Replica-Exchange分子動態模擬法研究類澱粉胜肽25-35
嵌入膜與折疊的行為

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曾勝煊(Sheng-Xuan Zeng) 查詢紙本館藏

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論文名稱

Replica-Exchange分子動態模擬法研究類澱粉胜肽25-35 嵌入膜與折疊的行為
(Folding and Membrane Insertion of Amyloid-β Peptide (25-35): A Replica-Exchange Molecular Dynamics Simulation Study )

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摘要(中)

本論文利用平行淬煉分子動態法 (Replica-Exchange molecular dynamics, REMD) 模擬類澱粉蛋白(Aβ)片段- Aβ25-35及其突變物N27A- Aβ25-35折疊及穿膜的機制。Aβ是阿茲海默症的主要病源，Aβ25-35保有和全長A???????類似的特性?具細胞毒性及amphipathicity (N?端具親水性，C?端具疏水性)。模擬中，Aβ25-35是以全原子的方式進行，水相及膜是以implicit model的方式進行，搭配REMD，以達到有效率的空間搜尋效果。
模擬結果顯示，Aβ25-35以疏水性的C?端插入膜的疏水區域，並形成穩定的α-helix構形 (Ala30- Leu34); N?端(Gly25 -Lys28)具極性，分佈在水相及頭基的區域，沒有明顯的二級結構; 結果和NMR決定的結構吻合。此外有一小部份的Aβ25-35越過了能量障礙深入膜的疏水核心區域，但並不是穩定結構。
N27A-Aβ25-35 是將Aβ25-35中極性的Asn取代成疏水性Ala，此一改變使得N27A-Aβ25-35毒性下降。模擬結果顯示，N27A-Aβ25-35 和Aβ25-35具有相似的構形及性質，但N27A-Aβ25-35 的C?端較Aβ25-35更深入膜的疏水區域，α-helix構形往N?端延長且較穩定。
膜變薄效應也會影響Aβ25-35及N27A-Aβ25-35的構形，當膜逐漸變薄時，Aβ25-35及N27A-Aβ25-35會更容易深入膜內，形成較長且穩定的α-helix構形。

摘要(英)

The folding and membrane insertion of the Alzheimer’s amyloid-β(25-35) peptide and the mutate N27A-Aβ(25-35) peptide are explored using replica exchange molecular dynamics(REMD). All the peptide use all atom model and the solvent region (water and water-membrane region) are implicit solvent model This amphiphilic peptide (hydrophilicity in N-terminus , hydrophobicity in C-terminus) is a natural by-product of the Alzheimer’s amyloid-β(1-40) peptide and retains the toxicity of its full-length counterpart as the ability to aggregate into β-sheet rich fibrils.
The simulation result show that Aβ(25-35) insert into the membrane and form the helix structure in C-terminus (Ala30-Leu34);and N-terminus(Gly25-Lys28) are disordered at the water region.Our simulation result agree with the NMR structure.A little portion of structures inser into membrane but the structures are unstable.
N27A-Aβ(25-35) peptide,where Asn27 is repliced by Ala. The mutate peptide shows lower neurotoxicity than the wild type despite its increased hydrophobicity. The simulation result shows N27A-Aβ(25-35) peptide and Aβ(25-35) peptide have similar structure and property, but N27A-Aβ(25-35) peptide can insert into membrane more deeper than Aβ(25-35) and the helix structure form more complete than Aβ(25-35).The membrane thining effect also affect the structure of Aβ(25-35) and N27A-Aβ(25-35). When the membrane become thin,two kind of peptide can insert into membrane easily and form stable α-helix structure.

關鍵字(中)

★ 分子動態模擬
★ 類澱粉蛋白
★ 阿茲海默症

關鍵字(英)

★ molecular dynamics simulation
★ amyloid beta
★ Alzheimer's disease

論文目次

摘要 I
Abstract II
致謝 III
目錄 IV
圖目錄 V
表目錄 VIII
第一章序論 1
第二章文獻回顧 2
2.1簡介 2
2.2 蛋白質折疊原理及機制 3
2.3蛋白質錯誤折疊，聚集到纖維成形的過程 5
2.4阿茲海默症(Alzheimer’s Disease,AD) 7
2.5實驗上測定類澱粉胜肽纖維分子結構 8
2.6類澱粉胜肽Amyloid Beta peptide 11
第三章方法與原理 16
3.1 簡介 16
3.2分子力場(Force Field) 17
3.3分子動態模擬基本原理 22
3.5 Generalized Born 溶劑模型(GB Model) 24
3.6 Replica-Exchange Molecular Dynamics Method(REMD) 28
3.7 Dictionary of Secondary Structure of Proteins (DSSP) 34
3.8分子動態摸擬系統與方法介紹 38
第四章結果與討論 41
4.1模擬Aβ25-35單體在細胞膜的行為 43
4.2模擬N27A-Aβ25-35單體在細胞膜的行為 58
4.3 模擬Aβ25-35單體在膜變薄時構形的變化 66
4.4模擬N27A-Aβ25-35單體在膜變薄時構形的變化 73
第五章總結 78
第六章參考文獻 80

參考文獻

1. C. A. McLean , R. A. Cherny, F. W. Fraser, , M. J. Fuller, K. Smith, A. I. Beyreuther, Bush and C. L. Masters (1999) Soluble pool of A beta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Annals of Neurology. 46, 860-866.
2. W. I. Rosenblum (2002) Structure and location of amyloid beta peptide chains and arrays in Alzheimer's disease:New findings require reevaluation of the amyloid hypothesis and of tests of the hypothesis.Neurobiology of Aging. 23, 225-230.
3. D. M. Walsh , I. Klyubin, J. V. Fadeeva, W. K. Cullen, R. Anwyl, M. S.Wolfe, M. J. Rowan and D. J. Selkoe (2002) Naturally secreted oligomersof amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature. 416, 535-539.
4. R. S. Armen , M. L. DeMarco, D. O. V. Alonso and V. Daggett (2004) Pauling and Corey's alpha-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease. Proceedings of the National Academy of Sciences of the United States of America. 101, 11622-11627.
5. S. L. Bernstein , T. Wyttenbach, A. Baumketner, J. E. Shea, G. Bitan, D. B. Teplow and M. T. Bowers (2005) Amyloid beta-protein: Monomer structure and early aggregation states of A beta 42 and its Pro(19) alloform. Journal of the American Chemical Society. 127, 2075-2084.
6. J. M. Borreguero, B. Urbanc, N. D. Lazo, S. V. Buldyrev, D. B. Teplow an d H. E. Stanley (2005) Folding events i n the 21-30 region ofamyloid-beta-protein (A beta) studied in sili co. Proceedings of the National Academy of Sciences of the United States of America. 102, 6015-6020.
7. M. M. Dedmon , K. Lindorff-Larsen, J. Christodoulou, M. Vendruscolo and C. M. Dobson (2005) Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations. Journal of the American Chemical Society. 127, 476-477.
8. F. Massi and J. E, Straub. (2003) Structural and dynamical analysis of the hydration of the Alzheimer's beta-amyloid peptide.Journal of Computational Chemistry. 24, 143-153.
9. N. G. Sgourakis , Y. L. Yan, S. A. McCallum, C. Y. Wang and A. E. Garcia 130 (2007) The Alzheimer's peptides A beta 40 and 42 adopt distinct conformations in water: A combined MD/NMR study. Journal of Molecular Biology. 368, 1448-1457.
10. A. Barducci , R. Chelli, P. Procacci, V. Schettino, F. L. Gervasio and M. Parrinello (2006) Metadynamics simulation of prion protein: beta-structure stability and the early stages of misfolding. Journal of the American Chemical Society. 128, 2705-2710.
11. W. Han and Y. D. Wu (2005) A strand-loop-strand structure is a possible intermediate in fibril elongation: Long time simulations of amylold-beta peptide (10-35). Journal of the American Chemical Society.127, 15408-15416.
12. N. Haspel , D. Zanuy, B. Y. Ma, H. Wolfson and R. Nussinov (2005) A comparative study of amyloid fibril formation by residues 15-19 of the human calcitonin hormone: A single beta-sheet model with a small hydrophobic core. Journal of Molecular Biology. 345, 1213-1227.
13. A. Huet, and P. Derreumaux (2006) Impact of the mutation A21G (Flemish variant) on Alzheimer's beta-amyloid dimers by molecular dynamics simulations. Biophysical Journal. 91, 3829-3840.
14. F. Massi, D. Klimov, D. Thirumalai and J. E. Straub (2002) Charge states rather than propensity for beta-structure determine enhanced fibrillogenesis in wild-type Alzheimer's beta-amyloid peptide compared to E22Q Dutch mutant. Protein Science. 11, 1639-1647.
15. D. K. Klimov and D. Thirumalai (2003) Dissecting the assembly of A beta(16-22) amyloid peptides into antiparallel beta sheets. Structure. 11, 295-307.
16. A. Melquiond, G. Boucher, N. Mousseau and P. Derreumaux (2005) Following the aggregation of amyloid-forming peptides by computer simulations. Journal of Chemical Physics. 122
17. E. Paci, J. Gsponer, X. Salvatella and M. Vendruscolo (2004) Molecular dynamics studies of the process of amyloid aggregation of peptide fragments of transthyretin. Journal of Molecular Biology. 340, 555-569.
18. S. Santini, N. Mousseau and P. Derreumaux (2004) In silico assembly of Alzheimer's A beta(16-22) peptide into beta-sheets. Journal of the American Chemical Society. 126, 11509-11516.
19. S. Santini, G. H. Wei, N. Mousseau and P. Derreumaux (2004) Pathway complexity of Alzheimer's beta-amyloid A beta(16-22) peptide assembly. Structure. 12, 1245-1255.
20. B. Tarus, J. E. Straub and D. Thirumalai (2005) Probing the initial stage of aggregation of the A beta(10-35)-protein: Assessing the propensity for peptide dimerization. Journal of Molecular Biology. 345, 1141-1156.
21. G. H. Wei, N. Mousseau and P. Derreumaux (2004) Sampling the self-assembly pathways of KFFE hexamers. Biophysical Journal. 87, 3648-3656.
22. C. Wu, H. X. Lei and Y. Duan (2005) Elongation of ordered peptide aggregate of an amyloidogenic hexapeptide NFGAIL observed in molecular dynamics simulations with explicit solvent. Journal of the American Chemical Society. 127, 13530-13537.
23. L. P. Li, T. A. Darden, L. Bartolotti, D. Kominos and L. G. Pedersen (1999) An atomic model for the pleated beta-sheet structure of A beta amyloid protofilaments. Biophysical Journal. 76, 2871-2878.
24. B. Y. Ma, and R. Nussinov (2002) Stabilities and conformations of Alzheimer's beta-amyloid peptide oligomers (A beta(16-22 ') A beta(16-35') and A beta(10-35)): Sequence effects. Proceedings of the National Academy of Sciences of the United States of America. 99, 14126-14131
25. J. H. Meinke and U. H. E. Hansmann (2007) Aggregation of beta-amyloid fragments. Journal of Chemical Physics. 126
26. D. Zanuy, K. Gunasekaran, B. Y. Ma, H. H. Tsai, C. J. Tsai and R.Nussinov (2004) Insights into amyloid structural formation and assembly through computational approaches. Amyloid-Journal of Protein Folding Disorders. 11, 143-161.
27. W. Hwang, S. G. Zhang, R. D. Kamm and M. Karplus (2004) Kinetic control of dimer structure formation in amyloid fibrillogenesis. Proceedings of the National Academy of Sciences of the United States of America. 101, 12916-12921.
28. H. D. Nguyen and C. K. Hall (2005) Kinetics of fibril formation by polyalanine peptides. Journal of Biological Chemistry. 280, 9074-9082
29. A. Baumketner and J. E. Shea (2005) Free energy landscapes for amyloidogenic tetrapeptides dimerization. Biophysical Journal. 89, 1493-1503.
30. M. Cecchini, F. Rao, M. Seeber and A. Caflisch (2004) Replica exchange molecular dynamics simulations of amyloid peptide aggregation. Journal of Chemical Physics. 121, 10748-10756.
31. G. Favrin, A. Irback and S. Mohanty (2004) Oligomerization of amyloid A beta(16-22) peptides using hydrogen bonds and hydrophobicity forces. Biophysical Journal. 87, 3657-3664.
32. S. Gnanakaran, R. Nussinov and A. E. Garcia (2006) Atomic-level description of amyloid beta-dimer formation. Journal of the American Chemical Society. 128, 2158-2159.
33. H. D. Nguyen and C. K. Hall (2006) Spontaneous fibril formation by polyalanines; Discontinuous molecular dynamics simulations. Journal of the American Chemical Society. 128, 1890-1901.
34. H. H. Tsai, M. Reches, C. J. Tsai, K. Gunasekaran, E. Gazit and R.Nussinov (2005) Energy landscape of amyloidogenic peptide oligomerization by parallel-tempering molecular dynamics simulation: Significant role of Asn ladder. Proceedings of the National Academy of Sciences of the United States of America. 102, 8174-8179.
35. B. Urbanc ,L.Cruz, F. Ding, D.Sammond, S.Khare, S.V. Buldyrev, H. E. Stanley and N. V. Dokholyan (2004) Molecular dynamics simulation of amyloid beta dimer formation. Biophysical Journal. 87, 2310-2321.
36. M. Stefani and C. M. Dobson (2003) Protein aggregation and aggregate toxicity:new insights into protein folding, misfolding diseases and biological evolution. Journal of Molecular Medicine-Jmm. 81, 678-699.
37. K. A. Dill and H. S. Chan (1997) From Levinthal to pathways to funnels. Nature Structural Biology. 4,10-19.
38. P. G. Wolynes , J. N. Onuchic and D. Thirumalai (1995)Navigating the Folding Routes. Science. 267, 1619-1620.
39. M. Vendruscolo, E. Paci, C. M. Dobson and M. Karplus (2001) Three key residues form a critical contact network in a protein folding transition state. Nature. 409, 641-645.
40. J. Hardy and D. J. Selkoe (2002) Medicine - The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science. 297, 353-356.
41. R. Kayed, E. Head, J. L. Thompson, T. M. McIntire, S. C. Milton, C. W. Cotman and C. G. Glabe (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science.300,486-489.
42. D. L. Miller, I. A. Papayannopoulos, J. Styles, S. A. Bobin, Y. Y. Lin, K. Biemann and K. Iqbal (1993) Peptide Compositions of the Cerebrovascular and Senile Plaque Core Amyloid Deposits of Alzheimers-Disease. Arch Biochem Biophys. 301, 41-52.
43. M. P. Lambert, A. K. Barlow, B. A. Chromy, C. Edwards, R. Freed, M. Liosatos, T. E. Morgan, I. Rozovsky, B. Trommer, K. L. Viola, P. Wals, C. Zhang, C. E. Finch, G. A. Krafft and W. L. Klein (1998) Diffusible, nonfibrillar ligands derived from A beta(1-42) are potent central nervous system neurotoxins. Proceedings of the National Academy of Sciences of the United States of America.95, 6448-6453
44. D. J. Selkoe (1991) The Molecular Pathology of Alzheimers-Disease. Neuron. 6, 487-498
45. B. Sommer (2002) Alzheimer's disease and the amyloid cascade hypothesis: Ten years on. Current Opinion in Pharmacology. 2, 87-92. 46
46. Y. M. Xing and K. Higuchi (2002) Amyloid fibril proteins. Mechanisms of Ageing and Development. 123, 1625-1636.
47. K. Shoghi-Jadid, J. R. Barrio, V. Kepe, H. M. Wu, G. W. Small, M. E. Phelps and S. C. Huang (2005) Imaging beta-amyloid fibrils in Alzheimer's disease: a critical analysis through simulation of amyloid fibril polymerization. Nucl Med Biol. 32, 337-351.
48. J. D. Buxbaum, K. N. Liu, Y. X. Luo, J. L. Slack, K. L. Stocking, J. J. Peschon, R. S. Johnson, B. J. Castner, D. P. Cerretti and R. A. Black (1998) Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor. Journal of Biological Chemistry. 273, 27765-27767.
49. S. Lammich, E. Kojro, R. Postina, S. Gilbert, R. Pfeiffer, M. Jasionowski, C. Haass and F. Fahrenholz (1999) Constitutive and regulated alpha-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease. Proceedings of the National Academy of Sciences of the United States of America. 96, 3922-3927
50. S. Sinha, J. P. Anderson, R. Barbour, G. S. Basi, R. Caccavello, D. Davis, M. Doan, H. F. Dovey, N. Frigon, J. Hong, K. Jacobson-Croak, N. Jewett, P. Keim, J. Knops, I. Lieberburg, M. Power, H. Tan, G. Tatsuno, J. Tung, D. Schenk, P. Seubert, S. M. Suomensaari, S. W. Wang, D. Walker, J. Zhao, L. McConlogue and V. John (1999) Purification and cloning of amyloid precursor protein beta-secretase from human brain. Nature. 402, 537-540.
51. R. Vassar, B. D. Bennett, S. Babu-Khan, S. Kahn, E. A. Mendiaz, P. Denis, D. B. Teplow, S. Ross, P. Amarante, R. Loeloff, Y. Luo, S. Fisher, L. Fuller, S. Edenson, J. Lile, M. A. Jarosinski, A. L. Biere, E. Curran, T. Burgess, J. C. Louis, F. Collins, J. Treanor, G. Rogers and M. Citron (1999) beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science. 286, 735-741.
52. R. Q. Yan, M. J. Bienkowski, M. E. Shuck, H. Y. Miao, M. C. Tory, A. M. Pauley, J. R. Brashler, N. C. Stratman, W. R. Mathews, A. E. Buhl, D. B. Carter, A. G. Tomasselli, L. A. Parodi, R. L. Heinrikson and M. E. Gurney(1999) Membrane-anchored aspartyl protease with Alzheimer's disease beta-secretase activity. Nature. 402, 533-537.
53. B. De Strooper, P. Saftig, K. Craessaerts, H. Vanderstichele, G. Guhde, W. Annaert, K. Von Figura and F. Van Leuven (1998) Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature. 391, 387-390.
54. P. T. Lansbury, P. R. Costa, J. M. Griffiths, E. J. Simon, M. Auger, K. J. Halverson, D. A. Kocisko, Z. S. Hendsch, T. T. Ashburn, R. G. S. Spencer, B. Tidor and R. G. Griffin (1995) Structural Model for the Beta-Amyloid Fibril Based on Interstrand Alignment of an ntiparallel-Sheet Comprising a C-Terminal Peptide. Nature Structural Biology. 2, 990-998
55. T. L. S. Benzinger, D. M. Gregory, T. S. Burkoth, H. Miller-Auer, D. G. Lynn, R. E. Botto and S. C. Meredith (1998) Propagating structure of Alzheimer's beta-amyloid(10-35) is parallel beta-sheet with residues in exact register. Proceedings of the National Academy of Sciences of the United States of America. 95, 13407-13412.
56. R. Tycko, A. Petkova, N. Oyler, C. C. Chan and J. Balbach (2002) Probing the molecular structure of amyloid fibrils with solid state NMR. Biophysical Journal. 82, 187a-187a.
57. A. Der-Sarkissian, C. C. Jao, J. Chen and R. Langen (2003) Structural organization of alpha-synuclein fibrils studied by site-directed spin labeling. Journal of Biological Chemistry. 278, 37530-37535.
58. M. Torok, S. Milton, R. Kayed, P. Wu, T. McIntire, C. G. Glabe and R. Langen (2002) Structural and dynamic features of Alzheimer's A beta peptide in amyloid fibrils studied by site-directed spin labeling. Journal of Biological Chemistry. 277, 40810 -40815.
59. O. S. Makin, E. Atkins, P. Sikorski, J. Johansson and L. C. Serpell (2005) Molecular basis for amyloid fibril formation and stability. Proceedings of the National Academy of Sciences of the United States of America. 102, 315-320.
60. P. P. Mager, B. Penke, R. Walter, T. Harkany and W. Hartig (2002) Pathological peptide folding in Alzheimer's disease and other conformational disorders. Curr Med Chem. 9, 1763-1780.
61. C. D. Snow, N. Nguyen, V. S. Pande and M. Gruebele (2002) Absolute comparison of simulated and experimental protein-folding dynamics. Nature. 420, 102-106.
62. R. H. Zhou (2003) Trp-cage: Folding free energy landscape in explicit water. Proceedings of the National Academy of Sciences of the United States of America. 100, 13280-13285.
63. D. K. Klimov, J. E. Straub and D. Thirumalai (2004) Aqueous urea solution destabilizes A beta(16-22) oligomers. Proceedings of the National Academy of Sciences of the United States of America. 101, 14760-14765.
64. H. D. Nguyen and C. K. Hall (2004) Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides. Proceedings of the National Academy of Sciences of the United States of America. 101, 16180-16185.
65. Y. C. Xu, J. J. Shen, X. M. Luo, W. L. Zhu, K. X. Chen, J. P. Ma and H. L. Jiang (2005) Conformational transition of amyloid beta-peptide. Proceedings of the National Academy of Sciences of the United States of America. 102, 5403-5407.
66. C. J. Barrow, A. Yasuda, P. T. M. Kenny and M. G. Zagorski (1992) Solution Conformations and Aggregational Properties of Synthetic Amyloid Beta-Peptides of Alzheimers-Disease – Analysis of Circular-Dichroism Spectra. Journal of Molecular Biology. 225, 1075-1093.
67. M. Coles, W. Bicknell, A. A. Watson, D. P. Fairlie and D. J. Craik (1998) Solution structure of amyloid beta-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is? Biochemistry. 37, 11064-11077.
68. H. Y. Shao, S. C. Jao, K. Ma and M. G. Zagorski (1999) Solution structures of micelle-bound amyloid beta-(1-40) and beta-(1-42) peptides of Alzheimer's disease. Journal of Molecular Biology. 285, 755-773.
69. C. Soto, E. M. Castano, B. Frangione and N. C. Inestrosa (1995) The Alpha-Helical to Beta-Strand Transition in the Amino-Terminal Fragment of the Amyloid Beta-Peptide Modulates Amyloid Formation. Journal of Biological Chemistry. 270, 3063-3067
70. H. Sticht, P. Bayer, D. Willbold, S. Dames, C. Hilbich, K. Beyreuther, R. W. Frank and P. Rosch (1995) Structure of Amyloid A4-(1-40)-Peptide of Alzheimers-Disease. European Journal of Biochemistry. 233, 293-298.
71. C. J. Barrow and M. G. Zagorski (1991) Solution Structures of Beta Peptide and Its Constituent Fragments - Relation to Amyloid Deposition. Science. 253, 179-182.
72. T. A. Good and R. M. Murphy (1995) Aggregation State-Dependent Binding of Beta-Amyloid Peptide to Protein and Lipid Components of Rat Cortical Homogenates. Biochemical and Biophysical Research Communications. 207, 209-215.
73. L. C. Serpell (2000) Alzheimer's amyloid fibrils: structure and assembly. Bba-Mol Basis Dis. 1502, 16-30.
74. T. Kohno Kobayashi K, Maeda T, Sato K, Takashima A. Three-dimensional structures of the amyloid beta peptide (25-35) in membrane-mimicking environment. Biochemistry. 1996 Dec 17;35(50):16094–16104
75. S. Dante, T. Hauss, and N. A. Dencher. 2002. β-Amyloid 25 to 35 is intercalated in anionic and zwitterionic lipid membranes to different extents. Biophys. J. 83:2610–2616.
76. Amyloid beta protein-induced irreversible current in rat cortical neurons Neuroreport,5(16),(1994),2016-2018 Furukawa K, Abe Y, Akaike N
77. Nguyen, P. H., M. S. Li, G. Stock, J. E. Straub and D. Thirumalai (2007) Monomer adds to preformed structured oligomers of A beta-peptides by a two-stage dock-lock mechanism. Proceedings of the National Academy of Sciences of the United States of America. 104, 111-116.
78. M. Buck, S. Bouguet-Bonnet, R. W. Pastor and A. D. MacKerell (2006) Importance of the CMAP correction to the CHARMM22 protein force field: Dynamics of hen lysozyme. Biophysical Journal. 90, L36-L38.
79. T. Lazaridis and M. Karplus (1999) Effective energy function for proteins in solution. Proteins-Structure Function and Genetics. 35, 133-152.
80. M. Schaefer and M. Karplus (1996) A comprehensive analytical treatment of continuum electrostatics. Journal of Physical Chemistry. 100, 1578-1599.
81. W. C. Still, A. Tempczyk, R. C. Hawley and T. Hendrickson (1990) Semianalytical Treatment of Solvation for Molecular Mechanics and Dynamics. Journal of the American Chemical Society. 112, 6127-6129.
82. M. Feig, A. Onufriev, M. S. Lee, W. Im, D. A. Case and C. L. Brooks (2004) Performance comparison of generalized born and Poisson methods in the calculation of electrostatic solvation energies for protein structures. Journal of Computational Chemistry. 25, 265-284.
83. Y. Sugita, and Y. Okamoto (1999) Replica-exchange molecular dynamics method for protein folding. Chemical Physics Letters. 314, 141-151.
84. S. Dante, T. Hauss and N. A. Dencher (2002) beta-amyloid 25 to 35 is intercalated in anionic and zwitterionic lipid membranes to different extents. Biophysical Journal. 83, 2610-2616.
85. C. Esposito, A. Tedeschi, M. Scrima, G. D'Errico, M. F. Ottaviani, P. Rovero and A. M. D'Ursi (2006) Exploring interaction of beta-amyloid segment (25-35) with membrane models through paramagnetic probes. Journal of Peptide Science. 12, 766-774.
86. A. M. D'Ursi, M. R. Armenante, R. Guerrini, S. Salvadori, G. Sorrentino, and D. Picone. 2004. Solution structure of amyloid beta-peptide (25-35) in different media. J. Med. Chem. 47:4231-4238.
87. H. Jang, B. Ma, T. B. Woolf, and R. Nussinov. 2006. Interaction of protegrin-1 with lipid bilayers: Membrane thinning effect. Biophys. J. 91:2848-2859.

指導教授

蔡惠旭(Hui-Hsu Gavin Tsai)

審核日期

2009-10-15

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