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Scleroproteins are proteins that form long rod-like filaments, which generally serve as a storage unit or in a structural capacity, as in collagen. Because of the filamentous nature of scleroprotein assemblies, they are insoluble in aqueous solutions and prone to aggregation.
Metallic surfaces are often coated with corrosion inhibitors to prevent damage but these are typically toxic to the environment. Here, a recombinant adhesive cement protein from barnacles is shown to effectively protect steel against corrosion under marine environment conditions.
Stiffness in the extracellular matrix is thought to contribute to pathological cutaneous fibrosis. Here, the authors identify the elastic fibre protein Fibulin-5 as a link and potential therapeutic target mediating the transition of cutaneous stiffening to fibrosis.
Cells package proteins into vesicles for secretion to the extracellular milieu. A study has now identified an enzyme that modifies the packaging machinery to encapsulate unusually large proteins, such as collagen. See Article p.495
