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10.1371/journal.pone.0199541 http://scihub22266oqcxt.onion/10.1371/journal.pone.0199541 C6023135!6023135!29953467     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 278.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 278.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 278.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 278.79999999999995 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       PLoS+One 2018 ; 13 (6): ä Nephropedia Template TP {{tp|p=29953467|t=2018. The role of phenolic OH groups of flavonoid compounds with H-bond formation ability to suppress amyloid mature fibrils by destabilizing ?-sheet conformation of monomeric A?17-42 |pdf=|usr=}}{{29953467}} gab.com Text The role of phenolic OH groups of flavonoid compounds with H-bond formation ability to suppress amyloid mature fibrils by destabilizing -sheet conformation of monomeric A 17-42 JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=29953467 #FOAvip Alzheimer?s disease (AD) is a kind of brain disease that arises due to the aggregation and fibrillation of amyloid ?-peptides (A?). The peptide A?17?42 forms U-shape protofilaments of amyloid mature fibrils by cross-? strands, detected in brain cells of individuals with AD. Targeting the structure of A?17?42 and destabilizing its ?-strands by natural compounds could be effective in the treatment of AD patients. Therefore, the interaction features of monomeric U-shape A?17?42 with natural flavonoids including myricetin, morin and flavone at different mole ratios were comprehensively studied to recognize the mechanism of A? monomer instability using molecular dynamics (MD) simulations. We found that all flavonoids have tendency to interact and destabilize A? peptide structure with mole ratio-dependent effects. The interaction free energies of myricetin (with 6 OHs) and morin (with 5 OHs) were more negative compared to flavone, although the total binding energies of all flavonoids are favorable and negative. Myricetin, morin and flavone penetrated into the core of the A?17?42 and formed self-clusters of A?17-42-flavonoid complexes. Analysis of A?17-42-flavonoids interactions identified that the hydrophobic interactions related to SASA-dependent energy are weak in all complexes. However, the intermolecular H-bonds are a main binding factor for shifting U-shape rod-like state of A?17?42 to globular-like disordered state. Myricetin and morin polyphenols form H-bonds with both peptide?s carbonyl and amine groups whereas flavone makes H-bonds only with amine substitution. As a result, polyphenols are more efficient in destabilizing ?-sheet structures of peptide. Accordingly, the natural polyphenolic flavonoids are useful in forming stable A?17-42-flavonoid clusters to inhibit A?17?42 aggregation and these compounds could be an effective candidate for therapeutically targeting U-shape protofilaments? monomer in amyloid mature fibrils. Twit Text FOAVip The role of phenolic OH groups of flavonoid compounds with H-bond formation ability to suppress amyloid mature fibrils by destabilizing -sheet conformation of monomeric A 17-42 ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=29953467 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29953467 #FOAvip English Wikipedia <ref>{{Cite pmid|29953467}}</ref> The role of phenolic OH groups of flavonoid compounds with H-bond formation ability to suppress amyloid mature fibrils by destabilizing ?-sheet conformation of monomeric A?17-42 #MMPMID29953467 Andarzi Gargari S; Barzegar A; Tarinejad A PLoS One 2018[]; 13 (6): ä PMID29953467show ga Alzheimer?s disease (AD) is a kind of brain disease that arises due to the aggregation and fibrillation of amyloid ?-peptides (A?). The peptide A?17?42 forms U-shape protofilaments of amyloid mature fibrils by cross-? strands, detected in brain cells of individuals with AD. Targeting the structure of A?17?42 and destabilizing its ?-strands by natural compounds could be effective in the treatment of AD patients. Therefore, the interaction features of monomeric U-shape A?17?42 with natural flavonoids including myricetin, morin and flavone at different mole ratios were comprehensively studied to recognize the mechanism of A? monomer instability using molecular dynamics (MD) simulations. We found that all flavonoids have tendency to interact and destabilize A? peptide structure with mole ratio-dependent effects. The interaction free energies of myricetin (with 6 OHs) and morin (with 5 OHs) were more negative compared to flavone, although the total binding energies of all flavonoids are favorable and negative. Myricetin, morin and flavone penetrated into the core of the A?17?42 and formed self-clusters of A?17-42-flavonoid complexes. Analysis of A?17-42-flavonoids interactions identified that the hydrophobic interactions related to SASA-dependent energy are weak in all complexes. However, the intermolecular H-bonds are a main binding factor for shifting U-shape rod-like state of A?17?42 to globular-like disordered state. Myricetin and morin polyphenols form H-bonds with both peptide?s carbonyl and amine groups whereas flavone makes H-bonds only with amine substitution. As a result, polyphenols are more efficient in destabilizing ?-sheet structures of peptide. Accordingly, the natural polyphenolic flavonoids are useful in forming stable A?17-42-flavonoid clusters to inhibit A?17?42 aggregation and these compounds could be an effective candidate for therapeutically targeting U-shape protofilaments? monomer in amyloid mature fibrils. äThe role of phenolic OH groups of flavonoid compounds with H-bond form(epmc).pdf DeepDyve Pubget Overpricing