Snap-8 10mg

SNAP-8 (INCI name: acetyl octapeptide-3, also sometimes written acetyl octapeptide-1 in older literature) is an 8-amino-acid cosmetic peptide derived from the N-terminal region of SNAP-25, the synaptosomal-associated protein of 25 kDa that is a core SNARE-complex component required for synaptic vesicle fusion at neuronal presynaptic terminals. SNAP-8 is the 8-amino-acid extension/analog of the better-known 6-amino-acid Argireline (acetyl hexapeptide-8 / acetyl hexapeptide-3) and was developed as a successor cosmetic peptide in the SNAP-25-fragment chemotype originally developed by Lipotec S.A. The molecule is used as an active ingredient in topical anti-aging cosmetic formulations with the proposed cosmetic positioning of softening expression-line appearance through a mechanism related to SNARE-complex modulation in cultured cell systems.

This page is a research-only educational reference for SNAP-8 as a cosmetic-ingredient research peptide. The molecule is a cosmetic ingredient regulated under cosmetic-product frameworks, not a medicine; no medical or therapeutic claims are made on this page.

SNAP-8 is the N-terminal-acetylated octapeptide with sequence Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH2 (with amide-capped C-terminus). The molecular weight is approximately 990 g/mol. The sequence corresponds to a portion of the N-terminal region of SNAP-25 with two additional residues relative to the parent Argireline hexapeptide (which corresponds to a slightly shorter portion of the same SNAP-25 region). The N-terminal acetylation and C-terminal amidation are the standard cosmetic-peptide protective modifications providing resistance to exopeptidase degradation.

SNAP-25 is a presynaptic SNARE-complex component required for synaptic vesicle fusion at neuronal terminals. The SNARE complex consists of three principal components: SNAP-25, syntaxin-1, and synaptobrevin/VAMP, which assemble into a four-helix coiled-coil bundle that brings the vesicle and plasma membranes into apposition and drives membrane fusion releasing neurotransmitter into the synaptic cleft. SNAP-25 is also the cleavage target of botulinum neurotoxin serotypes A and E (BoNT/A, BoNT/E), the protease-toxin basis for therapeutic and cosmetic botulinum-toxin products. The pharmacological positioning of SNAP-25-fragment cosmetic peptides like SNAP-8 and Argireline is based on the proposal that the peptide can interfere with SNARE-complex assembly through a competitive mechanism, modulating neurotransmitter-release efficiency at neuromuscular junctions when applied topically.

It is important to be clear about the mechanistic and regulatory framing. SNAP-8 and Argireline are cosmetic ingredients, not pharmaceutical neurotoxin substitutes. They are not botulinum-toxin equivalents. The proposed mechanism — SNARE-complex modulation — is characterized in cell-culture systems with reports of effects on catecholamine secretion from cultured chromaffin cells and related preparations; the in-vivo translation of these effects after topical cosmetic application to human skin is necessarily different from the effects of injected pharmaceutical botulinum toxin and should not be confused with that pharmacology. The cosmeceutical research literature on SNAP-8 includes published clinical-research studies of topical formulations with reports of effects on wrinkle measurements and skin-texture parameters in cosmetic-product evaluation studies.

Lipotec S.A. (a Spanish cosmetic-ingredients company, subsequently part of the Lubrizol group) developed Argireline (acetyl hexapeptide-8) as a cosmetic peptide in the late 1990s and 2000s based on the SNAP-25-fragment design rationale. Argireline became a widely recognized cosmeceutical-peptide active ingredient. SNAP-8 was developed as a successor cosmetic peptide in the same chemotype, extending the Argireline hexapeptide by two N-terminal residues and providing a related cosmetic-active ingredient with similar mechanistic positioning. The two peptides are sold and used as cosmetic-formulation ingredients across many topical anti-aging cosmetic products. Published cosmetic-research evaluation includes cultured cell-system studies (chromaffin cell preparations, dermal fibroblast cultures), and human clinical-research studies of topical formulations evaluating wrinkle and skin-texture endpoints.

SNAP-8 is regulated under the cosmetic-product framework of the FDA in the US, the Cosmetics Regulation in the EU, and equivalent frameworks in other jurisdictions. It is not approved as a pharmaceutical for any indication and is not a medicine.

The SNARE-complex apparatus for synaptic vesicle fusion is a central component of neurotransmitter release at neuronal presynaptic terminals. The complex consists of SNAP-25 (on the plasma membrane), syntaxin-1 (on the plasma membrane), and synaptobrevin/VAMP (on the vesicle membrane), which assemble into a four-helix coiled-coil bundle that brings the vesicle and plasma membranes together and drives fusion. The SNARE complex is regulated by additional proteins (synaptotagmin as the calcium sensor, complexins as fusion clamps, Munc18 and Munc13 as assembly factors) that determine the precise calcium-triggered timing of fusion. SNAP-25 specifically contributes two of the four helices in the assembled SNARE bundle (the N-terminal and C-terminal SNARE motifs of SNAP-25).

The proposed mechanism of SNAP-8 and Argireline as cosmetic SNARE-complex modulators is that the synthetic peptides — sharing sequence identity with a region of SNAP-25 — can compete with endogenous SNAP-25 for incorporation into assembling SNARE complexes, producing non-productive complexes that reduce the efficiency of vesicle fusion and neurotransmitter release. The cellular evidence for this mechanism comes from cultured chromaffin-cell preparations (a classical cell model for regulated secretion that uses the same SNARE-complex apparatus as neuronal terminals) with reports of attenuated catecholamine release in response to depolarizing stimuli in the presence of the peptide. The in-vivo translation of this cellular pharmacology to topical cosmetic application on human skin involves topical-delivery considerations (the peptide must reach viable epidermis and dermis), local-application considerations (effects would be expected only in the local application site, not systemic), and dose-response considerations (cosmetic-formulation concentrations are far below pharmaceutical-injectable botulinum-toxin equivalents).

The cosmetic-positioning of SNAP-8 is as a topical anti-expression-line cosmetic active ingredient. Published cosmetic-product evaluation studies have reported effects on wrinkle depth (particularly around the eyes and forehead, where expression lines are prominent), on skin-texture parameters, and on subjective skin-appearance assessments over typical 4-12 week cosmetic-product evaluation periods. Effect magnitudes are modest in the cosmetic-product evaluation context and are not equivalent to the effects of pharmaceutical injected botulinum toxin.

SNAP-8 is the acetylated and amidated octapeptide Ac-Glu-Glu-Met-Gln-Arg-Arg-Ala-Asp-NH2. The molecular weight is approximately 990 g/mol. The N-terminal acetyl and C-terminal amide modifications provide resistance to exopeptidase degradation. Research-grade SNAP-8 is produced by solid-phase peptide synthesis, purified by reversed-phase HPLC to ≥98% purity, and verified by analytical HPLC and mass spectrometry. The product is typically supplied as a lyophilized peptide for laboratory or formulation work, or as a solution in a cosmetic-compatible carrier at a standardized concentration for formulation use. Storage of the lyophilized peptide is at -20 °C or below; solution-format storage follows the supplier's specific instructions.

In published cosmetic and cell-biology research, SNAP-8 has been used in cultured cell-system studies of regulated secretion (chromaffin cell preparations, related secretory cell models) investigating the SNARE-complex modulation hypothesis; in cosmetic-formulation development for incorporation as an active ingredient in topical anti-aging products; in published clinical-research evaluation of topical SNAP-8-containing cosmetic formulations in human skin with wrinkle, skin-texture, and subjective-appearance endpoints; and in comparative cosmeceutical-peptide research alongside Argireline, Matrixyl, GHK-Cu and other cosmetic-peptide active ingredients. All applications are research and cosmetic-formulation context; the molecule is a cosmetic ingredient, not a medicine.

SNAP-8 sits within the cosmeceutical-peptide active-ingredient category alongside the closely related Argireline and the broader Matrixyl-family and copper-peptide cosmetic actives.

SNAP-8 (INCI: acetyl octapeptide-3) is an 8-amino-acid SNAP-25-fragment cosmetic peptide developed by Lipotec as an extension of the Argireline (acetyl hexapeptide-8) chemotype. The peptide is proposed to interfere with SNARE-complex assembly through a competitive mechanism, modulating neurotransmitter-release efficiency in cultured cell systems. It is used as an active ingredient in topical anti-aging cosmetic formulations with published cosmetic-product evaluation studies reporting effects on wrinkle and skin-texture endpoints. SNAP-8 is a cosmetic ingredient regulated under cosmetic-product frameworks; it is NOT equivalent to and does NOT substitute for pharmaceutical injected botulinum toxin, which is an entirely distinct molecular class and regulatory category. This page is research educational only; no medical or therapeutic claims are made.