Cork is the bark of Quercus suber L., the cork oak tree. It is currently explored for different industrial applications, of which stoppers for the wine industry is the most representative and economically important. During the processing stages, up to 30% of cork is transformed into powder, which is mainly used for energy production by the industry. This underexploited natural resource stream constitutes an opportunity for the development of new products. In this review, we discuss cork as a potential source of chemicals for alternative applications. Special emphasis is dedicated to (a) suberin, (b) the extractives fraction, and (c) the use of cork in nontraditional applications. Suberin constitutes a source of long chain hydroxyacids which can serve as building blocks for new macromolecules and materials. The structure and composition are briefly addressed, while the advances in suberin depolymerization, extraction methodologies, and the proposed applications for this material are thoroughly discussed. The extractives fraction is constituted by lipophilic and phenolic compounds that present strong antioxidant and biological activities. The extractives composition and its properties are addressed. Finally, the use of cork for recently proposed applications, such as the preparation of activated carbons and as templates for the adsorption of pollutants, are also presented. This review is intended to summarize the current knowledge and technological development state and to push for the progress toward an integrated cork economy.

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The isomers vescalagin and castalagin protect SH-SY5Y cells from Aβ42-mediated death. This is achieved better by vescalagin due to the spatial organization of its OH group at the C1 position of the glycosidic chain, improving its capacity to remodel the secondary structure of toxic Aβ42 oligomers.Alzheimer´s Disease (AD) is the most common cause of dementia, characterized by cognitive impairment and memory loss. 1 The most characteristic hallmarks of AD are the presence of intracellular neurofibrillary tangles (of hyperphosphorylated Tau protein) in the affected neurons, and the deposition of extracellular plaques of amyloid-β (Aβ) peptides in the hippocampus and entorhinal cortex. In the case of the amyloid deposits, they are usually composed of Aβ of different lengths, i.e. between 38 and 43 amino acids. Aβ is produced by neurons during the sequential proteolytic cleavage of amyloid precursor protein (APP). 2 Aβ (1-42) (Aβ42) is the less abundant species, however, it is the most amyloidogenic due to its higher propensity to self-assemble into supramolecular aggregates, which has been linked with the predominance of hydrophobic amino acid residues at its C-terminus. 3 Aβ42 can exist in several forms, e.g. monomers, oligomers or fibrils, however, its oligomeric species are reported to be the most cytotoxic 4 . They comprise different levels of association, such as dimers, trimers and higher hierarchical assemblies that lead to the formation of