Mechanisms of protein aggregation and inhibition

Frontiers in Bioscience - Elite

Volumn 9, Issue 1, 2017, Pages 1-20

  Siddiqi, Mohammad Khursheed ^a   Alam, Parvez ^a   Chaturvedi, Sumit Kumar ^a   Shahein, Yasser E ^b   Khan, Rizwan Hasan ^a  

^a ALIGARH MUSLIM UNIVERSITY   (India)

^b NATIONAL RESEARCH CENTRE   (Egypt)

Author keywords

Protein Aggregation; Protein Misfolding, Amyloid, Review

Indexed keywords

AMYLOID; PROTEIN;

HUMAN; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN MISFOLDING; REVIEW; BIOLOGICAL MODEL; METABOLISM; PROTEINOSIS;

AMYLOID; HUMANS; MODELS, BIOLOGICAL; PROTEIN AGGREGATION, PATHOLOGICAL; PROTEIN FOLDING;

EID: 85016162443     PISSN: 19450494     EISSN: 19450508     Source Type: Journal    
DOI: 10.2741/e781     Document Type: Review

References (138)

1. R. H. Falk, R. L. Comenzo and M. Skinner: The systemic amyloidoses. New Eng J Med., 337(13), 898-909 (1997). DOI: 10.1056/nejm199709253371306
2. M. L. Biewend, D. M. Menke and K. T. Calamia: The spectrum of localized amyloidosis: a case series of 20 patients and review of the literature. Amyloid, 13(3), 135-142 (2006) DOI: 10.1080/13506120600876773
3. M. Renner and R. Melki: Protein aggregation and prionopathies. Pathologie Biologie (2014) DOI: 10.1016/j.patbio.2014.01.003
4. T. P. J. Knowles, M. Vendruscolo and C. M. Dobson: The amyloid state and its association with protein misfolding diseases. Nat Rev Mol Cell Biology, 15(6), 384-396 (2014) DOI: 10.1038/nrm3810
5. A. s. Association: 2010 Alzheimer's disease facts and figures. Alz Dement, 6(2), 158-94 (2010) doi:S1552-5260(10)00014-2 (pii) DOI: 10.1016/j.jalz.2010.01.009
6. D. Majoor-Krakauer, P. J. Willems and A. Hofman: Genetic epidemiology of amyotrophic lateral sclerosis. Clin Genet, 63(2), 83-101 (2003) DOI: 10.1046/j.0009-9163.2002.00001.x
7. E. M. Sivertsson and L. S. Itzhaki: Protein folding: When ribosomes pick the structure. Nat chem, 6(5), 378-379 (2014) DOI: 10.1038/nchem.1926
8. R. J. Ellis and A. P. Minton: Protein aggregation in crowded environments. J Biolog Chem, 387(5), 485-97 (2006) doi:10.1.515/BC.2006.0.64 DOI: 10.1515/bc.2006.064
9. C. M. Dobson: Protein folding and misfolding. Nature, 426(6968), 884-890 (2003) DOI: 10.1038/nature02261
10. T. R. Jahn and S. E. Radford: The Yin and Yang of protein folding. Febs J, 272(23), 5962-5970 (2005) DOI: 10.1111/j.1742-4658.2005.05021.x
11. J. M. Khan, A. Qadeer, E. Ahmad, R. Ashraf, B. Bhushan, S. K. Chaturvedi, G. Rabbani and R. H. Khan: Monomeric banana lectin at acidic pH overrules conformational stability of its native dimeric form. PloS one, 8(4), e62428 (2013) DOI: 10.1371/journal.pone.0062428
12. R. S. Rajan, M. E. Illing, N. F. Bence and R. R. Kopito: Specificity in intracellular protein aggregation and inclusion body formation. Pro Nat Acad Sci, 98(23), 13060-13065 (2001) DOI: 10.1073/pnas.181479798
13. M. Gopalswamy, A. Kumar, J. Adler, M. Baumann, M. Henze, S. T. Kumar, M. Fandrich, H. A. Scheidt, D. Huster and J. Balbach: Structural characterization of amyloid fibrils from the human parathyroid hormone. Biochim Biophy Acta (BBA)-Proteins and Proteomics, 1854(4), 249-257 (2015) DOI: 10.1016/j.bbapap.2014.12.020
14. H. Inouye, P. E. Fraser and D. A. Kirschner: Structure of beta-crystallite assemblies formed by Alzheimer beta-Amyloid protein analogues: analysis by x-ray diffraction. Biophy J, 64(2), 502 (1993) DOI: 10.1016/s0006-3495(93)81393-6
15. J. M. Khan, A. Qadeer, S. K. Chaturvedi, E. Ahmad, S. A. Rehman, S. Gourinath and R. H. Khan: SDS can be utilized as an amyloid inducer: a case study on diverse proteins. PloS one, 7(1), e29694 (2012) DOI: 10.1371/journal.pone.0029694
16. S. K. Chaturvedi, P. Alam, J. M. Khan, M. K. Siddiqui, P. Kalaiarasan, N. Subbarao, Z. Ahmad and R. H. Khan: Biophysical insight into the anti-Amyloidogenic behavior of taurine. Inter J bio macro, 80, 375-384 (2015) DOI: 10.1016/j.ijbiomac.2015.06.035
17. J. W. Kelly: Towards an understanding of amyloidogenesis. Nat Struct Biol, 9(5), 323-5 (2002) DOI: 10.1038/nsb0502-323
18. S. Barghorn, V. Nimmrich, A. Striebinger, C. Krantz, P. Keller, B. Janson, M. Bahr, M. Schmidt, R. S. Bitner and J. Harlan: Globular amyloid beta-peptide1-42 oligomer-A homogenous and stable neuropathological protein in Alzheimer's disease. J of neurochem, 95(3), 834-847 (2005) DOI: 10.1111/j.1471-4159.2005.03407.x
19. C. M. Dobson: The structural basis of protein folding and its links with human disease. Philos Trans R Soc Lond B BiolSci, 356(1406), 133-45 (2001) DOI: 10.1098/rstb.2000.0758
20. R. Wetzel: For protein misassembly, it's the "I" decade. Cell, 86(5), 699-702 (1996) DOI: 10.1016/s0092-8674(00)80143-9
21. A. H. Pekar and B. H. Frank: Conformation of proinsulin. A comparison of insulin and proinsulin self-Association at neutral pH.Biochemistry, 11(22), 4013-6 (1972) DOI: 10.1021/bi00772a001
22. E. Barbu and M. Joly: The globular-fibrous protein transformation. Discuss. Faraday Soc., 13, 77-93 (1953) DOI: 10.1039/df9531300077
23. B. S. Kendrick, J. F. Carpenter, J. L. Cleland and T. W. Randolph: A transient expansion of the native state precedes aggregation of recombinant human interferon-gamma. Proc Nat Acad Sci U S A, 95(24), 14142-6 (1998) DOI: 10.1073/pnas.95.24.14142
24. S. W. Raso, J. Abel, J. M. Barnes, K. M. Maloney, G. Pipes, M. J. Treuheit, J. King and D. N. Brems: Aggregation of granulocytecolony stimulating factor in vitro involves a conformationally altered monomeric state. Protein Sci, 14(9), 2246-57 (2005) DOI: 10.1110/ps.051489405
25. S. J. Shire, Z. Shahrokh and J. Liu: Challenges in the development of high protein concentration formulations. J Pharm Sci, 93(6), 1390-402 (2004) DOI: 10.1002/jps.20079
26. E. Y. Chi, J. Weickmann, J. F. Carpenter, M. C. Manning and T. W. Randolph: Heterogeneous nucleation-controlled particulate formation of recombinant human platelet-Activating factor acetylhydrolase in pharmaceutical formulation. J of pharma sci, 94(2), 256-274 (2005) DOI: 10.1002/jps.20237
27. S. I. A. Cohen, S. Linse, L. M. Luheshi, E. Hellstrand, D. A. White, L. Rajah, D. E. Otzen, M. Vendruscolo, C. M. Dobson and T. P. J. Knowles: Proliferation of amyloid-beta 42 aggregates occurs through a secondary nucleation mechanism. Pro of Nat Acad Sci, 110(24), 9758-9763 (2013) DOI: 10.1073/pnas.1218402110
28. S. Sambashivan, Y. Liu, M. R. Sawaya, M. Gingery and D. Eisenberg: Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure. Nature, 437(7056), 266-269 (2005) DOI: 10.1038/nature03916
29. F. U. Hartl, A. Bracher and M. Hayer-Hartl: Molecular chaperones in protein folding and proteostasis. Nature, 475(7356), 324-332 (2011) DOI: 10.1146/annurev-biochem-060208-092442
30. Y. E. Kim, M. S. Hipp, A. Bracher, M. Hayer-Hartl and F. Ulrich Hartl: Molecular chaperone functions in protein folding and proteostasis. Ann rev of biochem, 82, 323-355 (2013) DOI: 10.1146/annurev-biochem-060208-092442
31. J. C. Faver, M. L. Benson, X. He, B. P. Roberts, B. Wang, M. S. Marshall, C. D. Sherrill and K. M. Merz Jr: The energy computation paradox and ab initio protein folding. PloS one, 6(4), e18868 (2011) DOI: 10.1371/journal.pone.0018868
32. C. N. Pace, H. Fu, K. L. Fryar, J. Landua, S. R. Trevino, B. A. Shirley, M. M. Hendricks, S. Iimura, K. Gajiwala and J. M. Scholtz: Contribution of hydrophobic interactions to protein stability. J mol bio, 408(3), 514-528 (2011) DOI: 10.1016/j.jmb.2011.02.053
33. A. W. Fitzpatrick, T. P. J. Knowles, C. A. Waudby, M. Vendruscolo and C. M. Dobson: Inversion of the balance between hydrophobic and hydrogen bonding interactions in protein folding and aggregation. PLoS comput bio, 7(10), e1002169 (2011) DOI: 10.1371/journal.pcbi.1002169
34. W. Wang: Instability, stabilization, and formulation of liquid protein pharmaceuticals. Int J Pharm, 185(2), 129-88 (1999) DOI: 10.1016/s0378-5173(99)00152-0
35. R. C. Elgersma, L. M. Kroon-Batenburg, G. Posthuma, J. D. Meeldijk, D. T. Rijkers and R. M. Liskamp: pH-controlled aggregation polymorphism of amyloidogenic Abeta(16-22): Insights for obtaining peptide tapes and peptide nanotubes, as function of the N-terminal capping moiety. Eur J Med Chem (2014) DOI: 10.1016/j.ejmech.2014.07.089
36. W. Dzwolak, S. Grudzielanek, V. Smirnovas, R. Ravindra, C. Nicolini, R. Jansen, A. Loksztejn, S. Porowski and R. Winter: Ethanolperturbed amyloidogenic self-Assembly of insulin: looking for origins of amyloid strains. Biochemistry, 44(25), 8948-58 (2005) DOI: 10.1021/bi050281t
37. F. Hane, G. Tran, S. J. Attwood and Z. Leonenko: Cu(2+) affects amyloid-beta (1-42) aggregation by increasing peptidepeptide binding forces. PLoS One, 8(3), e59005 (2013) DOI: 10.1371/journal.pone.0059005
38. E. Cao, Y. Chen, Z. Cui and P. R. Foster: Effect of freezing and thawing rates on denaturation of proteins in aqueous solutions. Biotechnol Bioeng, 82(6), 684-90 (2003) DOI: 10.1002/bit.10612
39. H. C. Mahler, R. Muller, W. Friess, A. Delille and S. Matheus: Induction and analysis of aggregates in a liquid IgG1-Antibody formulation. Eur J Pharm Biopharm, 59(3), 407-17 (2005) DOI: 10.1016/j.ejpb.2004.12.004
40. J. M. Khan, S. K. Chaturvedi, S. K. Rahman, M. Ishtikhar, A. Qadeer, E. Ahmad and R. H. Khan: Protonation favors aggregation of lysozyme with SDS. Soft matter, 10(15), 2591-2599 (2014) DOI: 10.1039/c3sm52435c
41. F. Chiti and C. M. Dobson: Protein misfolding, functional amyloid, and human disease. Ann Rev Biochem, 75, 333-366 (2006) DOI: 10.1146/annurev. biochem.75.101304.123901
42. D. A. Drummond and C. O. Wilke: Mistranslation-induced protein misfolding as a dominant constraint on coding-sequence evolution. Cell, 134(2), 341-52 (2008) DOI: 10.1016/j.cell.2008.05.042
43. C. Munch and A. Bertolotti: Exposure of hydrophobic surfaces initiates aggregation of diverse ALS-causing superoxide dismutase-1 mutants. J mol bio, 399(3), 512-525 (2010) DOI: 10.1016/j.jmb.2010.04.019
44. L. Breydo, K. D. Reddy, A. Piai, I. C. Felli, R. Pierattelli and V. N. Uversky: The crowd you're in with: effects of different types of crowding agents on protein aggregation. Biochim Biophy Acta (BBA)-Proteins and Proteomics, 1844(2), 346-357 (2014) DOI: 10.1016/j.bbapap.2013.11.004
45. S. K. Chaturvedi, E. Ahmad, J. M. Khan, P. Alam, M. Ishtikhar and R. H. Khan: Elucidating the interaction of limonene with bovine serum albumin: a multi-technique approach. Mol BioSystems, 11(1), 307-316 (2015) DOI: 10.1039/c4mb00548a
46. D. M. Byler and H. Susi: Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers, 25(3), 469-487 (1986) DOI: 10.1002/bip.360250307
47. H. LeVine, 3rd: Alzheimer's betapeptide oligomer formation at physiologic concentrations. Anal Biochem, 335(1), 81-90 (2004) doi:S0003-2697(04)00664-5 (pii) DOI: 10.1016/j.ab.2004.08.014
48. S. N. Bagriantsev, V. V. Kushnirov and S. W. Liebman: Analysis of amyloid aggregates using agarose gel electrophoresis. Methods Enzymol, 412, 33-48 (2006) DOI: 10.1016/s0076-6879(06)12003-0
49. E. Miranda, I. MacLeod, M. J. Davies, J. Perez, K. Romisch, D. C. Crowther and D. A. Lomas: The intracellular accumulation of polymeric neuroserpin explains the severity of the dementia FENIB. Hum Mol Genet, 17(11), 1527-39 (2008) DOI: 10.1093/hmg/ddn041
50. K. A. Coalier, G. S. Paranjape, S. Karki and M. R. Nichols: Stability of early-stage amyloid-beta (1-42) aggregation species. Biochim Biophy Acta (BBA)-Proteins and Proteomics, 1834(1), 65-70 (2013) DOI: 10.1016/j.bbapap.2012.08.017
51. A. A. Reinke and J. E. Gestwicki: Structureactivity relationships of amyloid betaaggregation inhibitors based on curcumin: influence of linker length and flexibility. Chem Biol Drug Des, 70(3), 206-15 (2007) DOI: 10.1111/j.1747-0285.2007.00557.x
52. M. R. Nilsson: Techniques to study amyloid fibril formation in vitro. Methods, 34(1), 151-160 (2004) DOI: 10.1016/j.ymeth.2004.03.012
53. A. K. Chamberlain, C. E. MacPhee, J. s. Zurdo, L. A. Morozova-Roche, H. A. O. Hill, C. M. Dobson and J. J. Davis: Ultrastructural Organization of Amyloid Fibrils byAtomic Force Microscopy. Biophy J, 79(6), 3282-3293 (2000) DOI: 10.1016/s0006-3495(00)76560-x
54. M. Biancalana and S. Koide: Molecular mechanism of Thioflavin-T binding to amyloid fibrils. Biochim Biophy Acta (BBA)-Proteins and Proteomics, 1804(7), 1405-1412 (2010) DOI: 10.1016/j.bbapap.2010.04.001
55. I. W. Hamley, V. Castelletto, C. Moulton, D. Myatt, G. Siligardi, C. L. P. Oliveira, J. S. Pedersen, I. Abutbul and D. Danino: Self-Assembly of a Modified Amyloid Peptide Fragment: pH-Responsiveness and Nematic Phase Formation. Macromol biosci, 10(1), 40-48 (2010) DOI: 10.1002/mabi.200900217
56. S. L. Gras, L. J. Waddington and K. N. Goldie: Transmission electron microscopy of amyloid fibrils. In: Protein Folding, Misfolding, and Disease. Springer, (2011) DOI: 10.1007/978-1-60327-223-0-13
57. H. Seiler: Secondary electron emission in the scanning electron microscope. J App Phy, 54(11), R1-R18 (1983) DOI: 10.1063/1.332840
58. L. Hughes, C. Hawes, S. Monteith and S. Vaughan: Serial block face scanning electron microscopy-the future of cell ultrastructure imaging. Protoplasma, 251(2), 395-401 (2014) DOI: 10.1007/s00709-013-0580-1
59. V. N. Uversky and A. L. Fink: Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim Biophy Acta (BBA)-Proteins and Proteomics, 1698(2), 131-153 (2004) DOI: 10.1016/j.bbapap.2003.12.008
60. M. Stefani and C. M. Dobson: Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J mol med, 81(11), 678-699 (2003) DOI: 10.1007/s00109-003-0464-5
61. D. M. Fowler, A. V. Koulov, W. E. Balch and J. W. Kelly: Functional amyloid-from bacteria to humans. Trends in biocheml sci, 32(5), 217-224 (2007) DOI: 10.1016/j.tibs.2007.03.003
62. M. Masuda, N. Suzuki, S. Taniguchi, T. Oikawa, T. Nonaka, T. Iwatsubo, S. Hisanaga, M. Goedert and M. Hasegawa: Small molecule inhibitors of alpha-synuclein filament assembly. Biochemistry, 45(19), 6085-94 (2006) DOI: 10.1021/bi0600749
63. D. E. Ehrnhoefer, J. Bieschke, A. Boeddrich, M. Herbst, L. Masino, R. Lurz, S. Engemann, A. Pastore and E. E. Wanker: EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers. Nat Struct Mol Biol, 15(6), 558-66 (2008) DOI: 10.1038/nsmb.1437
64. P. Frid, S. V. Anisimov and N. Popovic: Congo red and protein aggregation in neurodegenerative diseases. Brain Res Rev, 53(1), 135-60 (2007) DOI: 10.1016/j.brainresrev.2006.08.001
65. A. Ciechanover: The ubiquitin proteolytic system: from a vague idea, through basic mechanisms, and onto human diseases and drug targeting. Neurology, 66(2 Suppl 1), S7-19 (2006) DOI: 10.1212/01.wnl.0000192261.02023.b8
66. U. B. Pandey, Z. Nie, Y. Batlevi, B. A. McCray, G. P. Ritson, N. B. Nedelsky, S. L. Schwartz, N. A. DiProspero, M. A. Knight, O. Schuldiner, R. Padmanabhan, M. Hild, D. L. Berry, D. Garza, C. C. Hubbert, T. P. Yao, E. H. Baehrecke and J. P. Taylor: HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS. Nature, 447(7146), 859-63 (2007) DOI: 10.1038/nature05853
67. L. Bedford, D. Hay, A. Devoy, S. Paine, D. G. Powe, R. Seth, T. Gray, I. Topham, K. Fone, N. Rezvani, M. Mee, T. Soane, R. Layfield, P. W. Sheppard, T. Ebendal, D. Usoskin, J. Lowe and R. J. Mayer: Depletion of 26S proteasomes in mouse brain neurons causes neurodegeneration and Lewy-like inclusions resembling human pale bodies. J Neurosci, 28(33), 8189-98 (2008) DOI: 10.1523/jneurosci.2218-08.2008
68. H. Nakatogawa, K. Suzuki, Y. Kamada and Y. Ohsumi: Dynamics and diversity in autophagy mechanisms: lessons from yeast. Nat Rev Mol Cell Bio, 10(7), 458-467 (2009) DOI: 10.1038/nrm2708
69. C. He and D. J. Klionsky: Regulation mechanisms and signaling pathways of autophagy. Annu Rev Genet, 43, 67-93 (2009) doi:10.1.146/annurev-genet-102808-114910 DOI: 10.1146/annurev-genet-102808-114910
70. J. Fortun, W. A. Dunn, S. Joy, J. Li and L. Notterpek: Emerging role for autophagy in the removal of aggresomes in Schwann cells. The J neurosci, 23(33), 10672-10680 (2003) (doi not found)
71. J. A. Olzmann and L.-S. Chin: Parkinmediated K63-linked polyubiquitination: a signal for targeting misfolded proteins to the aggresome-Autophagy pathway. Autophagy, 4(1), 85 (2008) DOI: 10.4161/auto.5172
72. M. Bier and F. F. Nord: Aggregation phenomena in egg albumin solutions as determined by light scattering measurements. Proc Nat Aca Sci, 35(1), 17 (1949) DOI: 10.1073/pnas.35.1.17
73. L. Pauling: Protein interactions. Aggregation of globular proteins. Discuss. Faraday Soc., 13, 170-176 (1952) DOI: 10.1039/df9531300170
74. E. V. Jensen: Sulfhydryl-Disulfide Interchange This biological chain reaction explains aspects of protein denaturation, blood clotting, and mitosis. Sci, 130(3385), 1319-1323 (1959) DOI: 10.1126/science.130.3385.1319
75. W. Colon and J. W. Kelly: Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry, 31(36), 8654-8660 (1992) DOI: 10.1021/bi00151a036
76. K. Halverson, P. E. Fraser, D. A. Kirschner and P. T. Lansbury Jr: Molecular determinants of amyloid deposition in Alzheimer's disease: conformational studies of synthetic. beta.-protein fragments. Biochemistry, 29(11), 2639-2644 (1990) DOI: 10.1021/bi00463a003
77. A. L. Fink: Protein aggregation: folding aggregates, inclusion bodies and amyloid. Folding and design, 3(1), R9-R23 (1998) DOI: 10.1016/s1359-0278(98)00002-9
78. M. Sunde, L. C. Serpell, M. Bartlam, P. E. Fraser, M. B. Pepys and C. C. F. Blake: Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J mol bio, 273(3), 729-739 (1997) DOI: 10.1006/jmbi.1997.1348
79. J. M. Khan, A. Qadeer, S. K. Chaturvedi, E. Ahmad, S. A. A. Rehman, S. Gourinath and R. H. Khan: SDS can be utilized as an amyloid inducer: a case study on diverse proteins. PloS one, 7(1), e29694 (2012) DOI: 10.1371/journal.pone.0029694
80. M. Pitschke, R. Prior, M. Haupt and D. Riesner: Detection of single amyloid beta-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy. Nat med, 4(7), 832-834 (1998) DOI: 10.1038/nm0798-832
81. B. J. Bacskai, W. E. Klunk, C. A. Mathis and B. T. Hyman: Imaging Amyloid-&bgr; Deposits In vivo. J Cereb Blood Flow & Metab, 22(9), 1035-1041 (2002) DOI: 10.1097/00004647-200209000-00001
82. R. Khurana, C. Coleman, C. Ionescu-Zanetti, S. A. Carter, V. Krishna, R. K. Grover, R. Roy and S. Singh: Mechanism of thioflavin T binding to amyloid fibrils. J str bio, 151(3), 229-238 (2005) DOI: 10.1016/j.jsb.2005.06.006
83. I. V. Baskakov, G. Legname, M. A. Baldwin, S. B. Prusiner and F. E. Cohen: Pathway complexity of prion protein assembly into amyloid. J Biolog Chem, 277(24), 21140-21148 (2002) DOI: 10.1074/jbc.m111402200
84. C.-C. Lee, A. Nayak, A. Sethuraman, G. Belfort and G. J. McRae: A three-stage kinetic model of amyloid fibrillation. Biophy j, 92(10), 3448-3458 (2007) DOI: 10.1529/biophysj.106.098608
85. P. H. Axelsen, H. Komatsu and I. V. J. Murray: Oxidative stress and cell membranes in the pathogenesis of Alzheimer's disease. Physiology, 26(1), 54-69 (2011) DOI: 10.1152/physiol.00024.2010
86. P. Cao, L.-H. Tu, A. Abedini, O. Levsh, R. Akter, V. Patsalo, A. M. Schmidt and D. P. Raleigh: Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue J mol bio, 421(2), 282-295 (2012) DOI: 10.1016/j.jmb.2011.12.032
87. J. Tyedmers, A. Mogk and B. Bukau: Cellular strategies for controlling protein aggregation. Nat rev Mol cell biology, 11(11), 777-788 (2010) DOI: 10.1038/nrm2993
88. Q. I. Churches, J. Caine, K. Cavanagh, V. C. Epa, L. Waddington, C. E. Tranberg, A. G. Meyer, J. N. Varghese, V. Streltsov and P. J. Duggan: Naturally occurring polyphenolic inhibitors of amyloid beta aggregation. Bioorganic & med chem lett (2104) DOI: 10.1016/j.bmcl.2014.05.008
89. Z. Wang, L. Chang, W. L. Klein, G. R. J. Thatcher and D. L. Venton: Per-6-substitutedper-6-deoxy beta-cyclodextrins inhibit the formation of beta-Amyloid peptide derived soluble oligomers. J med chem, 47(13), 3329-3333 (2004) DOI: 10.1021/jm034224e
90. J. Jayamani and G. Shanmugam: Gallic acid, one of the components in many plant tissues, is a potential inhibitor for insulin amyloid fibril formation. Europ j med chem (2014) DOI: 10.1016/j.ejmech.2014.07.111v
91. D. C. Thorn, S. Meehan, M. Sunde, A. Rekas, S. L. Gras, C. E. MacPhee, C. M. Dobson, M. R. Wilson and J. A. Carver: Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alphaS-And beta-casein. Biochemistry, 44(51), 17027-36 (2005) DOI: 10.1021/bi051352r
92. A. Lorenzo and B. A. Yankner: Beta-Amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Pro Nat Aca Sci, 91(25), 12243-12247 (1994) DOI: 10.1073/pnas.91.25.12243
93. C. M. Wischik, P. C. Edwards, R. Y. Lai, M. Roth and C. R. Harrington: Selective inhibition of Alzheimer disease-like tau aggregation by phenothiazines. Pro Nat Aca Sci, 93(20), 11213-11218 (1996) DOI: 10.1073/pnas.93.20.11213
94. K. Suzuki, T. Miura and H. Takeuchi: Inhibitory effect of copper (II) on zinc (II)-induced aggregation of amyloid beta-peptide. Biochem biophys res comm, 285(4), 991-996 (2001) DOI: 10.1006/bbrc.2001.5263
95. R. Liu, H. Barkhordarian, S. Emadi, C. B. Park and M. R. Sierks: Trehalose differentially inhibits aggregation and neurotoxicity of betaamyloid 40 and Neurobio of disease, 20(1), 74-81 (2005) DOI: 10.1016/j.nbd.2005.02.003
96. Z. Ignatova and L. M. Gierasch: Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant. Pro Nat Aca Sci, 103(36), 13357-13361 (2006) DOI: 10.1073/pnas.0603772103
97. J. Wawer, J. Krakowiak, M. Szocinski, Z. Lustig, M. Olszewski and K. Szostak: Inhibition of amyloid fibril formation of hen egg white lysozyme by trimethylamine N-oxide at low pH. Inter j bio mac, 70, 214-221 (2014) DOI: 10.1016/j.ijbiomac.2014.06.057
98. C. Cabaleiro-Lago, F. Quinlan-Pluck, I. Lynch, S. Lindman, A. M. Minogue, E. Thulin, D. M. Walsh, K. A. Dawson and S. Linse: Inhibition of amyloid beta protein fibrillation by polymeric nanoparticles. J American Chem Soc, 130(46), 15437-15443 (2008) DOI: 10.1021/ja8041806
99. S. Palmal, A. R. Maity, B. K. Singh, S. Basu, N. R. Jana and N. R. Jana: Inhibition of Amyloid Fibril Growth and Dissolution of Amyloid Fibrils by Curcumin-Gold Nanoparticles. Chem-A Europ J, 20(20), 6184-6191 (2014) DOI: 10.1002/chem.201400079
100. F. Yang, G. P. Lim, A. N. Begum, O. J. Ubeda, M. R. Simmons, S. S. Ambegaokar, P. P. Chen, R. Kayed, C. G. Glabe and S. A. Frautschy: Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo. J Biolog Chem, 280(7), 5892-5901 (2005) DOI: 10.1074/jbc.m404751200
101. J. Luo, S. K. T. S. Warmlander, A. Graslund and J. P. Abrahams: Non-chaperone Proteins Can Inhibit Aggregation and Cytotoxicity of Alzheimer Amyloid beta Peptide. J Biolog Chem, 289(40), 27766-27775 (2014) DOI: 10.1074/jbc.m114.574947
102. T. Jiang, J. T. Yu, X. C. Zhu, M.-S. Tan, H. F. Wang, L. Cao, Q. Q. Zhang, J. Q. Shi, L. Gao and H. Qin: Temsirolimus promotes autophagic clearance of amyloid-beta and provides protective effects in cellular and animal models of Alzheimer's disease. Pharmacol Res, 81, 54-63 (2014) DOI: 10.1016/j.phrs.2014.02.008
103. L. Hong, H.-C. Huang and Z.-F. Jiang: Relationship between amyloid-beta and the ubiquitin-proteasome system in Alzheimer's disease. Neurolog res, 36(3), 276-282 (2014) DOI: 10.1179/1743132813y.0000000288
104. H. F. Dovey, V. John, J. P. Anderson, L. Z. Chen, P. de Saint Andrieu, L. Y. Fang, S. B. Freedman, B. Folmer, E. Goldbach and E. J. Holsztynska: Functional gamma-secretase inhibitors reduce beta-Amyloid peptide levels in brain. J neurochem, 76(1), 173-181 (2001) DOI: 10.1046/j.1471-4159.2001.00012.x
105. K. Rezai-Zadeh, D. Shytle, N. Sun, T. Mori, H. Hou, D. Jeanniton, J. Ehrhart, K. Townsend, J. Zeng and D. Morgan: Green tea epigallocatechin-3-gallate (EGCG) modulates amyloid precursor protein cleavage and reduces cerebral amyloidosis in Alzheimer transgenic mice. J neurosci, 25(38), 8807-8814 (2005) DOI: 10.1523/jneurosci.1521-05.2005
106. G. T. Bramblett, M. Goedert, R. Jakes, S. E. Merrick, J. Q. Trojanowski and V. M. Y. Lee: Abnormal tau phosphorylation at Ser 396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding. Neuron, 10(6), 1089-1099 (1993) DOI: 10.1016/0896-6273(93)90057-x
107. C. A. Lasagna-Reeves, A. L. Clos, D. Castillo-Carranza, U. Sengupta, M. Guerrero-Munoz, B. Kelly, R. Wagner and R. Kayed: Dual role of p53 amyloid formation in cancer; loss of function and gain of toxicity. Biochem biophys res comm, 430(3), 963-968 (2013) DOI: 10.1016/j.bbrc.2012.11.130
108. S. Gupta, T. Chattopadhyay, M. P. Singh and A. Surolia: Supramolecular insulin assembly II for a sustained treatment of type 1 diabetes mellitus. Pro Nat Aca Sci, 107(30), 13246-13251 (2010) DOI: 10.1073/pnas.1005704107
109. U. Shimanovich, I. Efimov, T. O. Mason, P. Flagmeier, A. K. Buell, A. Gedanken, S. Linse, K. S. A kerfeldt, C. M. Dobson and D. A. Weitz: Protein Microgels from Amyloid Fibril Networks. ACS nano, 9(1), 43-51 (2015) DOI: 10.1021/nn504869d
110. U. Shimanovich, I. Efimov, T. O. Mason, P. Flagmeier, A. K. Buell, A. Gedanken, S. A. Linse, Karin S., C. M. Dobson and D. A. Weitz: Protein Microgels from Amyloid Fibril Networks. ACS nano, 9(1), 43-51 (2015) DOI: 10.1021/nn504869d
111. E. Reisler, J. Pouyet and H. Eisenberg: Molecular weights, association, and frictional resistance of bovine liver glutamate dehydrogenase at low concentrations. Equilibrium and velocity sedimentation, light-scattering studies, and settling experiments with macroscopic models of the enzyme oligomer. Biochemistry, 9(15), 3095-102 (1970) DOI: 10.1021/bi00817a600
112. J. Hofrichter, P. D. Ross and W. A. Eaton: Kinetics and mechanism of deoxyhemoglobin S gelation: a new approach to understanding sickle cell disease. Pro Nat Aca Sci, 71(12), 4864-4868 (1974) DOI: 10.1073/pnas.71.12.4864
113. A. Wegner and J. Engel: Kinetics of the cooperative association of actin to actin filament. Biophy chem, 3(3), 215-225 (1975) DOI: 10.1016/0301-4622(75)80013-5
114. F. A. Ferrone, J. Hofrichter, H. R. Sunshine and W. A. Eaton: Kinetic studies on photolysisinduced gelation of sickle cell hemoglobin suggest a new mechanism. Biophy j, 32(1), 361-380 (1980) DOI: 10.1016/s0006-3495(80)84962-9
115. M. P. Firestone, R. De Levie and S. K. Rangarajan: On one-dimensional nucleation and growth of "living" polymers I. Homogeneous nucleation. J theoret bio, 104(4), 535-552 (1983) DOI: 10.1016/0022-5193(83)90244-8
116. S. B. Prusiner: Molecular biology of prion diseases. Science, 252(5012), 1515-1522 (1991) DOI: 10.1126/science.1675487
117. M. A. Watzky and R. G. Finke: Transition metal nanocluster formation kinetic and mechanistic studies. A new mechanism when hydrogen is the reductant: slow, continuous nucleation and fast autocatalytic surface growth. J American Chem Soc, 119(43), 10382-10400 (1997) DOI: 10.1021/ja9705102
118. K. F. DuBay, A. P. Pawar, F. Chiti, J. s. Zurdo, C. M. Dobson and M. Vendruscolo: Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. J mol bio, 341(5), 1317-1326 (2004) DOI: 10.1016/j.jmb.2004.06.043
119. M. M. Barnhart and M. R. Chapman: Curli biogenesis and function. Ann rev microbio, 60, 131 (2006) DOI: 10.1146/micro.2006.60.issue-1
120. M. F. B. G. Gebbink, D. Claessen, B. Bouma, L. Dijkhuizen and H. A. B. Wosten: Amyloids-A functional coat for microorganisms. Nat Rev Microbio, 3(4), 333-341 (2005) DOI: 10.1038/nrmicro1127
121. P. Chien, J. S. Weissman and A. H. DePace: Emerging principles of conformation-based prion inheritance. Ann rev biochem, 73(1), 617-656 (2004) DOI: 10.1146/annurev. biochem.72.121801.161837
122. A. H. Y. Kwan, R. D. Winefield, M. Sunde, J. M. Matthews, R. G. Haverkamp, M. D. Templeton and J. P. Mackay: Structural basis for rodlet assembly in fungal hydrophobins. Pro Nat Aca Sci, 103(10), 3621-3626 (2006) DOI: 10.1073/pnas.0505704103
123. S. J. Saupe: Molecular genetics of heterokaryon incompatibility in filamentous ascomycetes. Microbio and mol bio rev, 64(3), 489-502 (2000) DOI: 10.1128/mmbr.64.3.489-502.2000
124. J. M. Kenney, D. Knight, M. J. Wise and F. Vollrath: Amyloidogenic nature of spider silk. Europ J Biochem, 269(16), 4159-4163 (2002) DOI: 10.1046/j.1432-1033.2002.03112.x
125. K. Si, S. Lindquist and E. R. Kandel: A neuronal isoform of the aplysia CPEB has prion-like properties. Cell, 115(7), 879-891 (2003) DOI: 10.1016/s0092-8674(03)01020-1
126. J. F. Berson, A. C. Theos, D. C. Harper, D. Tenza, G. Raposo and M. S. Marks: Proproteinconvertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis. J cell bio, 161(3), 521-533 (2003) DOI: 10.1083/jcb.200302072
127. S. A. Hudson, H. Ecroyd, F. C. Dehle, I. F. Musgrave and J. A. Carver: (-)-epigallocatechin-3-gallate (EGCG) maintains kappa-casein in its pre-fibrillar state without redirecting its aggregation pathway. J Mol Bio, 392(3), 689-700 (2009) DOI: 10.1016/j.jmb.2009.07.031
128. N. Ferreira, M. J. o. Saraiva and M. R. r. Almeida: Natural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formation. FEBS letters, 585(15), 2424-2430 (2011) DOI: 10.1016/j.febslet.2011.06.030
129. M. Hirohata, K. Hasegawa, S. Tsutsumi-Yasuhara, Y. Ohhashi, T. Ookoshi, K. Ono, M. Yamada and H. Naiki: The anti-Amyloidogenic effect is exerted against Alzheimer's betaamyloid fibrils in vitro by preferential and reversible binding of flavonoids to the amyloid fibril structure. Biochemistry, 46(7), 1888-99 (2007) DOI: 10.1021/bi061540x
130. F. Meng, A. Abedini, A. Plesner, C. B. Verchere and D. P. Raleigh: The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity. Biochemistry, 49(37), 8127-8133 (2010) DOI: 10.1021/bi100939a
131. A. Qadeer, M. Zaman and R. H. Khan: Inhibitory effect of post-micellar SDS concentration on thermal aggregation and activity of papain. Biochemistry (Moscow), 79(8), 785-796 (2014) DOI: 10.1134/s0006297914080069
132. N. Gull, M. A. Mir, J. M. Khan, R. H. Khan, G. M. Rather and A. A. Dar: Refolding of bovine serum albumin via artificial chaperone protocol using gemini surfactants. J coll interf sci, 364(1), 157-162 (2011) DOI: 10.1016/j.jcis.2011.08.015
133. Y. Miura, K. Yasuda, K. Yamamoto, M. Koike, Y. Nishida and K. Kobayashi: Inhibition of Alzheimer amyloid aggregation with sulfated glycopolymers. Biomac, 8(7), 2129-2134 (2007) DOI: 10.1021/bm0701402
134. S. Sardar, S. Pal, S. Maity, J. Chakraborty and U. C. Halder: Amyloid fibril formation by beta-lactoglobulin is inhibited by gold nanoparticles. Inter j bio macromol (2014) DOI: 10.1016/j.ijbiomac.2014.05.006
135. M. Kanapathipillai, G. Lentzen, M. Sierks and C. B. Park: Ectoine and hydroxyectoine inhibit aggregation and neurotoxicity of Alzheimer's beta-Amyloid. FEBS letters, 579(21), 4775-4780 (2005) DOI: 10.1016/j.febslet.2005.07.057
136. Y. S. Lee, H. Y. Kim, H. M. Youn, J. H. Seo, Y. Kim and K. J. Shin: 2-Phenylbenzofuran derivatives alleviate mitochondrial damage via the inhibition of beta-Amyloid aggregation. Bioorganic & med chem lett, 23(21), 5882-5886 (2013) DOI: 10.1016/j.bmcl.2013.08.087
137. Y.-P. Chen, Z.-Y.Zhang, Y.-P. Li, D. Li, S.-L. Huang, L.-Q.Gu, J. Xu and Z.-S. Huang: Syntheses and evaluation of novel isoliquiritigenin derivatives as potential dual inhibitors for amyloid-beta aggregation and 5-lipoxygenase. Europ j med chem, 66, 22-31 (2013) DOI: 10.1016/j.ejmech.2013.05.015
138. J. N. Abraham, D. Kedracki, E. Prado, C. Gourmel, P. Maroni and C. Nardin: Effect of the Interaction of the Amyloid beta (1-42) Peptide with Short Single Stranded Synthetic Nucleotide Sequences: Morphological Characterization of the Inhibition of Fibrils Formation and Fibrils Disassembly. Biomac (2014) DOI: 10.1021/bm501004q