메뉴 건너뛰기




Volumn 136, Issue 6, 2012, Pages

Kinetic pathways to peptide aggregation on surfaces: The effects of -sheet propensity and surface attraction

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATE GROWTH; ATOMISTIC SIMULATIONS; COARSE-GRAINED; CRYSTALLOGRAPHIC SYMMETRY; EXPERIMENTAL SYSTEM; FIBRIL FORMATION; HYDROPHOBIC RESIDUES; HYDROPHOBIC SURFACES; KINETIC PATHWAY; MOLECULAR DYNAMICS SIMULATIONS; MULTIPLE PATHWAYS; PEPTIDE AGGREGATION; SHEET FIBRILS;

EID: 84857349978     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.3682986     Document Type: Conference Paper
Times cited : (27)

References (43)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • F. Chiti and C. Dobson, Annu. Rev. Biochem. 75, 333 (2006). 10.1146/annurev.biochem.75.101304.123901 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 4
    • 1342302795 scopus 로고    scopus 로고
    • The interaction of proteins with solid surfaces
    • DOI 10.1016/j.sbi.2003.12.001
    • J. Gray, Curr. Opin. Struct. Biol. 14, 110 (2004). 10.1016/j.sbi.2003.12. 001 (Pubitemid 38249599)
    • (2004) Current Opinion in Structural Biology , vol.14 , Issue.1 , pp. 110-115
    • Gray, J.J.1
  • 5
    • 0141765883 scopus 로고    scopus 로고
    • Fabrication of novel biomaterials through molecular self-assembly
    • DOI 10.1038/nbt874
    • S. Zhang, Nat. Biotechnol. 21, 1171 (2003). 10.1038/nbt874 (Pubitemid 37186173)
    • (2003) Nature Biotechnology , vol.21 , Issue.10 , pp. 1171-1178
    • Zhang, S.1
  • 6
    • 0036897817 scopus 로고    scopus 로고
    • Design of nanostructured biological materials through self-assembly of peptides and proteins
    • DOI 10.1016/S1367-5931(02)00391-5
    • S. Zhang, D. Marini, W. Hwang, and S. Santoso, Curr. Opin. Chem. Biol. 6, 865 (2002). 10.1016/S1367-5931(02)00391-5 (Pubitemid 35449349)
    • (2002) Current Opinion in Chemical Biology , vol.6 , Issue.6 , pp. 865-871
    • Zhang, S.1    Marini, D.M.2    Hwang, W.3    Santoso, S.4
  • 7
    • 34547316314 scopus 로고    scopus 로고
    • 10.1039/b605536m
    • E. Gazit, Chem. Soc. Rev. 36, 1263 (2007). 10.1039/b605536m
    • (2007) Chem. Soc. Rev. , vol.36 , pp. 1263
    • Gazit, E.1
  • 10
    • 36249028919 scopus 로고    scopus 로고
    • edited by G. E. Wnek and G. L. Bowlin (Informa Healthcare USA, Inc., New York), Vol
    • R. Latour, in Encyclopedia of Biomaterials and Biomedical Engineering, edited by, G. E. Wnek, and, G. L. Bowlin, (Informa Healthcare USA, Inc., New York, 2008), Vol. 1, pp. 270-284.
    • (2008) Encyclopedia of Biomaterials and Biomedical Engineering , vol.1 , pp. 270-284
    • Latour, R.1
  • 18
    • 0345688752 scopus 로고    scopus 로고
    • Influence of hydrophobic teflon particles on the structure of amyloid β-peptide
    • DOI 10.1021/bm034151g
    • C. E. Giacomelli and W. Norde, Biomacromolecules 4, 1719 (2003). 10.1021/bm034151g (Pubitemid 37455585)
    • (2003) Biomacromolecules , vol.4 , Issue.6 , pp. 1719-1726
    • Giacomelli, C.E.1    Norde, W.2
  • 19
    • 33747182874 scopus 로고    scopus 로고
    • Ex situ atomic force microscopy analysis of β-amyloid self-assembly and deposition on a synthetic template
    • DOI 10.1021/la0601511
    • C. Ha and C. B. Park, Langmuir 22, 6977 (2006). 10.1021/la0601511 (Pubitemid 44231442)
    • (2006) Langmuir , vol.22 , Issue.16 , pp. 6977-6985
    • Ha, C.1    Park, C.B.2
  • 20
    • 19944406829 scopus 로고    scopus 로고
    • Template-directed self-assembly and growth of insulin amyloid fibrils
    • DOI 10.1002/bit.20486
    • C. Ha and C. B. Park, Biotechnol. Bioeng. 90, 848 (2005). 10.1002/bit.20486 (Pubitemid 40756679)
    • (2005) Biotechnology and Bioengineering , vol.90 , Issue.7 , pp. 848-855
    • Ha, C.1    Park, C.B.2
  • 26
    • 10844230140 scopus 로고    scopus 로고
    • Replica exchange molecular dynamics simulations of amyloid peptide aggregation
    • DOI 10.1063/1.1809588
    • M. Cecchini, F. Rao, M. Seeber, and A. Caflisch, J. Chem. Phys. 121, 10748 (2004). 10.1063/1.1809588 (Pubitemid 40001622)
    • (2004) Journal of Chemical Physics , vol.121 , Issue.21 , pp. 10748-10756
    • Cecchini, M.1    Rao, F.2    Seeber, M.3    Caflisch, A.4
  • 28
    • 84857338104 scopus 로고    scopus 로고
    • See supplementary material at E-JCPSA6-136-004207 for additional plots; a sample visualization of bulk amorphous aggregates binding to the surface; a sample visualization of bulk fibrillar aggregates binding to the surface; and a sample visualization of individual, unaggregated peptides binding to the surface
    • See supplementary material at http://dx.doi.org/10.1063/1.3682986 E-JCPSA6-136-004207 for additional plots; a sample visualization of bulk amorphous aggregates binding to the surface; a sample visualization of bulk fibrillar aggregates binding to the surface; and a sample visualization of individual, unaggregated peptides binding to the surface.
  • 29
    • 61549084018 scopus 로고    scopus 로고
    • 10.1016/j.bpj.2008.09.053
    • C. Davis and M. Berkowitz, Biophys. J. 96, 785 (2009). 10.1016/j.bpj.2008.09.053
    • (2009) Biophys. J. , vol.96 , pp. 785
    • Davis, C.1    Berkowitz, M.2
  • 32
    • 34548788549 scopus 로고    scopus 로고
    • Models of β-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process
    • DOI 10.1529/biophysj.107.110148
    • H. Jang, J. Zheng, and R. Nussinov, Biophys. J. 93, 1938 (2007). 10.1529/biophysj.107.110148 (Pubitemid 47437578)
    • (2007) Biophysical Journal , vol.93 , Issue.6 , pp. 1938-1949
    • Jang, H.1    Zheng, J.2    Nussinov, R.3
  • 33
    • 49649122274 scopus 로고    scopus 로고
    • 10.1021/jp8026513
    • V. Knecht, J. Phys. Chem. B 112, 9476 (2008). 10.1021/jp8026513
    • (2008) J. Phys. Chem. B , vol.112 , pp. 9476
    • Knecht, V.1
  • 34
    • 65549152828 scopus 로고    scopus 로고
    • 10.1111/j.1742-4658.2009.07024.x
    • J. Lemkul and D. Bevan, FEBS J. 276, 3060 (2009). 10.1111/j.1742-4658. 2009.07024.x
    • (2009) FEBS J. , vol.276 , pp. 3060
    • Lemkul, J.1    Bevan, D.2
  • 39
    • 77951290266 scopus 로고    scopus 로고
    • 10.1103/PhysRevLett.104.168105
    • S. Auer and D. Kashchiev, Phys. Rev. Lett. 104, 168105 (2010). 10.1103/PhysRevLett.104.168105
    • (2010) Phys. Rev. Lett. , vol.104 , pp. 168105
    • Auer, S.1    Kashchiev, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.