Bioactive peptide (BAP)

Bioactive peptides (BAPs) are short sequences of amino acids, generally ranging from 2 to 20 residues, that possess specific biological activities and provide physiological benefits to the body [1]. These molecules are typically inactive when encrypted within a parent protein and must be released through enzymatic hydrolysis, fermentation, or food processing to exert their effects [2]. Once active, they function in diverse roles such as hormones, neurotransmitters, and antimicrobial agents by interacting with high-affinity targets like G protein-coupled receptors or enzymes [3]. For example, antihypertensive peptides inhibit the angiotensin-converting enzyme to regulate blood pressure, while other peptides like insulin or GLP-1 analogs are critical in metabolic regulation [4][5]. Despite their high potency and specificity, bioactive peptides often face challenges in drug development due to rapid degradation by endogenous proteases and low permeability across biological membranes [1]. Consequently, the term "Bioactive peptides" refers to a heterogeneous functional class of molecules rather than a single, specific therapeutic target [3].

Other names

Functional peptidesPhysiologically active peptidesBiologically active peptidesBiopeptidesNutraceutical peptides

Bioactive peptides typically exert their effects by acting as ligands that bind to specific cell-surface receptors, such as G protein-coupled receptors (GPCRs), or by inhibiting specific enzymes like angiotensin-converting enzyme (ACE). Some bioactive peptides, such as antimicrobial peptides, act through direct physical disruption of microbial cell membranes or by entering cells to interfere with intracellular processes [1][3].