Beta-defensin 106

Also known as: Beta-defensin 6, Defensin, beta 106, DEFB106A, DEFB106B, Q8N104

Beta-defensin 106 (DEFB106A/B) is an antimicrobial peptide belonging to the beta-defensin family, characterized by a conserved six-cysteine motif forming three disulfide bridges. Its primary mechanism of action involves direct antibacterial activity, likely through disruption of microbial membrane integrity. Additionally, it functions as a ligand for the C-C chemokine receptor CCR2, suggesting a role in chemotaxis and immune modulation by recruiting leukocytes to sites of infection or inflammation. Currently classified as experimental, no peer-reviewed research findings are indexed in PubMed, indicating a lack of published in vitro, in vivo, or clinical studies. The dual antimicrobial and chemokine receptor-binding properties imply potential relevance in host defense and inflammatory regulation, but the absence of data precludes assessment of efficacy, safety, or therapeutic applications. Clinical relevance remains undefined due to the experimental status and absence of published evidence. Further investigation is required to characterize its biological functions and potential utility in infectious or inflammatory diseases. For research purposes only — not medical advice.

Key data

Mechanism of action

Has antibacterial activity (PubMed:12600824). Acts as a ligand for C-C chemokine receptor CCR2 (PubMed:23938203)

Frequently asked questions

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