# Tetradecylamine: A Newly Identified Biogenic Amine Compound from the Venom of Vespa affinis

## TL;DR

Scientists found a new compound in Asian hornet venom that can fight bacteria and may work better than some antibiotics.

## Contribution

Identification of tetradecylamine in Vespa affinis venom and its potential as an antibacterial agent with high binding affinity.

## Key findings

- Tetradecylamine showed inhibitory effects against E. coli, S. aureus, B. cereus, and K. pneumoniae at low concentrations.
- Molecular docking studies revealed tetradecylamine binds strongly to PBP2X and MurA proteins, better than some antibiotics.
- Tetradecylamine's binding affinity was comparable to or higher than doxycycline and gentamycin in tests.

## Abstract

The venom of the Asian hornet (Vespa affinis) contains a diverse array of biologically active compounds that contribute to its defensive and predatory functions. This study aimed to confirm the presence of tetradecylamine in V. affinis venom using the computational analysis software MetFrag, as well as to predict its biosynthetic pathway and potential biological functions. Bioinformatic analysis suggested that tetradecylamine may be involved in antibacterial activity, which was subsequently validated through in vitro antibacterial assays. The compound exhibited significant inhibitory effects against Escherichia coli, Staphylococcus aureus, Bacillus cereus, and Klebsiella pneumoniae at low concentrations. Furthermore, molecular docking studies demonstrated that tetradecylamine interacts favorably with penicillin-binding protein 2x (PBP2X) and UDP-N-acetylglucosamine enolpyruvyl transferase (MurA), a key enzyme involved in bacterial cell wall synthesis. Notably, tetradecylamine showed a higher predicted binding affinity than several commonly used antibiotics.

The venom of the Asian hornet (Vespa affinis) comprises a complex mixture of biologically active substances, including various enzymes such as phospholipase A and hyaluronidase; amines such as histamine, serotonin, and catecholamines; peptides such as mastoparan and vespakinin; and other components including acetylcholine and antigen 5. This complexity reflects the highly evolved nature of V. affinis as a venomous insect. The composition of animal venoms often exhibits a certain degree of variability, making the study of biogenic amines particularly intriguing. The objective of this research was to confirm and identify the presence of tetradecylamine in the venom of Vespa affinis using the scientific computational analysis software MetFrag. In addition, the study aimed to construct the biosynthetic pathway of this compound and to predict its potential biological roles. The predicted biosynthetic route of tetradecylamine suggested its possible involvement in antibacterial activity. Antibacterial assays were performed against four bacterial strains Escherichia coli, Staphylococcus aureus, Bacillus cereus, and Klebsiella pneumoniae. The results revealed that tetradecylamine exhibited notable inhibitory effects, with minimum inhibitory concentration (MIC) values of 2, 4, 8, and 4 µg/mL, and minimum bactericidal concentration (MBC) values of 2, 4, 8, and 4 µg/mL, respectively. Furthermore, molecular docking studies were conducted using penicillin-binding protein 2x (PBP2x, PDB ID: 5OIZ) as the target protein. Among eight tested ligands, streptomycin exhibited the highest binding affinity with a docking score of 64.76. In contrast, biogenic amines such as 2-phenylethylamine and tetradecylamine showed docking scores of 33.74 and 48.2, respectively. In the MurA protein (PDB ID: 3VCY), the biogenic amine ligand tetradecylamine exhibited a binding affinity comparable to that of certain reference drugs. Specifically, tetradecylamine achieved a GOLD score of 52.58, whereas ampicillin showed a higher score of 61.53. Notably, tetradecylamine demonstrated a higher binding affinity to the target protein compared with certain conventional antibiotics such as doxycycline and gentamycin.