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10.1021/acschembio.7b00045 http://scihub22266oqcxt.onion/10.1021/acschembio.7b00045 C5724361!5724361 !28240851     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28240851 &cmd=llinks): Failed to open stream: HTTP request failed! 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Ion Mobility-Mass Spectrometry Reveals a Dipeptide That Acts as a Molecular Chaperone for Amyloid ? |pdf=|usr=}}{{28240851 }} gab.com Text Ion Mobility-Mass Spectrometry Reveals a Dipeptide That Acts as a Molecular Chaperone for Amyloid JO: ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=28240851 #FOAvip Previously, we discovered and structurally characterized a complex between amyloid ? 1-40 and the neuropeptide leucine enkephalin. This work identified leucine enkephalin as a potentially useful starting point for the discovery of peptide-related biotherapeutics for Alzheimer's disease. In order to better understand such complexes that are formed in vitro, we describe here the analysis of a series of site-directed amino acid substitution variants of both peptides, covering the leucine enkephalin sequence in its entirety and a large number of selected residues of amyloid ? 1-40 (residues: D1, E3, F4, R5, H6, Y10, E11, H13, H14, Q15, K16, E22, K28, and V40). Ion mobility-mass spectrometry measurements and molecular dynamics simulations reveal that the hydrophobic C-terminus of leucine enkephalin (Phe-Leu, FL) is crucial for the formation of peptide complexes. As such, we explore here the interaction of the dipeptide FL with both wildtype and variant forms of amyloid ? in order to structurally characterize the complexes formed. We find that FL binds preferentially to amyloid ? oligomers and attaches to amyloid ? within the region between its N-terminus and its hydrophobic core, most specifically at residues Y10 and Q15. We further show that FL is able to prevent fibril formation. Twit Text FOAVip Ion Mobility-Mass Spectrometry Reveals a Dipeptide That Acts as a Molecular Chaperone for Amyloid ????ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=28240851 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28240851 #FOAvip English Wikipedia <ref>{{Cite pmid|28240851 }}</ref> Ion Mobility-Mass Spectrometry Reveals a Dipeptide That Acts as a Molecular Chaperone for Amyloid ? #MMPMID28240851 Soper-Hopper MT ; Eschweiler JD ; Ruotolo BT ACS Chem Biol 2017[Apr]; 12 (4 ): 1113-1120 PMID28240851 show ga Previously, we discovered and structurally characterized a complex between amyloid ? 1-40 and the neuropeptide leucine enkephalin. This work identified leucine enkephalin as a potentially useful starting point for the discovery of peptide-related biotherapeutics for Alzheimer's disease. In order to better understand such complexes that are formed in vitro, we describe here the analysis of a series of site-directed amino acid substitution variants of both peptides, covering the leucine enkephalin sequence in its entirety and a large number of selected residues of amyloid ? 1-40 (residues: D1, E3, F4, R5, H6, Y10, E11, H13, H14, Q15, K16, E22, K28, and V40). Ion mobility-mass spectrometry measurements and molecular dynamics simulations reveal that the hydrophobic C-terminus of leucine enkephalin (Phe-Leu, FL) is crucial for the formation of peptide complexes. As such, we explore here the interaction of the dipeptide FL with both wildtype and variant forms of amyloid ? in order to structurally characterize the complexes formed. We find that FL binds preferentially to amyloid ? oligomers and attaches to amyloid ? within the region between its N-terminus and its hydrophobic core, most specifically at residues Y10 and Q15. We further show that FL is able to prevent fibril formation. |Amino Acid Substitution [MESH] |Amyloid beta-Peptides/*chemistry [MESH] |Cluster Analysis [MESH] |Dipeptides/*chemistry [MESH] |Mass Spectrometry/*methods [MESH] |Microscopy, Electron, Transmission [MESH] |Molecular Chaperones/*chemistry [MESH] |Molecular Dynamics Simulation [MESH] |Peptide Fragments/*chemistry [MESH]Ion Mobility-Mass Spectrometry Reveals a Dipeptide That Acts as a Mole(epmc).pdf DeepDyve Pubget Overpricing