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Research

Publications: Dr John Viles

Liang R, Tian Y, Viles JH ( 2022 ) . Cross-seeding of WT amyloid-β with Arctic but not Italian familial mutants accelerates fibril formation in Alzheimer's disease . Journal of Biological Chemistry vol. 298 , ( 7 )
Tian Y, Liu J, Yang F, Lian C, Zhang H, Viles JH, Li Z ( 2022 ) . Therapeutic potential for amyloid surface inhibitor: only amyloid-β oligomers formed by secondary nucleation disrupt lipid membrane integrity . FEBS Journal
Tian Y, Liang R, Kumar A, Szwedziak P, Viles JH ( 2021 ) . 3D-visualization of amyloid-β oligomer interactions with lipid membranes by cryo-electron tomography . Chemical Science vol. 12 , ( 20 ) 6896 - 6907 .
Tian Y, Stanyon HF, Barritt JD, Mayet U, Patel P, Karamani E, Fusco G, Viles JH ( 2019 ) . Copper2+ Binding to α-Synuclein. Histidine50 Can Form a Ternary Complex with Cu2+ at the N-Terminus but Not a Macrochelate . Inorganic Chemistry: including bioinorganic chemistry vol. 58 , ( 22 ) 15580 - 15589 .
Bode DC, Freeley M, Nield J, Palma M, Viles JH ( 2019 ) . Amyloid-β oligomers have a profound detergent-like effect on lipid membrane bilayers, imaged by atomic force and electron microscopy . J Biol Chem vol. 294 , ( 19 ) 7566 - 7572 .
VILES JH ( 2018 ) . Copper Redox Cycling Inhibits Aβ Fibre Formation and Promotes Fibre Fragmentation, while Generating a Dityrosine Aβ Dimer . Scientific Reports
Younan ND, Chen K-F, Rose R-S, Crowther DC, Viles JH ( 2018 ) . Prion protein stabilizes amyloid-β (Aβ) oligomers and enhances Aβ neurotoxicity in a Drosophila model of Alzheimer's disease . J Biol Chem vol. 293 , ( 34 ) 13090 - 13099 .
Bode DC, Stanyon HF, Hirani T, Baker MD, Nield J, Viles JH ( 2018 ) . Serum Albumin's Protective Inhibition of Amyloid-β Fibre Formation Is Suppressed by Cholesterol, Fatty Acids and Warfarin . J Mol Biol
Barritt JD, Younan ND, Viles JH ( 2017 ) . N-Terminally Truncated Amyloid-β(11-40/42) Cofibrillizes with its Full-Length Counterpart: Implications for Alzheimer's Disease . Angew Chem Int Ed Engl vol. 56 , ( 33 ) 9816 - 9819 .
Barritt JD, Younan ND, Viles JH ( 2017 ) . N‐Terminally Truncated Amyloid‐β(11–40/42) Cofibrillizes with its Full‐Length Counterpart: Implications for Alzheimer's Disease . Angewandte Chemie vol. 129 , ( 33 ) 9948 - 9951 .
BAKER MD ( 2016 ) . Ion Channel Formation by Amyloid-β42 Oligomers but not Amyloid-β40 in Cellular Membranes . Journal of Biological Chemistry
Shahzad R, Jones MR, Viles JH, Jones CE ( 2016 ) . Endocytosis of the tachykinin neuropeptide, neurokinin B, in astrocytes and its role in cellular copper uptake . Journal of Inorganic Biochemistry vol. 162 , 319 - 325 .
Matheou CJ, Younan ND, Viles JH ( 2016 ) . The Rapid Exchange of Zinc2+ Enables Trace Levels to Profoundly Influence Amyloid-β Misfolding and Dominates Assembly Outcomes in Cu2+/Zn2+ Mixtures . Journal of Molecular Biology vol. 428 , ( 14 ) 2832 - 2846 .
Gu M, Viles JH ( 2016 ) . Methionine oxidation reduces lag-times for Amyloid-β(1–40) fibre formation but generates highly fragmented fibres . Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
Barritt JD, Viles JH ( 2015 ) . Truncated amyloid-β<inf>(11-40/42)</inf> from Alzheimer disease binds Cu<sup>2+</sup> with a femtomolar affinity and influences fiber assembly . Journal of Biological Chemistry vol. 290 , ( 46 ) 27791 - 27802 .
Younan ND, Viles JH ( 2015 ) . A Comparison of Three Fluorophores for the Detection of Amyloid Fibers and Prefibrillar Oligomeric Assemblies. ThT (Thioflavin T); ANS (1-Anilinonaphthalene-8-sulfonic Acid); and bisANS (4,4′-Dianilino-1,1′-binaphthyl-5,5′-disulfonic Acid) . Biochemistry vol. 54 , ( 28 ) 4297 - 4306 .
Nasica-Labouze J, Nguyen PH, Sterpone F, Berthoumieu O, Buchete NV, Coté S, De Simone A, Doig AJ et al. ( 2015 ) . Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies . Chemical Reviews vol. 115 , ( 9 ) 3518 - 3563 .
Matheou CJ, Younan ND, Viles JH ( 2015 ) . Cu<sup>2+</sup> accentuates distinct misfolding of Aβ<inf>(1-40)</inf> and Aβ<inf>(1-42)</inf> peptides, and potentiates membrane disruption . Biochemical Journal vol. 466 , 233 - 242 .
Jones CE, Otara CB, Younan ND, Viles JH, Elphick MR ( 2014 ) . Bioactivity and structural properties of chimeric analogs of the starfish SALMFamide neuropeptides S1 and S2 . Biochim Biophys Acta vol. 1844 , ( 10 ) 1842 - 1850 .
Stanyon HF, Cong X, Chen Y, Shahidullah N, Rossetti G, Dreyer J, Papamokos G, Carloni P et al. ( 2014 ) . Developing predictive rules for coordination geometry from visible circular dichroism of copper(II) and nickel(II) ions in histidine and amide main-chain complexes . FEBS J vol. 281 , ( 17 ) 3945 - 3954 .
Stanyon HF, Patel K, Begum N, Viles JH ( 2014 ) . Copper(II) sequentially loads onto the N-terminal amino group of the cellular prion protein before the individual octarepeats . Biochemistry vol. 53 , ( 24 ) 3934 - 3999 .
Otara CB, Jones CE, Younan ND, Viles JH, Elphick MR ( 2014 ) . Structural analysis of the starfish SALMFamide neuropeptides S1 and S2: the N-terminal region of S2 facilitates self-association . Biochim Biophys Acta vol. 1844 , ( 2 ) 358 - 365 .
Younan ND, Sarell CJ, Davies P, Brown DR, Viles JH ( 2013 ) . The cellular prion protein traps Alzheimer's Aβ in an oligomeric form and disassembles amyloid fibers . FASEB J vol. 27 , ( 5 ) 1847 - 1858 .
Viles JH ( 2012 ) . Metal ions and amyloid fiber formation in neurodegenerative diseases. Copper, zinc and iron in Alzheimer's, Parkinson's and prion diseases . COORDINATION CHEMISTRY REVIEWS vol. 256 , ( 19-20 ) 2271 - 2284 .
Younan ND, Nadal RC, Davies P, Brown DR, Viles JH ( 2012 ) . Methionine oxidation perturbs the structural core of the prion protein and suggests a generic misfolding pathway . J Biol Chem vol. 287 , ( 34 ) 28263 - 28275 .
Stanyon HF, Viles JH ( 2012 ) . Human serum albumin can regulate amyloid-β peptide fiber growth in the brain interstitium: implications for Alzheimer disease . J Biol Chem vol. 287 , ( 33 ) 28163 - 28168 .
Younan ND, Klewpatinond M, Davies P, Ruban AV, Brown DR, Viles JH ( 2011 ) . Copper(II)-induced secondary structure changes and reduced folding stability of the prion protein . J Mol Biol vol. 410 , ( 3 ) 369 - 382 .
Davies P, Wang X, Sarell CJ, Drewett A, Marken F, Viles JH, Brown DR ( 2011 ) . The synucleins are a family of redox-active copper binding proteins . Biochemistry vol. 50 , ( 1 ) 37 - 47 .
Sarell CJ, Wilkinson SR, Viles JH ( 2010 ) . Substoichiometric levels of Cu2+ ions accelerate the kinetics of fiber formation and promote cell toxicity of amyloid-{beta} from Alzheimer disease . J Biol Chem vol. 285 , ( 53 ) 41533 - 41540 .
Wright HM, Wyatt PB, Viles JH ( 2010 ) . Is oxidation the trigger of the Amyloid Cascade?: A synthesis of 2-oxo-histidine for incorporation into the Amyloid beta sequence . J PEPT SCI vol. 16 , 66 - 66 .
Nadal RC, Davies P, Brown DR, Viles JH ( 2009 ) . Evaluation of copper2+ affinities for the prion protein . Biochemistry vol. 48 , ( 38 ) 8929 - 8931 .
Sarell CJ, Syme CD, Rigby SEJ, Viles JH ( 2009 ) . Copper(II) binding to amyloid-beta fibrils of Alzheimer's disease reveals a picomolar affinity: stoichiometry and coordination geometry are independent of Abeta oligomeric form . Biochemistry vol. 48 , ( 20 ) 4388 - 4402 .
O'Sullivan DBD, Jones CE, Abdelraheim SR, Brazier MW, Toms H, Brown DR, Viles JH ( 2009 ) . Dynamics of a truncated prion protein, PrP(113-231), from (15)N NMR relaxation: order parameters calculated and slow conformational fluctuations localized to a distinct region . Protein Sci vol. 18 , ( 2 ) 410 - 423 .
Viles JH, Klewpatinond M, Nadal RC ( 2008 ) . Copper and the structural biology of the prion protein . Biochem Soc Trans vol. 36 , ( Pt 6 ) 1288 - 1292 .
Nadal RC, Rigby SEJ, Viles JH ( 2008 ) . Amyloid beta-Cu2+ complexes in both monomeric and fibrillar forms do not generate H2O2 catalytically but quench hydroxyl radicals . Biochemistry vol. 47 , ( 44 ) 11653 - 11664 .
Brazier MW, Davies P, Player E, Marken F, Viles JH, Brown DR ( 2008 ) . Manganese binding to the prion protein . J Biol Chem vol. 283 , ( 19 ) 12831 - 12839 .
Klewpatinond M, Davies P, Bowen S, Brown DR, Viles JH ( 2008 ) . Deconvoluting the Cu2+ binding modes of full-length prion protein . J BIOL CHEM vol. 283 , ( 4 ) 1870 - 1881 .
Klewpatinond M, Viles JH ( 2007 ) . Fragment length influences affinity for Cu2+ and Ni2+ binding to His(96) or His(111) of the prion protein and spectroscopic evidence for a multiple histidine binding only at low pH . BIOCHEM J vol. 404 , 393 - 402 .
Klewpatinond M, Viles JH ( 2007 ) . Empirical rules for rationalising visible circular dichroism of Cu2+ and Ni2+ histidine complexes: Applications to the prion protein . FEBS LETT vol. 581 , ( 7 ) 1430 - 1434 .
O'Sullivan DBD, Jones CE, Abdelraheim SR, Thompsett AR, Brazier MW, Toms H, Brown DR, Viles JH ( 2007 ) . NMR characterization of the pH 4 beta-intermediate of the prion protein: the N-terminal half of the protein remains unstructured and retains a high degree of flexibility . Biochem J vol. 401 , ( 2 ) 533 - 540 .
Nadal RC, Abdelraheim SR, Brazier MW, Rigby SEJ, Brown DR, Viles JH ( 2007 ) . Prion protein does not redox-silence Cu2+, but is a sacrificial quencher of hydroxyl radicals . Free Radic Biol Med vol. 42 , ( 1 ) 79 - 89 .
Syme CD, Viles JH ( 2006 ) . Solution 1H NMR investigation of Zn2+ and Cd2+ binding to amyloid-beta peptide (Abeta) of Alzheimer's disease . Biochim Biophys Acta vol. 1764 , ( 2 ) 246 - 256 .
Garnett AP, Jones CE, Viles JH ( 2006 ) . A survey of diamagnetic probes for copper2+ binding to the prion protein. 1H NMR solution structure of the palladium2+ bound single octarepeat . Dalton Trans ( 3 ) 509 - 518 .
Viles JH ( 2005 ) . Copper and the prion protein: Function and dysfunction . The Biochemist vol. 27 , ( 4 ) 9 - 12 .
Otara CB, Jones CE, Melarange R, Viles JH, Elphick MR ( 2005 ) . Tertiary structure and activity of SALMFamide neuropeptides . COMP BIOCHEM PHYS A vol. 141 , ( 3 ) S161 - S161 .
Jones CE, Klewpatinond M, Abdelraheim SR, Brown DR, Viles JH ( 2005 ) . Probing copper2+ binding to the prion protein using diamagnetic nickel2+ and 1H NMR: the unstructured N terminus facilitates the coordination of six copper2+ ions at physiological concentrations . J Mol Biol vol. 346 , ( 5 ) 1393 - 1407 .
Jones CE, Abdelraheim SR, Brown DR, Viles JH ( 2004 ) . Preferential Cu2+ coordination by His96 and His111 induces beta-sheet formation in the unstructured amyloidogenic region of the prion protein . J Biol Chem vol. 279 , ( 31 ) 32018 - 32027 .
Syme CD, Nadal RC, Rigby SEJ, Viles JH ( 2004 ) . Copper binding to the amyloid-beta (Abeta) peptide associated with Alzheimer's disease: folding, coordination geometry, pH dependence, stoichiometry, and affinity of Abeta-(1-28): insights from a range of complementary spectroscopic techniques . J Biol Chem vol. 279 , ( 18 ) 18169 - 18177 .
Garnett AP, Viles JH ( 2003 ) . Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: insights from circular dichroism . J Biol Chem vol. 278 , ( 9 ) 6795 - 6802 .
Dyson HJ, Wright PE, Mo HP, Viles JH ( 2002 ) . Structure and dynamics of prion and doppel proteins . ABSTR PAP AM CHEM S vol. 223 , C35 - C35 .
Dyson HJ, Mo HP, Viles JH, Wright PE, Prusiner SB, Cohen FE ( 2002 ) . Structure and dynamics of prion and Doppel proteins . BIOPHYS J vol. 82 , ( 1 ) 169A - 169A .
Viles JH, Duggan BM, Zaborowski E, Schwarzinger S, Huntley JJA, Kroon GJA, Dyson HJ, Wright PE ( 2001 ) . Potential bias in NMR relaxation data introduced by peak intensity analysis and curve fitting methods . J BIOMOL NMR vol. 21 , ( 1 ) 1 - 9 .
Viles JH, Donne D, Kroon G, Prusiner SB, Cohen FE, Dyson HJ, Wright PE ( 2001 ) . Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics . BIOCHEMISTRY-US vol. 40 , ( 9 ) 2743 - 2753 .
Viles JH, Cohen FE, Prusiner SB, Goodin DB, Wright PE, Dyson HJ ( 1999 ) . Copper binding to the prion protein: structural implications of four identical cooperative binding sites . Proc Natl Acad Sci U S A vol. 96 , ( 5 ) 2042 - 2047 .
Viles JH, Patel SU, Mitchell JB, Moody CM, Justice DE, Uppenbrink J, Doyle PM, Harris CJ et al. ( 1998 ) . Design, synthesis and structure of a zinc finger with an artificial beta-turn . J Mol Biol vol. 279 , ( 4 ) 973 - 986 .
Donne DG, Viles JH, Groth D, Mehlhorn I, James TL, Cohen FE, Prusiner SB, Wright PE et al. ( 1997 ) . Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible . Proc Natl Acad Sci U S A vol. 94 , ( 25 ) 13452 - 13457 .
Viles JH, Mitchell JB, Gough SL, Doyle PM, Harris CJ, Sadler PJ, Thornton JM ( 1996 ) . Multiple solution conformations of the integrin-binding cyclic pentapeptide cyclo(-Ser-D-Leu-Asp-Val-Pro-). Analysis of the (phi, psi) space available to cyclic pentapeptides . Eur J Biochem vol. 242 , ( 2 ) 352 - 362 .
Sadler PJ, Viles JH ( 1996 ) . 1H and (113)Cd NMR Investigations of Cd(2+) and Zn(2+) Binding Sites on Serum Albumin: Competition with Ca(2+), Ni(2+), Cu(2+), and Zn(2+) . Inorg Chem vol. 35 , ( 15 ) 4490 - 4496 .
Harris R, Patel SU, Sadler PJ, Viles JH ( 1996 ) . Observation of albumin resonances in proton nuclear magnetic resonance spectra of human blood plasma: N-terminal assignments aided by use of modified recombinant albumin . Analyst vol. 121 , ( 7 ) 913 - 922 .
Doyle PM, Harris JC, Moody CM, Sadler PJ, Sims M, Thornton JM, Uppenbrink J, Viles JH ( 1996 ) . Solution structure of a biologically active cyclic LDV peptide analogue containing a type II' beta-turn mimetic . Int J Pept Protein Res vol. 47 , ( 6 ) 427 - 436 .
Jones DT, Moody CM, Uppenbrink J, Viles JH, Doyle PM, Harris CJ, Pearl LH, Sadler PJ et al. ( 1996 ) . Towards meeting the Paracelsus Challenge: The design, synthesis, and characterization of paracelsin-43, an α-helical protein with over 50% sequence identity to an all-β protein . Proteins: Structure, Function and Genetics vol. 24 , ( 4 ) 502 - 513 .
Jones DT, Moody CM, Uppenbrink J, Viles JH, Doyle PM, Harris CJ, Pearl LH, Sadler PJ et al. ( 1996 ) . Towards meeting the Paracelsus Challenge: The design, synthesis, and characterization of paracelsin-43, an alpha-helical protein with over 50% sequence identity to an all-beta protein . Proteins vol. 24 , ( 4 ) 502 - 513 .
Sadler PJ, Viles JH ( 1996 ) . <sup>1</sup>H and <sup>113</sup>Cd NMR Investigations of Cd<sup>2+</sup> and Zn<sup>2+</sup> Binding Sites on Serum Albumin: Competition with Ca<sup>2+</sup>, Ni<sup>2+</sup>, Cu<sup>2+</sup>, and Zn<sup>2+</sup> . Inorganic Chemistry vol. 35 , ( 15 ) 4490 - 4496 .
Sadler PJ, Tucker A, Viles JH ( 1994 ) . Involvement of a lysine residue in the N-terminal Ni2+ and Cu2+ binding site of serum albumins. Comparison with Co2+, Cd2+ and Al3+ . Eur J Biochem vol. 220 , ( 1 ) 193 - 200 .
Patel SU, Sadler PJ, Tucker A, Viles JH ( 1993 ) . Direct Detection of Albumin in Human Blood Plasma by <sup>1</sup>H NMR Spectroscopy. Complexation of Nickel<sup>2+</sup> . Journal of the American Chemical Society vol. 115 , ( 20 ) 9285 - 9286 .
PATEL SU, SADLER PJ, TUCKER A, VILES JH ( 1993 ) . PROTON NMR DETECTION OF ALBUMIN IN INTACT HUMAN BLOOD-PLASMA . JOURNAL OF CELLULAR BIOCHEMISTRY . 298 - 298 .