Salts drive controllable multilayered upright assembly of amyloid-like peptides at mica/water interface

Proceedings of the National Academy of Sciences of the United States of America

Volumn 110, Issue 21, 2013, Pages 8543-8548

  Dai, Bin ^a,b   Kang, Seung Gu ^c   Huynh, Tien ^c   Lei, Haozhi ^a   Castelli, Matteo ^c   Hu, Jun ^a   Zhang, Yi ^a   Zhou, Ruhong ^c,d  

^a SHANGHAI INSTITUTE OF APPLIED PHYSICS   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

^c IBM T J WATSON RESEARCH CENTER   (United States)

^d Columbia University ^*  (United States)

Author keywords

Amyloid peptide; Atomic force microscopy; Salt effect; Self assembly on mica

Indexed keywords

AMYLOID PROTEIN; INORGANIC SALT; MICA; NANOMATERIAL; WATER;

ARTICLE; ATOM; ATOMIC FORCE MICROSCOPY; BETA SHEET; CONCENTRATION RESPONSE; CONTROLLED STUDY; IONIC STRENGTH; MICROENVIRONMENT; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; SURFACE PROPERTY; TUNING CURVE;

AMYLOID PEPTIDE; ATOMIC FORCE MICROSCOPY; SALT EFFECT; SELF-ASSEMBLY ON MICA;

AMYLOIDOGENIC PROTEINS; HUMANS; MAGNESIUM CHLORIDE; NANOSTRUCTURES; OLIGOPEPTIDES; PROTEIN STRUCTURE, SECONDARY;

EID: 84878153018     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1220711110     Document Type: Article

References (55)

1. Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75: 333-366.
2. Zhang S (2003) Building from the bottom up. Mater Today 6(5): 20-27.
3. Cherny I, Gazit E (2008) Amyloids: Not only pathological agents but also ordered nanomaterials. Angew Chem Int Ed Engl 47(22): 4062-4069.
4. Dong H, Paramonov SE, Aulisa L, Bakota EL, Hartgerink JD (2007) Self-assembly of multidomain peptides: Balancing molecular frustration controls conformation and nanostructure. J Am Chem Soc 129(41): 12468-12472.
5. Kammerer RA, et al. (2004) Exploring amyloid formation by a de novo design. Proc Natl Acad Sci USA 101(13): 4435-4440.
6. Zimenkov Y, et al. (2006) Rational design of a reversible pH-responsive switch for peptide self-assembly. J Am Chem Soc 128(21): 6770-6771.
7. Zhang F, et al. (2006) Epitaxial growth of peptide nanofilaments on inorganic surfaces: Effects of interfacial hydrophobicity/hydrophilicity. Angew Chem Int Ed Engl 45(22): 3611-3613.
8. Kowalewski T, Holtzman DM (1999) In situ atomic force microscopy study of Alzheimer's beta-amyloid peptide on different substrates: New insights into mechanism of beta-sheet formation. Proc Natl Acad Sci USA 96(7): 3688-3693.
9. Whitehouse C, et al. (2005) Adsorption and self-assembly of peptides on mica substrates. Angew Chem Int Ed Engl 44(13): 1965-1968.
10. Hoyer WG, Cherny D, Subramaniam V, Jovin TM (2004) Rapid self-assembly of alphasynuclein observed by in situ atomic force microscopy. J Mol Biol 340(1): 127-139.
11. Zhu M, Souillac PO, Ionescu-Zanetti C, Carter SA, Fink AL (2002) Surface-catalyzed amyloid fibril formation. J Biol Chem 277(52): 50914-50922.
12. Pettersson T, Konttinen YT (2010) Amyloidosis-recent developments. Semin Arthritis Rheum 39(5): 356-368.
13. Jelinek R, Sheynis T (2010) Amyloid-membrane interactions: Experimental approaches and techniques. Curr Protein Pept Sci 11(5): 372-384.
14. Kinnunen PKJ (2009) Amyloid formation on lipid membrane surfaces. Open Biol J 2: 163-175.
15. So CR, et al. (2012) Controlling self-assembly of engineered peptides on graphite by rational mutation. ACS Nano 6(2): 1648-1656.
16. Kellermayer MSZ, Karsai A, Benke M, Soós K, Penke B (2008) Stepwise dynamics of epitaxially growing single amyloid fibrils. Proc Natl Acad Sci USA 105(1): 141-144.
17. Necula M, Chirita CN, Kuret J (2003) Rapid anionic micelle-mediated alpha-synuclein fibrillization in vitro. J Biol Chem 278(47): 46674-46680.
18. Du HN, et al. (2006) Acceleration of alpha-synuclein aggregation by homologous peptides. FEBS Lett 580(15): 3657-3664.
19. Munishkina LA, Henriques J, Uversky VN, Fink AL (2004) Role of protein-water interactions and electrostatics in alpha-synuclein fibril formation. Biochemistry 43(11): 3289-3300.
20. Raman B, et al. (2005) Critical balance of electrostatic and hydrophobic interactions is required for beta 2-microglobulin amyloid fibril growth and stability. Biochemistry 44(4): 1288-1299.
21. Pedersen JS, Flink JM, Dikov D, Otzen DE (2006) Sulfates dramatically stabilize a saltdependent type of glucagon fibrils. Biophys J 90(11): 4181-4194.
22. Klement K, et al. (2007) Effect of different salt ions on the propensity of aggregation and on the structure of Alzheimer's abeta(1-40) amyloid fibrils. J Mol Biol 373(5): 1321-1333.
23. Hwang W, et al. (2009) Surface Induced nanofiber growth by self-assembly of a silkelastin- like protein polymer. Langmuir 25(21): 12682-12686.
24. Jain S, Udgaonkar JB (2010) Salt-induced modulation of the pathway of amyloid fibril formation by the mouse prion protein. Biochemistry 49(35): 7615-7624.
25. Kang SG, et al. (2012) Molecular mechanism of surface-assisted epitaxial self-assembly of amyloid-like peptides. ACS Nano 6(10): 9276-9282.
26. Kang SG, et al. (2013) Hydrophobic interaction drives surface-assisted epitaxial assembly of amyloid-like peptides. J Am Chem Soc 135(8): 3150-3157.
27. Zhang F-C, et al. (2010) Mechanical manipulation assisted self-assembly to achieve defect repair and guided epitaxial growth of individual peptide nanofilaments. ACS Nano 4(10): 5791-5796.
28. Jarzynski C (1997) Nonequilibrium equality for free energy differences. Phys Rev Lett 78(14): 2690-2693.
29. Park S, Khalili-Araghi F, Tajkhorshid E, Schulten K (2003) Free energy calculation from steered molecular dynamics simulations using Jarzynski's equality. J Chem Phys 119(6): 3559-3566.
30. Tarus B, Straub JE, Thirumalai D (2008) Structures and free-energy landscapes of the wild type and mutants of the Abeta(21-30) peptide are determined by an interplay between intrapeptide electrostatic and hydrophobic interactions. J Mol Biol 379(4): 815-829.
31. Tarus B, Straub JE, Thirumalai D (2006) Dynamics of Asp23-Lys28 salt-bridge formation in Abeta10-35 monomers. J Am Chem Soc 128(50): 16159-16168.
32. Arosio P, Jaquet B, Wu H, Morbidelli M (2012) On the role of salt type and concentration on the stability behavior of a monoclonal antibody solution. Biophys Chem 168-169: 19-27.
33. Cerf E, et al. (2009) Antiparallel beta-sheet: A signature structure of the oligomeric amyloid beta-peptide. Biochem J 421(3): 415-423.
34. Osman MA, Suter UW (2000) Determination of the cation-exchange capacity of muscovite mica. J Colloid Interface Sci 224(1): 112-115.
35. Nock S, Spudich JA, Wagner P (1997) Reversible, site-specific immobilization of polyarginine- tagged fusion proteins on mica surfaces. FEBS Lett 414(2): 233-238.
36. Xu L, Salmeron M (1998) Effects of surface ions on the friction and adhesion properties of mica. Langmuir 14(8): 2187-2190.
37. Xu L, Salmeron M (1998) An XPS and scanning polarization force microscopy study of the exchange and mobility of surface ions on mica. Langmuir 14(20): 5841-5844.
38. Osman MA, Moor C, Caseri WR, Suter UW (1999) Alkali Metals Ion Exchange on Muscovite Mica. J Colloid Interface Sci 209(1): 232-239.
39. van der Linden E, Venema P (2007) Self-assembly and aggregation of proteins. Curr Opin Colloid Interface Sci 12(4-5): 158-165.
40. Cygan RT, Liang JJ, Kalinichev AG (2004) Molecular models of hydroxide, oxyhydroxide, and clay phases and the development of a general force field. J Phys Chem B 108(4): 1255-1266.
41. Kuwahara Y (1999) Muscovite surface structure imaged by fluid contact mode AFM. Phys Chem Miner 26(3): 198-205.
42. Loewenstein W (1954) The distribution of aluminum in the tetrahedra of silicates and aluminates. Am Mineral 39(1-2): 92-96.
43. Jorgensen WL, Chandrasekhar J, Madura JD, Impey RW, Klein ML (1983) Comparison of simple potential functions for simulating liquid water. J Chem Phys 79(2): 926-935.
44. Phillips JC, et al. (2005) Scalable molecular dynamics with NAMD. J Comput Chem 26(16): 1781-1802.
45. Kumar S, et al. (2008) Scalable molecular dynamics with NAMD on the IBM Blue Gene/ L system. IBM J Res Develop 52(1-2): 177-188.
46. Brooks CL, 3rd, Onuchic JN, Wales DJ (2001) Statistical thermodynamics. Taking a walk on a landscape. Science 293(5530): 612-613.
47. Snow CD, Nguyen H, Pande VS, Gruebele M (2002) Absolute comparison of simulated and experimental protein-folding dynamics. Nature 420(6911): 102-106.
48. Zhou R, Berne BJ (2002) Can a continuum solvent model reproduce the free energy landscape of a beta-hairpin folding in water? Proc Natl Acad Sci USA 99(20): 12777-12782.
49. Zhou R, Eleftheriou M, Royyuru AK, Berne BJ (2007) Destruction of long-range interactions by a single mutation in lysozyme. Proc Natl Acad Sci USA 104(14): 5824-5829.
50. Hua L, Zhou R, Thirumalai D, Berne BJ (2008) Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding. Proc Natl Acad Sci USA 105(44): 16928-16933.
51. Ge C, et al. (2011) Binding of blood proteins to carbon nanotubes reduces cytotoxicity. Proc Natl Acad Sci USA 108(41): 16968-16973.
52. Kang SG, et al. (2012) Molecular mechanism of pancreatic tumor metastasis inhibition by Gd@C82(OH)22 and its implication for de novo design of nanomedicine. Proc Natl Acad Sci USA 109(38): 15431-15436.
53. Xia Z, Das P, Shakhnovich EI, Zhou R (2012) Collapse of unfolded proteins in a mixture of denaturants. J Am Chem Soc 134(44): 18266-18274.
54. Darden T, York D, Pedersen L (1993) Particle mesh Ewald: An Nlog(N) method for Ewald sums in large systems. J Chem Phys 98(12): 10089-10092.
55. MacKerell AD, et al. (1998) All-atom empirical potential for molecular modeling and dynamics studies of proteins. J Phys Chem B 102(18): 3586-3616.