ArticleFuture science OA2022
Optimized peptide extraction method for analysis of antimicrobial peptide Kn2-7/dKn2-7 stability in human serum by LC-MS.
Article in Future science OA, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 8 citations in OpenAlex.
- Rationally Engineered D-Amino Acid Peptide DT7-3 Combats Multidrug-ResistantMicroorganisms · 2026Article
- Mechanistic Study of Antimicrobial Effectiveness of Cyclic Amphipathic Peptide [RAntibiotics (Basel, Switzerland) · 2024Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
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Abstract
Aim: To develop an extraction protocol and determine stability for antimicrobial peptide (AMP) Kn2-7 and its d-enantiomer dKn2-7 in human serum. Materials & methods: We compared use of ethanol, acetonitrile, RapiGest SF Surfactant and 1% formic acid in ethanol for AMP recovery from serum prior to liquid chromatography-mass spectrometry quantification. Results: Precipitation of samples with 1% formic acid in ethanol caused the least amount of AMP loss during extraction from serum. Time-course experiments revealed dKn2-7 was significantly more stable than Kn2-7 in 25% serum, with 78.5% of dKn2-7 and only 1.0% of Kn2-7 remaining after 24 h at 37°C. Conclusion: The optimized method significantly increased peptide recovery and allowed more accurate and consistent quantification of Kn2-7 and dKn2-7 serum stability.
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