Indolicidin
Overview
Indolicidin is a 13-amino acid antimicrobial peptide derived from bovine neutrophils, characterized by a high tryptophan content (five residues). It exerts antimicrobial activity through multiple mechanisms, including membrane disruption, DNA binding, and inhibition of intracellular processes. The peptide adopts an extended wedge-shaped conformation that facilitates insertion into lipid bilayers. Indolicidin demonstrates activity against bacteria, fungi, and certain protozoa, though its clinical development has been limited by cytotoxicity.
Key Research Findings
Preclinical studies in vitro and in murine infection models have demonstrated broad-spectrum antimicrobial activity, including against methicillin-resistant Staphylococcus aureus and Candida species. Structural analogs with reduced mammalian cell toxicity have been synthesized and tested in rodent wound infection models with promising results. No clinical trials in humans have been reported to date, and the peptide remains in the research phase.
Topical
Research Phase
Interested in Indolicidin?
Find a verified provider experienced with Indolicidin protocols in your area. All providers are credentialed and use compliant sourcing.
Find a Indolicidin ProviderRelated Peptides
Enfuvirtide (Fuzeon)
FDA ApprovedA 36-amino acid synthetic peptide that inhibits HIV-1 entry into CD4+ T-cells by blocking the gp41-mediated membrane fusion step. Enfuvirtide binds to the first heptad repeat (HR1) region of gp41, preventing the conformational change required for viral-cell membrane fusion. It is the first and only FDA-approved fusion inhibitor and is active against HIV-1 strains resistant to other antiretroviral drug classes.
Magainin 2
Research PhaseMagainin 2 is a 23-amino acid antimicrobial peptide originally isolated from the skin of the African clawed frog Xenopus laevis. It exerts broad-spectrum antimicrobial activity through membrane disruption, forming pores in bacterial membranes while exhibiting relative selectivity over mammalian cells. Magainin 2 belongs to the alpha-helical cationic antimicrobial peptide family and has served as a template for numerous synthetic analogs. Its mechanism of action, which is distinct from conventional antibiotics, offers potential against multidrug-resistant pathogens.
Pexiganan (MSI-78)
In Clinical TrialsPexiganan is a 22-amino acid synthetic analog of magainin 2 designed to enhance antimicrobial potency and proteolytic stability. It disrupts bacterial membranes through electrostatic interaction and pore formation, demonstrating broad-spectrum activity against gram-positive and gram-negative organisms, including methicillin-resistant Staphylococcus aureus. Pexiganan was developed as a topical agent for infected diabetic foot ulcers, leveraging its rapid bactericidal action and low resistance potential. Structural modifications from the parent magainin sequence improve its pharmacological profile for clinical use.
Omiganan
In Clinical TrialsOmiganan is a synthetic 12-amino acid cationic antimicrobial peptide derived from indolicidin, a naturally occurring peptide from bovine neutrophils. It acts by disrupting microbial membranes and demonstrates activity against bacteria, fungi, and some viruses. Omiganan was developed as a topical agent to prevent catheter-related bloodstream infections through its broad-spectrum antimicrobial properties. Its small size and potent activity made it a candidate for preventing biofilm formation on medical devices.