NATURAL PROTEINS AND THEIR APPLICATION POTENTIAL: A CASE STUDY OF SILK PROTEINS

Natural proteins represent a diverse class of biomacromolecules with exceptional properties that have inspired numerous technological applications. Among these, silk proteins produced by silkworms (Bombyx mori) and spiders stand out as remarkable examples of natural materials combining mechanical strength, biocompatibility, and biodegradability. This study examines the structural characteristics, physicochemical properties, and application potential of silk proteins, particularly silk fibroin and sericin. We analyzed the hierarchical structure of silk proteins from primary amino acid sequences to supramolecular assemblies, investigating how these structures determine their unique mechanical and biological properties. Our comprehensive review encompasses applications in tissue engineering, drug delivery systems, wound healing, cosmetics, textiles, and optical devices. The analysis reveals that silk proteins exhibit tensile strength comparable to synthetic polymers (up to 1.3 GPa for spider silk), excellent biocompatibility with minimal immunogenic response, controllable biodegradation rates, and versatile processing capabilities into various formats including films, hydrogels, scaffolds, and nanoparticles. Recent advances in recombinant protein technology and materials processing have expanded the application scope of silk proteins beyond traditional uses. This review synthesizes current knowledge on silk protein structure-property relationships and discusses emerging applications in regenerative medicine, sustainable materials, and advanced biotechnology.