collagen type I is a critical component of the extracellular matrix and plays an essential role in providing tensile strength and structural support to dermal cells. It forms the bulk of the collagen found in connective tissues and is fundamental for maintaining the dermal layer’s firmness and resilience. In the context of dermal repair and renewal, the presence of collagen type I is posited to be crucial for re-establishing the proper architecture of the extracellular matrix, thereby facilitating the repair process following cellular stress or injury. Better-supported collagen synthesis, as observed in the study, may contribute to a more robust and potentially more stable matrix environment, which in turn might support the optimal functioning of dermal cells.

You can find Pal AHK Peptide for sale with 99% purity, on our website (available for research use only).

NOTE: These products are intended for laboratory research use only. This peptide is not intended for personal use. Please review and adhere to our Terms and Conditions before ordering.

 

References:

  1. Kapoor R, Shome D, Vadera S, Kumar V, Ram MS. QR678 & QR678 Neo Hair Growth Formulations: A Cellular Toxicity & Animal Efficacy Study. Plast Reconstr Surg Glob Open. 2020 Aug 25;8(8):e2843. doi: 10.1097/GOX.0000000000002843. PMID: 32983753; PMCID: PMC7489598.
  2. Sadgrove NJ, Simmonds MSJ. Topical and nutricosmetic products for healthy hair and dermal antiaging using “dual-acting” (2 for 1) plant-based peptides, hormones, and cannabinoids. FASEB Bioadv. 2021 Jun 6;3(8):601-610. doi: 10.1096/fba.2021-00022. PMID: 34377956; PMCID: PMC8332470.
  3. Pyo HK, Yoo HG, Won CH, Lee SH, Kang YJ, Eun HC, Cho KH, Kim KH. The effect of the tripeptide-copper complex on human hair growth in vitro. Arch Pharm Res. 2007 Jul;30(7):834-9. doi: 10.1007/BF02978833. PMID: 17703734.
  4. Patt, L. M., & Procyte, A. (2009). Neova® DNA Repair Factor Nourishing Lotion Stimulates Collagen and Speeds Natural Repair Process. skin, 1, 2.

Dr. Marinov

Dr. Marinov (MD, Ph.D.) is a researcher and chief assistant professor in Preventative Medicine & Public Health. Prior to his professorship, Dr. Marinov practiced preventative, evidence-based medicine with an emphasis on Nutrition and Dietetics. He is widely published in international peer-reviewed scientific journals and specializes in peptide therapy research.

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