Defensin beta 136

Also known as: Beta-defensin 136, DEFB137, DEFB136, Q30KP8

**Mechanism of Action** Defensin beta 136 (DEFB136) is a member of the beta-defensin family of host defense peptides, characterized by a conserved six-cysteine motif forming three disulfide bridges. As a cationic antimicrobial peptide, it is predicted to disrupt microbial membranes via electrostatic interactions with negatively charged phospholipids, leading to pore formation, membrane permeabilization, and cell lysis. Its activity spectrum includes both Gram-positive and Gram-negative bacteria, as well as fungi, though specific molecular targets remain uncharacterized due to limited experimental data. **Key Research Findings** No peer-reviewed publications indexed in PubMed currently exist for DEFB136. The peptide is classified as "experimental" based on genomic and transcriptomic evidence, with its sequence (UniProt Q30KP8) inferred from computational predictions and homology to other beta-defensins. Functional studies are absent, and its expression patterns, regulation, or in vivo roles have not been empirically validated. The lack of direct research limits mechanistic understanding beyond general beta-defensin properties. **Clinical Relevance** DEFB136 has no established clinical applications. As an experimental peptide, its therapeutic potential—such as use in antimicrobial-resistant infections or immune modulation—remains speculative. Without preclinical or clinical data, its safety, efficacy, and pharmacokinetics are unknown. Further investigation is required to determine if DEFB136 contributes to innate immunity or could be developed as a novel antimicrobial agent. For research purposes only — not medical advice.

Key data

Mechanism of action

Host defense peptide that exhibits antibacterial and antifungal activity (PubMed:34481960). Exhibits antimicrobial activity against E.coli, S.aureus and C.albicans (in vitro) (PubMed:34481960). Has high lipopolysaccharide (LPS)-binding affinity, and may thereby be involved in immunoregulation through LPS neutralization (PubMed:34481960)

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