SYN-AKE
C23H37N5O7
Research Use Only. SYN-AKE is a research compound intended strictly for laboratory and scientific research purposes. It is not approved for human consumption, therapeutic use, or veterinary use. Information on this page is provided for educational and research reference purposes only.
Overview
SYN-AKE is a synthetic tripeptide that was designed to mimic the activity of a naturally occurring compound found in the venom of the Temple Viper (*Tropidolaemus wagleri*), specifically a peptide known as waglerin-1. It belongs to a class of compounds studied for their ability to interact with neuromuscular junction receptors, making it of interest to researchers exploring how such interactions occur at a molecular level. SYN-AKE is sometimes categorized as a neuropeptide mimic due to its structural resemblance to naturally occurring venom-derived compounds. With the molecular formula C23H37N5O7 and a molecular weight of approximately 495.6 g/mol, it is used strictly in laboratory and research settings to better understand peptide-receptor interactions and related biological mechanisms. All research involving SYN-AKE is conducted for scientific inquiry only, and it is not approved or intended for human use.
Compound Data
| CAS Number |
823202-99-9 |
| Molecular Formula |
C23H37N5O7 |
| Molecular Weight |
495.60 g/mol |
| IUPAC Name |
acetic acid;(2S)-N-[(2S)-4-amino-1-(benzylamino)-1-oxobutan-2-yl]-1-(3-aminopropanoyl)pyrrolidine-2-carboxamide |
| PubChem CID |
71465152
|
Research & Bioactivity
Researchers have studied SYN-AKE, a synthetic tripeptide analog inspired by a component found in temple viper venom, primarily in the context of skin biology and the molecular processes associated with aging. Studies have examined its potential interactions with matrix metalloproteinases (MMPs), enzymes involved in the breakdown of extracellular matrix proteins such as collagen, as well as with Sirtuin 1 (SIRT1), a protein linked to cellular regulation and longevity pathways. Research has investigated how SYN-AKE may interact with neuromuscular signaling mechanisms, specifically in relation to acetylcholine receptor activity, which has made it a subject of interest in studies exploring muscle contraction at a cellular level. In vitro and computational modeling approaches have been used to characterize these molecular interactions and better understand the peptide's binding behavior with relevant biological targets. As interest in synthetic peptides for research applications continues to grow, SYN-AKE has been included in studies aimed at identifying candidate molecules for further investigation in dermatological and aging-related research contexts.
Also Known As
- 823202-99-9
- Syn-ake
- Dipeptide diaminobutyroyl benzylamide diacetate
- 38H206R00R
- UNII-38H206R00R
- DTXSID40231699
- Dipeptide diaminobutyroyl benzylamide diacetate [INCI]
- Butanamide, beta-alanyl-L-prolyl-2,4-diamino-N-(phenylmethyl)-, (2S)-, acetate (1:2)
- Butanamide, beta-alanyl-L-prolyl-2,4-diamino-N-(phenylmethyl)-, (2S)-, diacetate
- BUTANAMIDE, .BETA.-ALANYL-L-PROLYL-2,4-DIAMINO-N-(PHENYLMETHYL)-, (2S)-, DIACETATE
- BUTANAMIDE, .BETA.-ALANYL-L-PROLYL-2,4-DIAMINO-N-(PHENYLMETHYL)-, (2S)-, ACETATE (1:2)
- RefChem:134618
- DTXCID20154190
- Syn-Ake acetate
- (2S)-beta-Alanyl-L-prolyl-2,4-diamino-N-(phenylmethyl)butanamide acetate
Published Research
Anti-aging activity of Syn-Ake peptide by approaches and tests.
Gok B, Budama-Kilinc Y, Kecel-Gunduz S — 2024
The increase in the aging population worldwide has led scientists to turn to research to prevent the aging process. In this context, synthetic peptides emerge as candidate molecules for developing new anti-aging products. This study aims to investigate the possible interactions of Syn-Ake, a synthetic peptide, with matrix metalloproteinases (MMPs) and Sirtuin 1 (SIRT1), which are the targets of anti-aging activities with approaches, and to determine the antioxidant activity, and safety profile of the peptide by methods such as cytotoxicity (MTT) and genotoxicity (Ames) tests. The molecular docking study showed that the docking score energy of MMP receptors was in the order of MMP-13 < MMP-8 < MMP-1. Syn-Ake peptide provided the lowest and the most stable binding to the SIRT1 receptor at -9.32 kcal/mol. Binding interaction and protein-ligand stability of Syn-Ake with MMPs and SIRT1 in a dynamic system were predicted by 50 ns molecular dynamic (MD) simulation studies. The MD results showed that the Syn-Ake peptide remained stable in the active site of MMP-13 and SIRT1 receptors during 50 ns simulations. In addition, the antioxidant activity of Syn-Ake was investigated using diphenyl-2-picril-hydrazine (DPPH) method since it is crucial to remove free radicals that are effective in skin aging. The results revealed the concentration-dependent increased DPPH radical scavenging activity of the peptide. Finally, the safety of the Syn-Ake was investigated, and the safe dose of the peptide was determined. In conclusion, and analyses show that the Syn-Ake peptide may hold promise in anti-aging formulations with its high efficacy and safety profile.Communicated by Ramaswamy H. Sarma.