Vialox Peptide: Interactions with Dermal Tissue Topography

Vialox appears to be a synthetic pentapeptide comprising the sequence Gly–Pro–Arg–Pro–Ala (GPRPA), also referred to as pentapeptide-3. It is purportedly derived from proteolytic fragments of snake venom, with its alternating proline residues perhaps lending conformational stability that favors receptor engagement.⁽¹⁾ Vialox peptide is believed to function as a competitive antagonist at nicotinic acetylcholine receptors on the post-synaptic membrane of neuromuscular junctions.

By occupying the acetylcholine-binding site, the peptide may mitigate the sodium ion influx normally triggered by receptor activation, thereby mitigating depolarization and sustaining muscular tissue relaxation in a curare-like manner. Due to this potential, Vialox peptide is actively researched for its action on dermal topography, such as wrinkles and epidermal roughness, in laboratory settings. Recent in silico studies, such as the 2025 experiment by Arkham et al., further suggest that Vialox peptide may contribute to the modulation of other ligand-gated ion channels or intracellular signaling cascades in mammalian research models, indicating a broader spectrum of bioactivity observed in laboratory settings.⁽²⁾

Research

Vialox peptide Actions On The N-Acetylcholine Receptors

Vialox peptide is posited to be a curare-like agent that may compete with acetylcholine for the same orthosteric binding sites at nicotinic acetylcholine receptors. These receptors appear to be found at the neuromuscular junction and may be pentameric ligand-gated ion channels assembled from α- and non-α subunits. Each receptor is posited to contain two acetylcholine binding sites located at the interfaces between adjacent subunits. The binding of acetylcholine appears to induce a conformational change that opens the central pore, allowing sodium ion influx, membrane depolarization, and subsequent muscle cell contraction.

Research by Lupo et al. and Hadmed et al. suggests that by occupying one or both sites without triggering the full conformational shift toward the open-channel state, Vialox peptide may stabilize the receptor in a “resting” or “desensitized” conformation.⁽³⁾⁽⁴⁾ In this scenario, even if acetylcholine diffuses into the synaptic cleft, the presence of Vialox peptide at the binding pocket should mitigate adequate pore opening, thereby mitigating sodium ion permeation and blocking end-plate depolarization. At the molecular level, curare-type antagonists like Vialox peptide are posited to interact with the so-called “cys-loop” motif in the extracellular domain, as well as with residues lining the channel pore’s M2 transmembrane helices.

Vialox’s Gly–Pro–Arg–Pro–Ala scaffold may position its arginine side chain toward aromatic residues in the binding pocket (such as Trp149 or Tyr190 in the α-subunit), mimicking key cation–π and hydrogen-bond interactions of acetylcholine. At the same time, its proline kinks may hinder the larger global movements required for full channel gating. Functionally, this blockade may manifest as a non-depolarizing mitigation, during which muscular tissue fibers remain at resting membrane potential rather than becoming persistently depolarized, and action-potential propagation is halted. According to in vitro experiments by Gorouhi and Maibach, the peptide implication may result in “muscle [tissue] contractions reduced by 71% within 1 min […] and 58% 2 h later. Less frequent muscle [cell] contractions result in shallower lines.”⁽⁵⁾

Other Potential Mechanisms of Vialox peptide

In addition to its curare‐like blockade of nicotinic receptors, research by Arkham et al. suggests that Vialox peptide may engage key signaling pathways implicated in dermal cell aging.⁽²⁾ The researchers employed in silico docking and observed that the peptide may bind the kinase domain of TGF-β receptor-1, hinting that it might modulate Smad‐dependent collagen synthesis.

By occupying residues such as ASP290 and HIS283, Vialox peptide may support TGF-β’s regulation of extracellular matrix turnover, potentially dampening the degradation of dermal collagen in laboratory settings. Furthermore, computational analyses by Arkham et al. also indicate that Vialox peptide may interact with MAPK14 (p38α), which may, in theory, attenuate stress‐activated protein kinase signaling.⁽²⁾ Such an interaction might help reduce reactive‐oxygen–species–driven inflammation in UV-exposed keratinocytes, although this remains to be confirmed in cell‐based assays.

Similarly, an apparently observed affinity for AKT-1 suggests the peptide may support cell‐survival pathways. Specifically, by transiently binding residues like ASP292 and GLU234, Vialox peptide may subtly alter downstream phosphorylation events that govern fibroblast proliferation and barrier function under oxidative stress. Moreover, the researchers apparently observed that Vialox peptide may interact with TNF-α, which raises the possibility of anti‐inflammatory action via partial stabilization of the cytokine’s conformation, perhaps reducing pro‐inflammatory signaling in dermal models.

Altogether, these in silico observations by Arkham et al. imply that, beyond neuromuscular blockade, Vialox may exert pleiotropic peptide‐mediated interactions on collagen homeostasis, stress‐kinase activation, cell survival, and inflammation—all of which warrant targeted in vitro verification.⁽²⁾

Vialox peptide Actions On Dermal Topography

In controlled laboratory assays, Vialox peptide appears to mitigate muscle cell contraction in a concentration‐dependent manner. Research by Reddy et al. suggests that the “recommended concentration is 0.05–0.3%” for scientists to observe a reliable blockade in laboratory settings.⁽⁶⁾ Some experimental studies, such as by Schagen, further suggest that prolonged exposure to these concentrations may lead to “a reduction of wrinkles by 49%, and lesser [epidermal] roughness (47%)”⁽¹⁾.

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References:

1. 1Schagen SK. Topical peptide treatments with effective anti-aging results. Cosmetics. 2017 Jun;4(2):16.
2. 2Akhan D, Bicak B, Kecel Gunduz S, Akalin E. Quantum Chemical, Spectroscopic and In Silico (Molecular Docking, Molecular Dynamic and ADME) Studies on Anti‐Aging Pentapeptide‐3 (Vialox peptide). International Journal of Quantum Chemistry. 2025 Aug 5;125(15):e70085.
3. 3Lupo MP, Cole AL. Cosmeceutical peptides. Dermatol Ther. 2007 Sep-Oct;20(5):343-9. doi: 10.1111/j.1529-8019.2007.00148.x. PMID: 18045359.
4. 4Husein El Hadmed H, Castillo RF. Cosmeceuticals: peptides, proteins, and growth factors. J Cosmet Dermatol. 2016 Dec;15(4):514-519. doi: 10.1111/jocd.12229. Epub 2016 May 3. PMID: 27142709.
5. 5Gorouhi F, Maibach HI. Role of topical peptides in preventing or treating aged skin. Int J Cosmet Sci. 2009 Oct;31(5):327-45. doi: 10.1111/j.1468-2494.2009.00490.x. Epub 2009 Jun 30. PMID: 19570099.
6. 6Reddy BY, Jow T, Hantash BM. Bioactive oligopeptides in dermatology: Part II. Exp Dermatol. 2012 Aug;21(8):569-75. doi: 10.1111/j.1600-0625.2012.01527.x. Epub 2012 Jun 4. PMID: 22672721.