ArticleApplied microbiology and biotechnology2024
Expression and purification of epinecidin-1 variant (Ac-Var-1) by acid cleavage.
Article in Applied microbiology and biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- Anticancer effects of alpha-helical peptide epinecidin-1 and its variants in combination with doxorubicin.Medical oncology (Northwood, London, England) · 2026Article
- Unlocking Antimicrobial Peptides from Marine Invertebrates: A Comprehensive Review of Antimicrobial Discovery.Antibiotics (Basel, Switzerland) · 2025Review
- Unlocking the power of antimicrobial peptides: advances in production, optimization, and therapeutics.Frontiers in cellular and infection microbiology · 2025Review
- A Step-by-Step Guide for Biosynthesis of Recombinant Fusion Antimicrobial Peptide and Release of the Active Peptide from Its Fusion Partner by Formic Acid Cleavage.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Antibiofilm Activity of Epinecidin-1 and Its Variants Against Drug-ResistantInfectious disease reports · 2024Article
- Fusion Partner Facilitates Expression of Cell-Penetrating Peptide L2 inAntibiotics (Basel, Switzerland) · 2024Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
The demand for massive quantities of therapeutic active antimicrobial peptides (AMPs) is high due to their potential as alternatives to antibiotics. However, each antimicrobial peptide has unique properties, necessitating distinct synthesis and purification strategies for their large-scale production. In this study, we bio-synthesized and purified a functional enhanced variant of the AMP epinecidin-1, known as Ac-Var-1 (acid-cleavable variant-1). To generate the active peptide, we cloned the gene for Ac-Var-1 with acid-cleavable site (aspartic acid-proline) into the pET-32a expression vector, purified the fusion protein by His tag enrichment chromatography, and performed acid cleavage to release the active Ac-Var-1 peptide. After acid cleavage, the active Ac-Var-1 was purified and characterized by SDS-PAGE and mass spectrometry. The results from both techniques provided confirmation of the intactness of the purified Ac-Var-1. The Ac-Var-1 inhibited the growth of pathogenic Escherichia coli and Staphylococcus aureus. KEY POINTS : • Epinecidin-1 is a well-known antimicrobial peptide having multipotential bioactivities. • Epinecidin-1 variant is developed via the site-directed mutagenesis method to improve its structural stability and bioactivity. • AC-Var-1 development is an economical and easy method to remove peptide from tag protein.
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Identifiers
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.