blp

Bombinin-Like Peptide (BLP-1) is an antimicrobial peptide derived from species of the genus Bombina.

Bombinin-like peptide 7, an antimicrobial peptide sourced from the Oriental fire-bellied toad (Bombina orientalis) [1], demonstrates bioactive properties.

Bombinin-like peptide 4, an antimicrobial peptide, originates from the skin secretions of the Asian toad (Bombina orientalis) [1].

Bombinin-like peptide 3, derived from the skin secretions of the Asian toad Bombina orientalis [1], is an antimicrobial peptide.

Bombinin-like peptide 2, an antimicrobial peptide sourced from the skin secretions of the Asian toad (Bombina orientalis), exhibits antimicrobial properties [1].

BLP-3, an endogenous peptide derived from X. laevis skin, exhibits antibacterial efficacy against N. meningitidis, N. gonorrhoeae, N. lactamica, and N. cinerea at a concentration of 20 µg/ml. Characterized by its ability to fold into an alpha-helix, BLP-3 penetrates and disrupts bacteriomimetic membranes, underlying its mechanism of action.

Diaminopimelic acid or DAPA is a lysine-like amino acid derivative that is a key component of the bacterial cell wall. DAPA is incorporated or integrated into peptidoglycan of gram negative bacteria and is the attachment point for Braun's lipoprotein (BLP or Murein Lipoprotein). BLP is found in gram-negative cell walls and is one of the most abundant membrane proteins. BLP is bound at its C-terminal end (a lysine) by a covalent bond to the peptidoglycan layer (specifically to diaminopimelic acid molecules) and is embedded in the outer membrane by its hydrophobic head (a cysteine with lipids attached). BLP tightly links the two layers and provides structural integrity to the bacterial outer membrane. Diaminopimelic acid can be found in human urine or feces due to the lysis or enzymatic breakdown of gram negative gut microbes.