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Nature Methods volume 18, pages 472–481 (2021) https://doi.org/10.1038/s41592-021-01117-3 Abstract Intrinsically disordered proteins, defying the traditional protein structure–function paradigm, are a challenge to study experimentally. Because a large part of our knowledge rests on computational predictions, it is crucial that their accuracy is high. The Critical Assessment of protein Intrinsic Disorder prediction (CAID) experiment was established as a community-based blind test to determine the state of the art in prediction of intrinsically disordered regions and the subset of residues involved in binding. A total of 43 methods were evaluated on a dataset of 646 proteins from DisProt. The best methods use deep learning techniques and notably outperform physicochemical metho

ChemMedChem. 2021 Apr 6.  doi: 10.1002/cmdc.202000992. Online ahead of print. Abstract NKT cells play an important role in the immune response and can be activated by glycolipids presented by CD1d protein. We present MCS-0208 an unprecedented arylthioether-phytoceramide able to induce potent iNKT cell activation, notably when tested in human iNKT cells. This arylsphingolipid analog has a simple phenyl group containing a single hydroxyl substituent as a surrogate of the sugar ring. The phenylthioether structure contrasts with a-galactosylceramide (1), the prototypical glycolipid used to induce iNKT cell stimulation, where the galactose 2'-OH and 3'-OH substituents are accepted as the minimal footprint and considered critical for NKT TCR recognition. A computational study suppo

https://doi.org/10.1016/j.jmb.2021.167059 Highlights In this review, we discuss the applications and limitations of AlphaFold in the field of protein aggregation.• AlphaFold might help in the computationally assisted optimization of the solubility of globular proteins with biomedical and industrial interest.• In amyloid diseases, the heterogeneous nature of aggregation intermediates and amyloid fibrils hinders the use of AlphaFold.• Residue covariation in functional amyloids suggests that AlphaFold could be trained to predict their structure, ultimately assisting in the design of amyloid-based nanomaterials. Abstract Protein aggregation is a widespread phenomenon with important implications in many scientific areas. Although amyloid formation is typi

ACS Appl. Mater. Interfaces 2021, 13, 13, 14875–14884 Publication Date: March 24, 2021 https://doi.org/10.1021/acsami.0c21996 Abstract Grafting biomolecules on nanostructures’ surfaces is an increasingly used strategy to target pathogenic cells, with both diagnostic and therapeutic applications. However, nanomaterials monofunctionalized by conjugating a single type of ligand find limited uses in pathologies/therapies that require two or more targets/receptors to be targeted and/or activated with a single molecular entity simultaneously. Therefore, multivalent nanomaterials for dual- or multitargeting are attracting significant interest. This study provides a proof of concept of such nanostructures. We have recently developed a modular methodology that allows obtaining amyloid

https://doi.org/10.1038/s42003-021-01930-8 Communications Biology volume 4, Article number: 414 (2021)  Abstract A disordered to β-sheet transition was thought to drive the functional switch of Q/N-rich prions, similar to pathogenic amyloids. However, recent evidence indicates a critical role for coiled-coil (CC) regions within yeast prion domains in amyloid formation. We show that many human prion-like domains (PrLDs) contain CC regions that overlap with polyQ tracts. Most of the proteins bearing these domains are transcriptional coactivators, including the Mediator complex subunit 15 (MED15) involved in bridging enhancers and promoters. We demonstrate that the human MED15-PrLD forms homodimers in solution sustained by CC interactions and th

In a study just published in “ACS Nano”, polymeric nanoparticles inspired by natural neuromelanin were used to encapsulate dopamine and to be administered via intranasal to reach the brain for Parkinson’s disease treatment. This work was coordinated by ICN2 Group Leader Dr Daniel Ruiz-Molina and Dr Julia Lorenzo, Group Leader at the Institute of Biotechnology and Biomedicine (IBB) of UAB, and developed in collaboration with the group led by Prof. Miquel Vila at VHIR. In a study just published in “ACS Nano”, polymeric nanoparticles inspired by natural neuromelanin were used to encapsulate dopamine and to be administered via intranasal to reach the brain for Parkinson’s disease treatment. This work was coordinated by ICN2 Group Leader Dr Daniel Ruiz-Molina and Dr Julia Lorenzo, Group