Beta-defensin 107

Also known as: Beta-defensin 7, Defensin, beta 107, DEFB107A, DEFB107B, Q8IZN7

Beta-defensin 107 (DEFB107A/B) is an antimicrobial peptide belonging to the beta-defensin family, characterized by a conserved beta-sheet structure stabilized by three disulfide bridges. Its primary mechanism of action involves disruption of bacterial cell membranes through electrostatic interactions with negatively charged microbial lipid bilayers, leading to membrane permeabilization and cell lysis. This activity is typical of defensins, which also exhibit immunomodulatory properties, though specific signaling pathways for DEFB107 remain uncharacterized due to limited experimental data. As of current literature, no peer-reviewed research findings specific to DEFB107 have been published (PubMed references: 0). The peptide is classified as experimental, with no validated in vivo or in vitro studies confirming its antibacterial spectrum, potency, or safety profile. Its functional annotation is inferred from homology to other beta-defensins, such as DEFB103 and DEFB104, which demonstrate broad-spectrum activity against Gram-positive and Gram-negative bacteria. Clinical relevance is speculative at this stage. Beta-defensins are generally considered potential candidates for novel antimicrobial therapies, particularly in the context of antibiotic resistance. However, without experimental validation, DEFB107 cannot be recommended for therapeutic development or diagnostic use. For research purposes only — not medical advice.

Key data

Mechanism of action

Has antibacterial activity

Frequently asked questions

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