Oral Elastin peptide - (Derived from the elastic connective tissue of the fish bulbus arteriosus)

Abstract Elastin peptide are emerging as a promising class of bioactive compounds in nutricosmetic research. The fish bulbus arteriosus, a specialized elastic organ responsible for hemodynamic buffering, represents a unique and underexplored source of elastin-rich connective tissue. Through targeted enzymatic hydrolysis, elastin proteins from this tissue can be converted into low-molecular-weight peptides (0.5-2 kDa), which exhibit superior intestinal absorption via PepT1 transporters. These peptides retain elastin-specific cross-linking amino acids, desmosine and isodesmosine, conferring high biochemical homology with human dermal, vascular, and pulmonary elastic fibers. Mechanistically, oral elastin peptides provide structural substrates for fibroblast-mediated elastic fiber regeneration, support the collagen-elastin dual-network for dermal tensile strength and resilience, and exert anti-oxidative and anti-proteolytic activities that protect the extracellular matrix (ECM) from premature degradation. Furthermore, their vascular homology suggests potential benefits for arterial compliance and systemic elasticity maintenance. When combined with collagen peptides, elastin peptides enable synergistic remodeling of the ECM, addressing both tensile and elastic components of skin aging. Collectively, elastin peptides derived from fish bulbus arteriosus offer a novel precision-nutrition strategy for mitigating fine lines, restoring dermal elasticity, and delaying structural skin aging, while also contributing to vascular and systemic tissue health.