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LL-37

Cathelicidin, hCAP-18, FALL-39, CAP-18

Quick Stats
Studies 2230
Trials 95
2013 pubmed 27 citations

Immobilization of antimicrobial peptide IG-25 onto fluoropolymers via fluorous interactions and click chemistry.

Santos. Catherine M CM; Kumar. Amit A; Kolar. Satya S SS; Contreras-Caceres. Rafael R; McDermott. Alison A; Cai. Chengzhi C

Key Findings

  • Fluorous‑tagged coating creates a clickable surface for peptides
  • IG‑25 can be covalently attached via copper‑catalyzed click reaction
  • N‑terminal click‑linked IG‑25 shows stronger antibacterial activity than randomly attached peptide

Practical Outcomes

  • For most biohackers this work isn’t directly usable; it’s mainly useful for developers of antimicrobial coatings like contact lenses, not for personal health protocols.

Summary

The paper describes a lab technique for sticking an antimicrobial peptide called IG‑25 onto plastic surfaces using special fluorous tags and click chemistry, which makes the surface better at killing eye‑infection bacteria.

Abstract

We report a practical method for biofunctionalization of fluoropolymers based on noncovalent, fluorous interactions and click chemistry that allows incorporation of biomolecules under physiological solutions. We demonstrate the method by immobilization of an antimicrobial peptide (AMP) on fluorous thin films and fluorosilicone contact lens. The fluorous surfaces were dip-coated with fluorous-tagged oligo(ethylene) chain terminated with a reactive group, such as an alkynyl group. This simple step generates a "clickable" surface. The noncovalent fluorous interaction was strong enough to allow subsequent covalent attachment of IG-25, a truncated version of the most extensively studied human AMP LL-37. The attachment was through copper-catalyzed click reaction between the alkynyl group on the surface and the azido-OEG tag at the N-terminus of IG-25. In comparison to surfaces presenting IG-25 randomly bound via carbodiimide chemistry, the surfaces presenting IG-25 tethering to the surface at the N-terminus via click chemistry displayed higher antibacterial activities against an ocular pathogen Pseudomonas aeruginosa (strain PA-O1).

Study Information

Provider

pubmed

Year

2013

Date

2013-12-04T00:00:00.000Z

DOI

10.1021/am404591n

Citations

27

References

36