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Syn-Ake | CAS: Available Upon Request

CAS Number:
Available Upon Request
Chemical Classification:
Research peptide

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Syn-Ake is a synthetic tripeptide inspired by temple viper waglerin sequences, used in dermatological research as a probe of nicotinic acetylcholine receptor modulation at the neuromuscular junction. Receptor subtype expression in skin-derived models differs from skeletal muscle, so relaxation endpoints must be interpreted within the specific cell system employed. Researchers deploy the peptide in micronucleus-free fibroblast contractility assays, in vitro neuromuscular junction co-cultures, and peptide-library screens comparing waglerin-mimetic scaffolds. Characterization follows COA and purity profiling standards for short synthetic peptides; laboratory research only.

CAS
Available Upon Request
Molecular Formula
C19H29N3O6
Molecular Weight
395.5 g/mol
Purity
≥98%
Appearance
White lyophilized powder
Storage
Store at -20°C

Analytical Documentation

COA✓ Available
LC-MS✓ Available
HPLC✓ Available
NMR✓ Available

Research Inquiry

Overview

Syn-Ake is a synthetic tripeptide dipeptide mimic inspired by waglerin, a peptide from Temple viper venom that antagonizes muscle nicotinic acetylcholine receptors at the neuromuscular junction. The sequence beta-Ala-Pro-Dab-NH2, with diaminobutyric acid in D-configuration, provides a non-toxic research alternative for studying nicotinic receptor blockade in cosmetic muscle relaxation assays. Syn-Ake enables dermatological research on micro-contraction-driven wrinkle formation through reversible nAChR antagonism in muscle cell culture and skin equivalent models without paralytic toxin administration. The peptide represents venom-inspired cosmetic biochemistry studied alongside Snap-8 SNARE inhibitors in complementary mechanism platforms. Supplied at ≥98% purity (C19H29N3O6; 395.5 g/mol), this material supports controlled laboratory investigation under research-use-only conditions.

Mechanism of Action

Syn-Ake antagonizes muscular nicotinic acetylcholine receptors, reducing calcium influx and actin-myosin contraction in muscle cell line research used in cosmetic wrinkle mimic assays. Reversible binding kinetics distinguish Syn-Ake from irreversible snake venom neurotoxins in safety profiling research. Reduced micro-contraction in skin equivalent models correlates with smoother surface topography in imaging readouts standardized by cosmetic research groups. Mechanism is postsynaptic receptor blockade unlike presynaptic Snap-8 SNARE interference. Syn-Ake does not affect SNARE protein cleavage or fusion directly.

Receptor Binding & Signaling

Syn-Ake targets muscle-type nicotinic acetylcholine receptors (nAChR alpha1/beta1/delta/epsilon subunits) with selectivity over neuronal nAChR subtypes in binding research. No muscarinic or GABA receptor engagement at cosmetic research concentrations. Competitive antagonism reversible upon washout in cell culture.

Research Applications

Nicotinic receptor antagonism assays

Radioligand binding on muscle nAChR membranes and electrophysiology on heterologous nAChR expression systems quantify Syn-Ake IC50 values for batch QC. Waglerin used as structural comparator in venom peptide research. Cosmetic biochemistry validates receptor specificity.

Muscle cell contraction mimic models

Myoblast-derived cell lines in collagen matrices contract upon electrical or chemical stimulation; Syn-Ake reduces contraction amplitude in research imaging assays. Calcium fluorophore imaging confirms mechanism. Platforms model wrinkle formation biochemistry in vitro.

Skin equivalent topography research

Reconstructed skin with embedded muscle mimic layers treats with Syn-Ake measuring surface roughness by profilometry or optical coherence tomography in cosmetic research. Controls include Snap-8 for mechanism comparison. Studies remain preclinical dermatological science.

Venom peptide structure-activity research

Analogs of waglerin sequence explore D-amino acid substitutions for receptor selectivity and stability in peptide medicinal chemistry programs. Syn-Ake serves as lead cosmetic research peptide in this series. Stability and purity characterized by HPLC-MS.

Molecular Information

Sequence & Chain Summary

β-Ala-Pro-Dab-NH2 (Diaminobutyric acid in D-configuration; tripeptide).

Modification Type

D-configured diaminobutyric acid (Dab); C-terminal amide.

Structural Notes

Syn-Ake molecular weight 395.5 g/mol as small tripeptide with high synthetic accessibility. D-amino acid confers protease resistance. RP-HPLC and MS confirm identity and enantiomeric purity critical for receptor selectivity research. Batch-specific molecular characterization—including mass confirmation and purity profiling—is available through COA, LC-MS, HPLC, and NMR documentation supplied with Syn-Ake.

Molecular Formula
C19H29N3O6
Molecular Weight
395.5 g/mol
Purity Specification
≥98%

Experimental Notes

Stability

Lyophilized Syn-Ake stable at −20°C. Small peptide degrades microbially in reconstituted aqueous solutions at room temperature over extended periods; use sterile technique and refrigeration for culture assays. Lyophilized Syn-Ake should be protected from repeated freeze-thaw cycles, moisture, and prolonged exposure to ambient light where applicable. Analytical integrity is best preserved when material is stored under the conditions specified on the certificate of analysis.

Storage Conditions

Store at -20°C. Syn-Ake is supplied as white lyophilized powder. For long-term archival storage in research inventories, maintain sealed containers with desiccant where recommended and document lot numbers for traceability across experimental runs.

Laboratory Handling

Reconstitute in sterile water for cell-based contraction assays. Avoid mixing with SNARE-targeting peptides in same assay without factorial design to separate mechanisms. Document antagonist concentration in micromolar ranges typical for nAChR research. Reconstitute only with appropriate research-grade solvents compatible with your assay format. Allow vials to reach equilibrium before opening, work under clean bench conditions, and label all working solutions with concentration, date, and researcher ID per institutional SOPs.

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Frequently Asked Questions

Research-focused answers about Syn-Ake. For laboratory use only — not medical advice.

What is Syn-Ake used for in research?
Syn-Ake is for cosmetic science and nicotinic receptor research in muscle cell and skin equivalent models. Not for injectable neuromodulation, human wrinkle treatment, or venom-derived therapeutic administration.
How does Syn-Ake work biologically?
Syn-Ake reversibly antagonizes muscle nicotinic acetylcholine receptors, reducing micro-contraction in cosmetic research models mimicking neuromuscular contributions to skin topography changes.
What receptors does Syn-Ake interact with?
Primary target is muscle-type nicotinic acetylcholine receptor (nAChR). Selectivity over neuronal nAChR subtypes supports cosmetic muscle relaxation assay specificity versus central effects.
Is Syn-Ake stable at room temperature?
Lyophilized Syn-Ake stable at −20°C. Small peptide degrades microbially in reconstituted aqueous solutions at room temperature over extended periods; use sterile technique and refrigeration for culture assays. For short-term laboratory workflows, minimize time at room temperature and return unused material to recommended storage promptly. Syn-Ake is not formulated for ambient long-term storage.
What is the recommended storage condition for Syn-Ake?
Store at -20°C. Store lyophilized material in a dedicated −20°C freezer, protect from moisture ingress, and avoid repeated temperature cycling. Reconstituted solutions should be aliquoted and frozen if not used within the validated window of your internal stability study.