dipeptide diaminobutyroyl benzylamide diacetate
beta-Ala-Pro-Dab-NH-Bzl diacetate, beta-alanyl-L-prolyl-L-2,4-diaminobutyryl benzylamide diacetate, waglerin-1 mimetic peptide, synthetic tripeptide amide diacetate
This is a fully synthetic small molecule, not a natural peptide and not a venom product, designed to imitate the C-terminal region of waglerin-1, a 22-residue toxin from the venom of Wagler's pit viper that blocks the adult form of the muscle nicotinic acetylcholine receptor. It is sold in cosmetics as a topical alternative to injectable botulinum toxin for expression lines. The waglerin-1 receptor pharmacology it borrows is precisely characterised; the claim that this fragment reproduces it after topical application remains untested.
Mechanism
Waglerin-1 is a 22-residue, disulfide-constrained peptide from Tropidolaemus wagleri venom. McArdle and colleagues showed it is a competitive antagonist highly selective for the adult, epsilon-subunit-containing muscle-type nicotinic acetylcholine receptor, with far lower affinity for the fetal gamma-containing receptor. Molles and colleagues mapped the binding to the alpha-epsilon subunit interface and identified the epsilon-subunit residues responsible for selectivity, including the marked species selectivity between mouse and human receptors. Blocking postsynaptic nicotinic receptors at the neuromuscular junction reduces endplate depolarisation and therefore contraction; Tsai and colleagues documented the resulting block in mouse nerve-muscle preparations. The cosmetic logic is that reducing contraction in the small mimetic muscles of the face would soften dynamic lines.
The ingredient is not waglerin-1. It is a three-residue construct (beta-alanine, proline and 2,4-diaminobutyric acid, capped as a benzylamide) intended to reproduce the C-terminal proline-basic-residue motif. It is designated a dipeptide under INCI convention because only proline and diaminobutyric acid count as alpha-amino acids. The extrapolation has structural and pharmacokinetic problems. Waglerin-1's potency depends on a folded, disulfide-stabilised conformation presenting a defined surface to the receptor interface; a linear tripeptide fragment cannot present that surface, and no published binding or electrophysiology study reports nicotinic antagonism by this molecule. Separately, even a potent antagonist would have to traverse intact stratum corneum, viable epidermis and dermis to reach neuromuscular junctions in the subcutis, a delivery problem no published work addresses.
What the research shows
The waglerin literature is precise and replicated. Schmidt and Weinstein characterised the waglerin peptides and their structure-activity relationships in 1992. McArdle and colleagues demonstrated in 1999 that waglerin-1 selectively blocks the epsilon form of the muscle nicotinic receptor. Molles and colleagues published two complementary 2002 papers, one in the Journal of Biological Chemistry identifying residues at the alpha and epsilon subunit interfaces mediating species selectivity, and one in Biochemistry showing how epsilon-subunit residues interact to confer selectivity for the alpha-epsilon site. Tsai and colleagues characterised the neuromuscular consequences in mouse preparations. This is a textbook example of a subunit-selective toxin used as a pharmacological probe, and none of it involves topical delivery, skin, or the cosmetic mimetic.
For the ingredient itself, the single relevant publication is the Zhu 2026 study, which reported that the serum increased elastic and collagen fibres in ex vivo skin and improved clinical wrinkle scoring by 35 to 69 per cent for static wrinkles over 12 weeks and 10 to 13 per cent for dynamic wrinkles, alongside improvements in smoothness, radiance, pore appearance, elasticity and firmness. Read carefully, this tells you about a multi-ingredient serum containing niacinamide and a polyhydroxy acid, not about the waglerin mimetic. Anyone comparing this ingredient with injected botulinum toxin should note that botulinum toxin acts presynaptically to prevent acetylcholine release and is injected directly into the target muscle; the two are not comparable in mechanism, delivery or evidential status.
Evidence assessment
Preclinical only
There is no published receptor-binding, electrophysiology or animal study of the ingredient. The draft this record corrects also claimed no clinical trial exists; that is now outdated. Zhu and colleagues (2026, International Journal of Cosmetic Science) reported an ex vivo human skin biomarker study plus two clinical studies (n=50 for static wrinkles, n=42 for dynamic wrinkles) of a serum containing this compound together with acetyl hexapeptide-8, gluconolactone, niacinamide and laminaria extract. That work is entirely authored by researchers at a multinational cosmetics manufacturer, tests a five-active formulation with no single-ingredient arm, and measures wrinkle appearance rather than any neuromuscular endpoint. It is real published clinical work on a product containing the molecule, and it is not evidence that the molecule antagonises nicotinic receptors or does anything in isolation. The tier therefore stays preclinical.
Tiers are applied consistently across the library and re-checked when new trials read out. Read the grading method.
Key studies
The effect of a serum containing acetyl hexapeptide-8, dipeptide diaminobutyroyl benzylamide diacetate and gluconolactone on skin biomarkers, wrinkles and skin texture: Ex vivo and clinical studies Preclinical only
The serum increased elastic and collagen fibres ex vivo and improved static wrinkle clinical scoring by 35-69% over 12 weeks and dynamic wrinkles by 10-13%, with improvements in smoothness, radiance, pore appearance, elasticity and firmness.
Molecular properties and structure-function relationships of lethal peptides from venom of Wagler's pit viper, Trimeresurus wagleri Preclinical only
Characterised the waglerin family and the sequence features required for lethality, defining the parent molecule the cosmetic ingredient claims to imitate.
Waglerin-1 selectively blocks the epsilon form of the muscle nicotinic acetylcholine receptor Preclinical only
Established waglerin-1 as a competitive antagonist highly selective for the adult, epsilon-subunit-containing muscle nicotinic receptor.
Identification of residues at the alpha and epsilon subunit interfaces mediating species selectivity of Waglerin-1 for nicotinic acetylcholine receptors Preclinical only
Mapped waglerin-1 binding to the alpha-epsilon subunit interface and identified the residues responsible for its marked species selectivity.
Residues in the epsilon subunit of the nicotinic acetylcholine receptor interact to confer selectivity of waglerin-1 for the alpha-epsilon subunit interface site Preclinical only
Defined the epsilon-subunit residue network producing waglerin-1's site selectivity, showing how tightly the toxin's activity depends on its full three-dimensional presentation.
Effects of waglerin-I on neuromuscular transmission of mouse nerve-muscle preparations Preclinical only
Documented postsynaptic neuromuscular block by waglerin-1, the functional consequence underlying the cosmetic rationale.
Safety
No adverse effects have been attributed to the molecule, and there is a straightforward reason to expect none: there is no evidence it reaches or acts on the neuromuscular junction. Consumers occasionally worry that products containing it carry venom-related risk. They do not. The ingredient is synthesised chemically, contains no snake-derived material, and is not waglerin-1. The Zhu 2026 clinical studies reported no tolerability problems for the finished serum, though that assessment covers the whole formulation. The residual uncertainties are the ordinary ones for a barely studied cosmetic ingredient: no repeat-insult patch test data in the public literature, no reproductive or developmental data, and no human pregnancy or lactation data. It is a topical cosmetic ingredient; it has not been evaluated for injection, and injecting a nicotinic-receptor mimetic without any toxicology would be reckless.
Regulatory status
| Jurisdiction | Status |
|---|---|
| United Kingdom | Permitted as a cosmetic ingredient under the UK Cosmetics Regulation (retained Regulation (EC) No 1223/2009); not listed in any prohibited or restricted annex. A Cosmetic Product Safety Report and responsible person are required. Claims positioning a cosmetic as an alternative to an injectable prescription medicine are liable to challenge under UK advertising rules and can render a product medicinal by function, bringing it within MHRA jurisdiction. No MHRA medicines authorisation. |
| United States | Not an FDA-approved drug and not covered by an OTC drug monograph; marketed as a cosmetic ingredient under the FD&C Act as amended by the Modernization of Cosmetics Regulation Act 2022. Marketing that positions a product as an alternative to botulinum toxin injections invites classification as an unapproved drug. |
| WADA (sport) | Not named on the WADA Prohibited List. Topical cosmetic use raises no anti-doping issue. |
Questions
No. It is a fully synthetic molecule made in a laboratory. It contains no snake-derived material and it is not waglerin-1; it is a three-residue construct designed to resemble part of that toxin.
There is no published evidence supporting that comparison, and the mechanisms differ fundamentally. Botulinum toxin is injected into a specific muscle and acts presynaptically to prevent acetylcholine release. This ingredient is applied to the skin surface and is claimed to act postsynaptically; no study demonstrates that it reaches a neuromuscular junction or blocks a nicotinic receptor.
There is one 2026 publication reporting ex vivo skin work and two clinical studies of a serum containing it. But the serum also contained acetyl hexapeptide-8, gluconolactone, niacinamide and laminaria extract, the studies were run and authored entirely by the manufacturer, and no arm isolated this ingredient. It is evidence for a product, not for the molecule.
INCI nomenclature counts only alpha-amino acid residues. Proline and 2,4-diaminobutyric acid are counted; the N-terminal beta-alanine is treated as an acyl group and the C-terminal benzylamide as a cap. Hence 'dipeptide diaminobutyroyl benzylamide'.