Beta-defensin 124 (DEFB124)

Beta-defensin 124 (DEFB124) is a member of the beta-defensin family of antimicrobial peptides, characterized by six conserved cysteine residues forming three disulfide bonds, giving the molecule a stable tertiary structure[1][2][4][5]. These peptides are cationic and have broad-spectrum antibacterial activity, implicated in the first-line defense against microbial infection at epithelial surfaces[1][2][5][6]. DEFB124 is upregulated by bacterial stimuli (e.g., peptidoglycan via TLR induction) in human prostate epithelial cells, primarily through NF-κB activation, leading to increased release of pro-inflammatory cytokines and chemokines and enhanced chemotactic function[1]. Beta-defensin 124, like other defensins, disrupts the integrity of bacterial cell membranes leading to cell lysis, and can also drive innate immune responses by recruiting immune cells[1][2][5][6]. While the protein is well-characterized as part of host antimicrobial defense, its roles in specific human diseases and as a drug target remain investigational[1][5][6][8].

Other names

Beta-defensin 124DEFB124DEFB24DEFB-24Beta-defensin 24Defensin, beta 124defensin, beta 24

Not established for any marketed drugs. Beta-defensin 124 itself acts mainly by inserting into and disrupting microbial membranes