129 research outputs found
Sericin Protein: Structure, Properties, and Applications
No full textSilk sericin, the glue protein binding fibroin fibers together, is present in the Bombyx mori silkworms’ cocoons. In recent years, sericin has gained attention for its wide range of properties and possible opportunities for various applications, as evidenced by the meta-analysis conducted in this review. Sericin extraction methods have evolved over the years to become more efficient and environmentally friendly, preserving its structure. Due to its biocompatibility, biodegradability, anti-inflammatory, antibacterial, antioxidant, UV-protective, anti-tyrosinase, anti-aging, and anti-cancer properties, sericin is increasingly used in biomedical fields like drug delivery, tissue engineering, and serum-free cell culture media. Beyond healthcare, sericin shows promise in industries such as textiles, cosmetics, and food packaging. This review aims to highlight recent advancements in sericin extraction, research, and applications, while also summarizing key findings from earlier studies
Design of a Collagen/Silk Mechano-Compatible Composite Scaffold for the Vascular Tissue Engineering: Focus on Compliance
No full textAtomic Force and Confocal Microscopic Studies of Collagen-Cell-based Scaffolds for Vascular Tissue Engineering
No full textEstimation of the binding force of the collagen molecule-decorin core protein complex in collagen fibril
No full textDecorin belongs to the small leucine proteoglycans family and is considered to play an important role in extracellular matrix organization. Experimental studies suggest that decorin is required for the assembly of collagen fibrils, as well as for the development of proper tissue mechanical properties. In tendons, decorins tie adjoining collagen fibrils together and probably guarantee the mechanical coupling of fibrils. The decorin molecule consists of one core protein and one glycosaminoglycan chain covalently linked to a serine residue of the core protein. Several studies have indicated that each core protein binds to the surface of collagen fibrils every 67 nm, by interacting non-covalently to one collagen molecule of the fibril surface, while the decorin glycosaminoglycans extend from the core protein to connect to another decorin core protein laying on adjacent fibril surface. The present paper investigates the complex composed of one decorin core protein and one collagen molecule in order to obtain their binding force. For this purpose, molecular models of collagen molecules type I and decorin core protein were developed and their interaction energies were evaluated by means of the molecular mechanics approach. Results show that the complex is characterized by a maximum binding force of about 12.4 x 10(3) nN and a binding stiffness of 8.33 x 10(-8) N/nm; the attained binding force is greater than the glycosaminoglycan chain's ultimate strength, thus indicating that overloads are likely to damage the collagen fibre's mechanical integrity by disrupting the glycosaminoglycan chains rather than by causing decorin core protein detachment from the collagen fibril
L'ETICA NELLA FINANZA E L'UTILIZZO DEGLI STRUMENTI FINANZIARI DERIVATI: PROFILI ECONOMICI, GIURIDICI E PSICOLOGICI
No full textPARTENDO DA UNA ANALISI STORICA DELL'UTILIZZO DEGLI STRUMENTI FINANZIARI DERIVATI L'AUTORE PASSA, POI, AD UN'ANALISI ECONOMICA, GIURIDICA E PSICOLOGICA AFFINCHE' SI POSSA REALIZZARE CORRETTAMENTE LA LORO APPLICAZIONE.FROM AN HISTORICAL ANALYSIS OF THE USE OF DERIVATIVE FINANCIAL INSTRUMENTS THE AUTHOR PASS , THEN , TO ECONOMIC ANALYSIS , LEGAL AND PSYCHOLOGICAL ORDER ' PROPERLY MAY MAKE THEIR APPLICATION
Single molecule effects of osteogenesis imperfecta mutations in tropocollagen protein domains.
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Response to letter to the editor: On the calculation of the binding force between decorin and collagen
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