Dynamics of protofibril elongation and association involved in Aβ42 peptide aggregation in Alzheimer's disease

BMC Bioinformatics

Volumn 11, Issue SUPPL. 6, 2010, Pages

  Ghosh, Preetam ^a   Kumar, Amit ^b   Datta, Bhaswati ^a   Rangachari, Vijayaraghavan ^b  

^a UNIVERSITY OF SOUTHERN MISSISSIPPI   (United States)

^b University of Southern Mississippi   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATION PROCESS; ALZHEIMER'S DISEASE; BIOPHYSICAL ANALYSIS; COMPUTATIONAL PREDICTIONS; CONCENTRATION VARIATION; KINETIC RATE CONSTANTS; PEPTIDE AGGREGATION; PROTEIN AGGREGATION;

AGGLOMERATION; AGGREGATES; ASSOCIATION REACTIONS; BIOPHYSICS; COMPUTER SIMULATION; CURVE FITTING; ESTIMATION; KINETIC PARAMETERS; NEURODEGENERATIVE DISEASES; NUCLEATION; OLIGOMERS; PEPTIDES; RATE CONSTANTS; SENSITIVITY ANALYSIS; SYSTEM THEORY;

ELONGATION;

AMYLOID; AMYLOID BETA PROTEIN;

ALZHEIMER DISEASE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; KINETICS; METABOLISM; MOLECULAR DYNAMICS; RADIATION SCATTERING;

ALZHEIMER DISEASE; AMYLOID; AMYLOID BETA-PEPTIDES; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; SCATTERING, RADIATION;

EID: 77957713248     PISSN: None     EISSN: 14712105     Source Type: Journal    
DOI: 10.1186/1471-2105-11-24     Document Type: Article

References (26)

1. Selkoe DJ, Schenk D. Alzheimer's disease: molecular understanding predicts amyloid-based therapeutics,. Annu Rev Pharmacol Toxicol 2003, 43:545-584. 10.1146/annurev.pharmtox.43.100901.140248, 12415125.
2. Harper JD, Lansbury PT. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins,. Annu Rev Biochem 1997, 66:385-407. 10.1146/annurev.biochem.66.1.385, 9242912.
3. Jarrett JT, Berger EP, Lansbury PT. The C-terminus of the beta protein is critical in amyloidogenesis,. Ann N Y Acad Sci 1993, 695:144-148. 10.1111/j.1749-6632.1993.tb23043.x, 8239273.
4. Walsh DM, Lomakin A, Benedek GB, Condron MM, Teplow DB. Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate,. J Biol Chem 1997, 272:22364-22372. 10.1074/jbc.272.35.22364, 9268388.
5. Lomakin A, Teplow DB, Kirschner DA, Benedek GB. Kinetic theory of fibrillogenesis of amyloid beta-protein,. Proc Natl Acad Sci U S A 1997, 94:7942-7947. 10.1073/pnas.94.15.7942, 21534, 9223292.
6. Evans KC, Berger EP, Cho CG, Weisgraber KH, Lansbury PT. Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: implications for the pathogenesis and treatment of Alzheimer disease,. Proc Natl Acad Sci U S A 1995, 92:763-767. 10.1073/pnas.92.3.763, 42700, 7846048.
7. O'Nuallain B, Williams AD, Westermark P, Wetzel R. Seeding specificity in amyloid growth induced by heterologous fibrils,. J Biol Chem 2004, 279:17490-17499. 10.1074/jbc.M311300200, 14752113.
8. Ward RV, Jennings KH, Jepras R, Neville W, Owen DE, Hawkins J, Christie G, Davis JB, George A, Karran EH, Howlett DR. Fractionation and characterization of oligomeric, protofibrillar and fibrillar forms of beta-amyloid peptide,. Biochem J 2000, 348(1):137-144. 10.1042/0264-6021:3480137, 1221046, 10794724.
9. Murphy RM, Pallitto MM. Probing the kinetics of beta-amyloid self-association,. J Struct Biol 2000, 130:109-122. 10.1006/jsbi.2000.4253, 10940219.
10. Harper JD, Wong SS, Lieber CM, Lansbury PT. Assembly of A beta amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease,. Biochemistry 1999, 38:8972-8980. 10.1021/bi9904149, 10413470.
11. Blackley HK, Sanders GH, Davies MC, Roberts CJ, Tendler SJ, Wilkinson MJ. In-situ atomic force microscopy study of beta-amyloid fibrillization,. J Mol Biol 2000, 298:833-840. 10.1006/jmbi.2000.3711, 10801352.
12. Harper JD, Wong SS, Lieber CM, Lansbury PT. Observation of metastable Abeta amyloid protofibrils by atomic force microscopy,. Chem Biol 1997, 4:119-125. 10.1016/S1074-5521(97)90255-6, 9190286.
13. Nichols MR, Moss MA, Reed DK, Lin WL, Mukhopadhyay R, Hoh JH, Rosenberry TL. Growth of beta-amyloid(1-40) protofibrils by monomer elongation and lateral association. Characterization of distinct products by light scattering and atomic force microscopy,. Biochemistry 2002, 41:6115-6127. 10.1021/bi015985r, 11994007.
14. O'Nuallain B, Shivaprasad S, Kheterpal I, Wetzel R. Thermodynamics of A beta(1-40) amyloid fibril elongation,. Biochemistry 2005, 44:12709-12718. 10.1021/bi050927h, 16171385.
15. Leissring MA, Lu A, Condron MM, Teplow DB, Stein RL, Farris W, Selkoe DJ. Kinetics of amyloid beta-protein degradation determined by novel fluorescence- and fluorescence polarization-based assays,. J Biol Chem 2003, 278:37314-37320. 10.1074/jbc.M305627200, 12867419.
16. Cannon MJ, Williams AD, Wetzel R, Myszka DG. Kinetic analysis of beta-amyloid fibril elongation,. Anal Biochem 2004, 328:67-75. 10.1016/j.ab.2004.01.014, 15081909.
17. Lomakin A, Chung DS, Benedek GB, Kirschner DA, Teplow DB. On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants,. Proc Natl Acad Sci U S A 1996, 93:1125-1129. 10.1073/pnas.93.3.1125, 40042, 8577726.
18. Lee CC, Nayak A, Sethuraman A, Belfort G, McRae GJ. A three-stage kinetic model of amyloid fibrillation,. Biophys J 2007, 92:3448-3458. 10.1529/biophysj.106.098608, 1853138, 17325005.
19. LeVine H. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution,. Protein Sci 1993, 2:404-410. 10.1002/pro.5560020312, 2142377, 8453378.
20. Nielsen L, Khurana R, Coats A, Frokjaer S, Brange J, Vyas S, Uversky VN, Fink AL. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism,. Biochemistry 2001, 40:6036-6046. 10.1021/bi002555c, 11352739.
21. Agena SM, Bogle IDL, Pessoas FLP. An activity coefficient model for proteins. Biotechnol. Bioeng. 1997, 55:65-71. 10.1002/(SICI)1097-0290(19970705)55:1<65::AID-BIT8>3.0.CO;2-V, 18636445.
22. Levine H. Quantification of beta-sheet amyloid fibril structure with thioflavin T. Methods Enzymol. 1999, 309:274-284. full_text, 10507030.
23. Slusky V, Tamada JA, Klibanov AM, Langer R. Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces. Proc Natl Acad Sci U S A 1991, 88:9377-9381. 10.1073/pnas.88.21.9377, 52720, 1946348.
24. Serio TR, Cashikar AG, Kowal AS, Sawicki GJ, Moslehi JJ, Arnsdorf MF, Lindquist SL. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 2000, 289:1317-1321. 10.1126/science.289.5483.1317, 10958771.
25. Morris AM, Watzky MA, Finke RG. Protein aggregation kinetics, mechanism, and curve-fitting: a review of the literature,. Biochim Biophys Acta 2009, 1794:375-397.
26. Moss MA, Varvel NH, Nichols MR, Reed DK, Rosenberry TL. Nordihydroguaiaretic acid does not disaggregate beta-amyloid(1-40) protofibrils but does inhibit growth arising from direct protofibril association,. Mol Pharmacol. 2004, 66(3):592-600.