메뉴 건너뛰기




Volumn 28, Issue 34, 2012, Pages 12588-12592

Light-Triggered disassembly of amyloid fibrils

Author keywords

[No Author keywords available]

Indexed keywords

AFM; AMYLOID FIBRIL; AMYLOIDOGENIC PEPTIDES; FIBRIL FORMATION; GROWING DEMAND; HIGHER-ORDER STRUCTURE; HYDROPHOBIC INTERACTIONS; HYDROPHOBIC REGIONS; INFRARED SPECTROSCOPIC; LYSINE SIDE CHAINS; NOVEL METHODS; PRIMARY SEQUENCES; SIDE-CHAINS;

EID: 84867518732     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la302626d     Document Type: Article
Times cited : (28)

References (36)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding functional amyloid and human disease
    • Chiti, F.; Dobson, C. M. Protein Misfolding, Functional Amyloid, and Human Disease. Annu. Rev. Biochem. 2006, 75, 333-366.
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 47049100201 scopus 로고    scopus 로고
    • Amyloid Not only pathological agents but also ordered nanomaterials
    • Cherny, I; Gazit, E. Amyloid: Not Only Pathological Agents but Also Ordered Nanomaterials. Angew. Chem., Int. Ed. 2008, 47, 4062-4069.
    • (2008) Angew. Chem., Int. Ed , vol.47 , pp. 4062-4069
    • Cherny, I.1    Gazit, E.2
  • 3
    • 79961211353 scopus 로고    scopus 로고
    • Nanomechanics of functional and pathological amyloid materials
    • Knowles, T. P. J.; Buehler, M. J. Nanomechanics of Functional and Pathological Amyloid Materials. Nat. Nanotechnol. 2011, 6, 469-479.
    • (2011) Nat. Nanotechnol , vol.6 , pp. 469-479
    • Knowles, T.P.J.1    Buehler, M.J.2
  • 4
    • 2942744730 scopus 로고    scopus 로고
    • Amyloid fibrils in biotechnology
    • Waterhouse, S. H.; Gerrard, J. A. Amyloid Fibrils in Biotechnology. Aust. J. Chem. 2004, 57, 519-523.
    • (2004) Aust. J. Chem , vol.57 , pp. 519-523
    • Waterhouse, S.H.1    Gerrard, J.A.2
  • 5
    • 4143141192 scopus 로고    scopus 로고
    • Self-Assembling peptides and proteins for nanotechnological applications
    • Rajagopal, K.; Schneider, J. Self-Assembling Peptides and Proteins for Nanotechnological Applications. Curr. Opin. Struct. Biol. 2004, 14, 480-486.
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 480-486
    • Rajagopal, K.1    Schneider, J.2
  • 6
    • 67549083305 scopus 로고    scopus 로고
    • Production of self-Assembling biomaterials for tissue engineering
    • Kyle, S.; Aggeli, A.; Ingham, E.; McPherson, M. J. Production of Self-Assembling Biomaterials for Tissue Engineering. Trends Biotechnol. 2009, 27, 423-433.
    • (2009) Trends Biotechnol , vol.27 , pp. 423-433
    • Kyle, S.1    Aggeli, A.2    Ingham, E.3    McPherson, M.J.4
  • 7
    • 0034612266 scopus 로고    scopus 로고
    • Extensive neurite outgrowth and active synapse formation on self-Assembling peptide scaffolds
    • Holmes, T. C.; de Lacalle, S.; Su, X.; Liu, G.; Rich, A.; Zhang, S. Extensive Neurite Outgrowth and Active Synapse Formation on Self-Assembling Peptide Scaffolds. Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 6728-6733.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 6728-6733
    • Holmes, T.C.1    De Lacalle, S.2    Su, X.3    Liu, G.4    Rich, A.5    Zhang, S.6
  • 10
    • 84867200449 scopus 로고    scopus 로고
    • Photoinduced fibrils formation of chicken egg white lysozyme under native conditions
    • just accepted DOI: 10.1002/prot.24132
    • Xie, J.-B.; Cao, Y.; Pan, H.; Qin, M.; Yan, Z.-Q.; Xiong, X.; Wang, W. Photoinduced Fibrils Formation of Chicken Egg White Lysozyme under Native Conditions. Proteins 2012, just accepted (DOI: 10.1002/prot.24132.
    • (2012) Proteins
    • Xie, J.-B.1    Cao, Y.2    Pan, H.3    Qin, M.4    Yan, Z.-Q.5    Xiong, X.6    Wang, W.7
  • 13
    • 77956244990 scopus 로고    scopus 로고
    • Precision control of cellular pathways with light
    • Lemke, E. A. Precision Control of Cellular Pathways with Light. ChemBioChem 2010, 11, 1825-1827.
    • (2010) ChemBioChem , vol.11 , pp. 1825-1827
    • Lemke, E.A.1
  • 14
    • 77955844090 scopus 로고    scopus 로고
    • Recent advances in the photochemical control of protein function
    • Riggsbee, C. W.; Deiters, A. Recent Advances in the Photochemical Control of Protein Function. Trends Biotechnol. 2010, 28, 468-475.
    • (2010) Trends Biotechnol , vol.28 , pp. 468-475
    • Riggsbee, C.W.1    Deiters, A.2
  • 15
    • 33746734322 scopus 로고    scopus 로고
    • Biologically active molecules with a light switch
    • Mayer, G.; Heckel, A. Biologically Active Molecules with a "Light Switch". Angew. Chem., Int. Ed. 2006, 45, 4900-4921.
    • (2006) Angew. Chem., Int. Ed , vol.45 , pp. 4900-4921
    • Mayer, G.1    Heckel, A.2
  • 16
    • 28844449157 scopus 로고    scopus 로고
    • Light-Activated hydrogel formation via the triggered folding and self-Assembly of a designed peptide
    • Haines, L. A.; Rajagopal, K.; Ozbas, B.; Salick, D. A.; Pochan, D. J.; Schneider, J. P. Light-Activated Hydrogel Formation via the Triggered Folding and Self-Assembly of a Designed Peptide. J. Am. Chem. Soc. 2005, 127, 17025-17029.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 17025-17029
    • Haines, L.A.1    Rajagopal, K.2    Ozbas, B.3    Salick, D.A.4    Pochan, D.J.5    Schneider, J.P.6
  • 17
    • 33750430630 scopus 로고    scopus 로고
    • Generic hydrophobic residues are sufficient to promote aggregation of the alzheimer's a42 peptide
    • Kim, W.; Hecht, M. H. Generic Hydrophobic Residues are Sufficient to Promote Aggregation of the Alzheimer's A42 Peptide. Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 15824-15829.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 15824-15829
    • Kim, W.1    Hecht, M.H.2
  • 18
    • 0034649352 scopus 로고    scopus 로고
    • Amyloid fibril formation by a16-22, a seven-residues fragment of the alzheimer's-Amyloid peptide, and structural characterization by solid state nmr
    • Balbach, J. J.; Ishii, Y.; Antzukin, O. N.; Leapman, R. D.; Rizzo, N. W.; Dyda, F.; Reed, J.; Tycko, R. Amyloid Fibril Formation by A16-22, a Seven-Residues Fragment of the Alzheimer's-Amyloid Peptide, and Structural Characterization by Solid State NMR. Biochemistry 2000, 39, 13748-13759.
    • (2000) Biochemistry , vol.39 , pp. 13748-13759
    • Balbach, J.J.1    Ishii, Y.2    Antzukin, O.N.3    Leapman, R.D.4    Rizzo, N.W.5    Dyda, F.6    Reed, J.7    Tycko, R.8
  • 19
    • 0027529269 scopus 로고
    • Synthesis of na-fmoc-ne-nvoc-lysine and use in the preparation of selectively functionalized peptides
    • Rusiecki, V. K.; Warne, S. A. Synthesis of Na-Fmoc-Ne-Nvoc-Lysine and Use in the Preparation of Selectively Functionalized Peptides. Bioorg. Med. Chem. Lett. 1993, 3, 707-710.
    • (1993) Bioorg. Med. Chem. Lett , vol.3 , pp. 707-710
    • Rusiecki, V.K.1    Warne, S.A.2
  • 20
    • 34447629532 scopus 로고    scopus 로고
    • Prediction of molar extinction coefficients of proteins and peptides using uv absorption of the constituent amino acids at 214 nm to enable quantitative reverse phase high-performance liquid chromatography-mass spectrometry analysis
    • Kuipers, B. J. H.; Gruppen, H. Prediction of Molar Extinction Coefficients of Proteins and Peptides Using UV Absorption of the Constituent Amino Acids at 214 nm to Enable Quantitative Reverse Phase High-Performance Liquid Chromatography-Mass Spectrometry Analysis. J. Agric. Food Chem. 2007, 55, 5445-5451.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 5445-5451
    • Kuipers, B.J.H.1    Gruppen, H.2
  • 21
    • 61949248657 scopus 로고    scopus 로고
    • Effect of dehydration on the aggregation kinetics of two amyloid peptides
    • Mukherjee, S.; Chowdhury, R.; Gai, F. Effect of Dehydration on the Aggregation Kinetics of Two Amyloid Peptides. J. Phys. Chem. B 2009, 113, 531-535.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 531-535
    • Mukherjee, S.1    Chowdhury, R.2    Gai, F.3
  • 22
    • 17444378611 scopus 로고    scopus 로고
    • Dynamics of amide-i modes of the alanine dipeptide in d2o
    • Kim, Y. S.; Hochstrasser, R. M. Dynamics of Amide-I Modes of the Alanine Dipeptide in D2O. J. Phys. Chem. B 2005, 109, 6884-6891.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 6884-6891
    • Kim, Y.S.1    Hochstrasser, R.M.2
  • 23
    • 77955785224 scopus 로고    scopus 로고
    • Differential effects of phe19 and phe20 on fibril formation by amyloidogenic peptide a16-22 (ac-klvffae-nh2
    • Inouye, H.; Gleason, K. A.; Zhang, D.; Decatur, S. M.; Kirschner, D. A. Differential Effects of Phe19 and Phe20 on Fibril Formation by Amyloidogenic Peptide A16-22 (Ac-KLVFFAE-NH2). Proteins 2010, 78, 2306-2321.
    • (2010) Proteins , vol.78 , pp. 2306-2321
    • Inouye, H.1    Gleason, K.A.2    Zhang, D.3    Decatur, S.M.4    Kirschner, D.A.5
  • 24
    • 0036135139 scopus 로고    scopus 로고
    • A possible role for p-stacking in the self-Assembly of amyloid fibrils
    • Gazit, E. A Possible Role for p-Stacking in the Self-Assembly of Amyloid Fibrils. FASEB J. 2002, 16, 77-83.
    • (2002) FASEB J , vol.16 , pp. 77-83
    • Gazit, E.1
  • 25
    • 0034730203 scopus 로고    scopus 로고
    • Designed protein tetramer zipped together with a hydrophobic alzheimer homology: A structural clue to amyloid assembly
    • Otzen, D. E.; Kristensen, O.; Oliveberg, M. Designed Protein Tetramer Zipped Together with a Hydrophobic Alzheimer Homology: A Structural Clue to Amyloid Assembly. Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 9907-9912.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 9907-9912
    • Otzen, D.E.1    Kristensen, O.2    Oliveberg, M.3
  • 26
    • 0037397705 scopus 로고    scopus 로고
    • Emerging ideas on the molecular basis of protein and peptide aggregation
    • Thirumalai, D.; Klimov, D. K.; Dima, R. I. Emerging Ideas on the Molecular Basis of Protein and Peptide Aggregation. Curr. Opin. Struct. Biol. 2003, 13, 1-14.
    • (2003) Curr. Opin. Struct. Biol , vol.13 , pp. 1-14
    • Thirumalai, D.1    Klimov, D.K.2    Dima, R.I.3
  • 27
    • 0037022563 scopus 로고    scopus 로고
    • Natural-sheet proteins use negative design to avoid edge-To-edge aggregation
    • Richardson, J. S.; Richardson, D. C. Natural-Sheet Proteins Use Negative Design to Avoid Edge-To-Edge Aggregation. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 2754-2759.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2
  • 28
    • 34548165708 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins
    • Barth, A. Infrared Spectroscopy of Proteins. Biochim. Biophys. Acta 2007, 1767, 1073-1101.
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1073-1101
    • Barth, A.1
  • 29
    • 25844493690 scopus 로고    scopus 로고
    • Experimental evidence for the reorganization of-strands within aggregates of the a (16-22) peptide
    • Petty, S. A.; Decatur, S. M. Experimental Evidence for the Reorganization of-Strands within Aggregates of the A (16-22) Peptide. J. Am. Chem. Soc. 2005, 127, 13488-13489.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 13488-13489
    • Petty, S.A.1    Decatur, S.M.2
  • 30
    • 11344272213 scopus 로고    scopus 로고
    • Local amide i mode frequencies and coupling constants in multiple-stranded antiparallel-sheet polypeptides
    • Lee, C.; Cho, M. Local Amide I Mode Frequencies and Coupling Constants in Multiple-Stranded Antiparallel-Sheet Polypeptides. J. Phys. Chem. B 2004, 108, 20391-20407.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 20391-20407
    • Lee, C.1    Cho, M.2
  • 31
    • 77953754754 scopus 로고    scopus 로고
    • Simulation of ir, raman and vcd amide i band profiles of self-Assembled peptides
    • Schweitzer-Stenner, R.; Measey, T. J. Simulation of IR, Raman and VCD Amide I Band Profiles of Self-Assembled Peptides. Spectroscopy 2010, 24, 25-36.
    • (2010) Spectroscopy , vol.24 , pp. 25-36
    • Schweitzer-Stenner, R.1    Measey, T.J.2
  • 32
    • 0031962158 scopus 로고    scopus 로고
    • Structural analysis of alzheimer's b(1-40) amyloid: Protofilament assembly of tubular fibrils
    • Malinchik, S. B; Inouye, H.; Szumowski, K. E.; Kirschner, D. A. Structural Analysis of Alzheimer's b(1-40) Amyloid: Protofilament Assembly of Tubular Fibrils. Biophys. J. 1998, 74, 537-545.
    • (1998) Biophys. J , vol.74 , pp. 537-545
    • Malinchik, S.B.1    Inouye, H.2    Szumowski, K.E.3    Kirschner, D.A.4
  • 34
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J.; Selkoe, D. J. The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to Therapeutics. Science 2002, 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 35
    • 84865098074 scopus 로고    scopus 로고
    • Caged intracellular nmda receptor blockers for the study of subcellular ion channel function
    • Reeve, J. E.; Kohl, M. M.; Rodríguez-Moreno, A.; Paulsen, O.; Anderson, H. L. Caged Intracellular NMDA Receptor Blockers for the Study of Subcellular Ion Channel Function. Commun. Integr. Biol. 2012, 5, 240-242.
    • (2012) Commun. Integr. Biol , vol.5 , pp. 240-242
    • Reeve, J.E.1    Kohl, M.M.2    Rodríguez-Moreno, A.3    Paulsen, O.4    Anderson, H.L.5
  • 36
    • 77951236321 scopus 로고    scopus 로고
    • Beyond the canonical 20 amino acids: Expanding the genetic lexicon
    • Young, T. S.; Schultz, P. G. Beyond the Canonical 20 Amino Acids: Expanding the Genetic Lexicon. J. Biol. Chem. 2010, 285, 11039-11044.
    • (2010) J. Biol. Chem , vol.285 , pp. 11039-11044
    • Young, T.S.1    Schultz, P.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.