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10.1016/j.abb.2014.12.008 http://scihub22266oqcxt.onion/10.1016/j.abb.2014.12.008 C5490837!5490837!25524740     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25524740&cmd=llinks): Failed to open stream: HTTP request failed! 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Aromaticity and amyloid formation: Effect of ?-electron distribution and aryl substituent geometry on the self-assembly of peptides derived from hIAPP22?29 |pdf=|usr=}}{{25524740}} gab.com Text Aromaticity and amyloid formation: Effect of -electron distribution and aryl substituent geometry on the self-assembly of peptides derived from hIAPP22 29 JO: Arch Biochem Biophys http://www.kidney.de/pget.php?&tw=1&pmid=25524740 #FOAvip A comprehensive investigation of peptides derived from the 22?29 region of human islet amyloid polypeptide (hIAPP) that contain phenylalanine analogs at position 23 with a variety of electron donating and withdrawing groups, along with heteroaromatic surrogates, has been employed to interrogate how ?-electron distribution effects amyloid formation. Kinetic aggregation studies using turbidity measurements indicate that electron rich aromatic ring systems consistently abolish the amyloidogenic propensity of hIAPP22?29. Electron poor systems modulate the rate of aggregation. Raman and Fourier transform infrared spectroscopy confirm the parallel ?-sheet secondary structure of aggregates derived from peptides containing electron poor phenylalanine analogs and provide direct evidence of ring stacking. Transmission electron microscopy confirms the presence of amyloid fibrils. The effect of aryl substituent geometry on peptide self-assembly reveals that the electronic nature of substituents and not their steric profile is responsible for failure of the electron donating group peptides to aggregate. Non-aggregating hIAPP22?29 peptides were found to inhibit the self-assembly of full-length hIAPP1?37. The most potent inhibitory peptides contain phenylalanine with the p-amino and p-formamido functionalities. These novel peptides may serve as leads for the development of future aggregation inhibitors. A potential mechanism for inhibition of amylin self-assembly by electron rich hIAPP22?29 peptides is proposed. Twit Text FOAVip Aromaticity and amyloid formation: Effect of -electron distribution and aryl substituent geometry on the self-assembly of peptides derived from hIAPP22 29 ????Arch Biochem Biophys http://www.kidney.de/pget.php?&tw=1&pmid=25524740 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25524740 #FOAvip English Wikipedia <ref>{{Cite pmid|25524740}}</ref> Aromaticity and amyloid formation: Effect of ?-electron distribution and aryl substituent geometry on the self-assembly of peptides derived from hIAPP22?29 #MMPMID25524740 Profit AA; Vedad J; Saleh M; Desamero RZ Arch Biochem Biophys 2015[Feb]; 567 (ä): 46-58 PMID25524740show ga A comprehensive investigation of peptides derived from the 22?29 region of human islet amyloid polypeptide (hIAPP) that contain phenylalanine analogs at position 23 with a variety of electron donating and withdrawing groups, along with heteroaromatic surrogates, has been employed to interrogate how ?-electron distribution effects amyloid formation. Kinetic aggregation studies using turbidity measurements indicate that electron rich aromatic ring systems consistently abolish the amyloidogenic propensity of hIAPP22?29. Electron poor systems modulate the rate of aggregation. Raman and Fourier transform infrared spectroscopy confirm the parallel ?-sheet secondary structure of aggregates derived from peptides containing electron poor phenylalanine analogs and provide direct evidence of ring stacking. Transmission electron microscopy confirms the presence of amyloid fibrils. The effect of aryl substituent geometry on peptide self-assembly reveals that the electronic nature of substituents and not their steric profile is responsible for failure of the electron donating group peptides to aggregate. Non-aggregating hIAPP22?29 peptides were found to inhibit the self-assembly of full-length hIAPP1?37. The most potent inhibitory peptides contain phenylalanine with the p-amino and p-formamido functionalities. These novel peptides may serve as leads for the development of future aggregation inhibitors. A potential mechanism for inhibition of amylin self-assembly by electron rich hIAPP22?29 peptides is proposed. äAromaticity and amyloid formation: Effect of ?-electron distribution a(epmc).pdf DeepDyve Pubget Overpricing