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10.1371/journal.pone.0135292 http://scihub22266oqcxt.onion/10.1371/journal.pone.0135292 C4556714!4556714 !26327208     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26327208 &cmd=llinks): Failed to open stream: HTTP request failed! 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Drug Development in Conformational Diseases: A Novel Family of Chemical Chaperones that Bind and Stabilise Several Polymorphic Amyloid Structures |pdf=|usr=}}{{26327208 }} gab.com Text Drug Development in Conformational Diseases: A Novel Family of Chemical Chaperones that Bind and Stabilise Several Polymorphic Amyloid Structures JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=26327208 #FOAvip The increasing prevalence of conformational diseases, including Alzheimer's disease, type 2 Diabetes Mellitus and Cancer, poses a global challenge at many different levels. It has devastating effects on the sufferers as well as a tremendous economic impact on families and the health system. In this work, we apply a cross-functional approach that combines ideas, concepts and technologies from several disciplines in order to study, in silico and in vitro, the role of a novel chemical chaperones family (NCHCHF) in processes of protein aggregation in conformational diseases. Given that Serum Albumin (SA) is the most abundant protein in the blood of mammals, and Bovine Serum Albumin (BSA) is an off-the-shelf protein available in most labs around the world, we compared the ligandability of BSA:NCHCHF with the interaction sites in the Human Islet Amyloid Polypeptide (hIAPP):NCHCHF, and in the amyloid pharmacophore fragments (A?17-42 and A?16-21):NCHCHF. We posit that the merging of this interaction sites is a meta-structure of pharmacophore which allows the development of chaperones that can prevent protein aggregation at various states from: stabilizing the native state to destabilizing oligomeric state and protofilament. Furthermore to stabilize fibrillar structures, thus decreasing the amount of toxic oligomers in solution, as is the case with the NCHCHF. The paper demonstrates how a set of NCHCHF can be used for studying and potentially treating the various physiopathological stages of a conformational disease. For instance, when dealing with an acute phase of cytotoxicity, what is needed is the recruitment of cytotoxic oligomers, thus chaperone F, which accelerates fiber formation, would be very useful; whereas in a chronic stage it is better to have chaperones A, B, C, and D, which stabilize the native and fibril structures halting self-catalysis and the creation of cytotoxic oligomers as a consequence of fiber formation. Furthermore, all the chaperones are able to protect and recondition the cerebellar granule cells (CGC) from the cytotoxicity produced by the hIAPP20-29 fragment or by a low potassium medium, regardless of their capacity for accelerating or inhibiting in vitro formation of fibers. In vivo animal experiments are required to study the impact of chemical chaperones in cognitive and metabolic syndromes. Twit Text FOAVip Drug Development in Conformational Diseases: A Novel Family of Chemical Chaperones that Bind and Stabilise Several Polymorphic Amyloid Structures ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=26327208 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26327208 #FOAvip English Wikipedia <ref>{{Cite pmid|26327208 }}</ref> Drug Development in Conformational Diseases: A Novel Family of Chemical Chaperones that Bind and Stabilise Several Polymorphic Amyloid Structures #MMPMID26327208 Sablón-Carrazana M ; Fernández I ; Bencomo A ; Lara-Martínez R ; Rivera-Marrero S ; Domínguez G ; Pérez-Perera R ; Jiménez-García LF ; Altamirano-Bustamante NF ; Diaz-Delgado M ; Vedrenne F ; Rivillas-Acevedo L ; Pasten-Hidalgo K ; Segura-Valdez Mde L ; Islas-Andrade S ; Garrido-Magaña E ; Perera-Pintado A ; Prats-Capote A ; Rodríguez-Tanty C ; Altamirano-Bustamante MM PLoS One 2015[]; 10 (9 ): e0135292 PMID26327208 show ga The increasing prevalence of conformational diseases, including Alzheimer's disease, type 2 Diabetes Mellitus and Cancer, poses a global challenge at many different levels. It has devastating effects on the sufferers as well as a tremendous economic impact on families and the health system. In this work, we apply a cross-functional approach that combines ideas, concepts and technologies from several disciplines in order to study, in silico and in vitro, the role of a novel chemical chaperones family (NCHCHF) in processes of protein aggregation in conformational diseases. Given that Serum Albumin (SA) is the most abundant protein in the blood of mammals, and Bovine Serum Albumin (BSA) is an off-the-shelf protein available in most labs around the world, we compared the ligandability of BSA:NCHCHF with the interaction sites in the Human Islet Amyloid Polypeptide (hIAPP):NCHCHF, and in the amyloid pharmacophore fragments (A?17-42 and A?16-21):NCHCHF. We posit that the merging of this interaction sites is a meta-structure of pharmacophore which allows the development of chaperones that can prevent protein aggregation at various states from: stabilizing the native state to destabilizing oligomeric state and protofilament. Furthermore to stabilize fibrillar structures, thus decreasing the amount of toxic oligomers in solution, as is the case with the NCHCHF. The paper demonstrates how a set of NCHCHF can be used for studying and potentially treating the various physiopathological stages of a conformational disease. For instance, when dealing with an acute phase of cytotoxicity, what is needed is the recruitment of cytotoxic oligomers, thus chaperone F, which accelerates fiber formation, would be very useful; whereas in a chronic stage it is better to have chaperones A, B, C, and D, which stabilize the native and fibril structures halting self-catalysis and the creation of cytotoxic oligomers as a consequence of fiber formation. Furthermore, all the chaperones are able to protect and recondition the cerebellar granule cells (CGC) from the cytotoxicity produced by the hIAPP20-29 fragment or by a low potassium medium, regardless of their capacity for accelerating or inhibiting in vitro formation of fibers. In vivo animal experiments are required to study the impact of chemical chaperones in cognitive and metabolic syndromes. |Amyloid beta-Peptides/drug effects/metabolism [MESH] |Amyloidogenic Proteins/drug effects/*metabolism [MESH] |Animals [MESH] |Binding Sites [MESH] |Circular Dichroism [MESH] |Computer Simulation [MESH] |Drug Discovery/methods [MESH] |Humans [MESH] |In Vitro Techniques [MESH] |Microscopy, Electron, Transmission [MESH] |Molecular Chaperones/*metabolism/pharmacology [MESH] |Molecular Docking Simulation [MESH] |Peptide Fragments/drug effects/metabolism [MESH] |Protein Aggregation, Pathological/drug therapy [MESH] |Serum Albumin, Bovine/metabolism/pharmacology [MESH]Drug Development in Conformational Diseases: A Novel Family of Chemica(epmc).pdf DeepDyve Pubget Overpricing