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Volumn 7, Issue 14, 2016, Pages 2758-2764

Structural and Mechanical Properties of Amyloid Beta Fibrils: A Combined Experimental and Theoretical Approach

Author keywords

[No Author keywords available]

Indexed keywords

ATOMIC FORCE MICROSCOPY; ELASTIC MODULI; GLYCOPROTEINS; MECHANICAL PROPERTIES; MOLECULAR DYNAMICS; STRAIN; STRESSES;

EID: 84979642904     PISSN: None     EISSN: 19487185     Source Type: Journal    
DOI: 10.1021/acs.jpclett.6b01066     Document Type: Article
Times cited : (28)

References (75)
  • 2
    • 84976907240 scopus 로고    scopus 로고
    • Mechanisms by Which Acellular Biologic Scaffolds Promote Functional Skeletal Muscle Restoration
    • Badylak, S. F.; Dziki, J. L.; Sicari, B. M.; Ambrosio, F.; Boninger, M. L. Mechanisms by Which Acellular Biologic Scaffolds Promote Functional Skeletal Muscle Restoration Biomaterials 2016, 103, 128-136 10.1016/j.biomaterials.2016.06.047
    • (2016) Biomaterials , vol.103 , pp. 128-136
    • Badylak, S.F.1    Dziki, J.L.2    Sicari, B.M.3    Ambrosio, F.4    Boninger, M.L.5
  • 5
    • 84983577457 scopus 로고    scopus 로고
    • Decellularized Scaffolds Containing Hyaluronic Acid and EGF for Promoting the Recovery of Skin Wounds
    • Wu, Z.; Tang, Y.; Fang, H.; Su, Z.; Xu, B.; Lin, Y.; Zhang, P.; Wei, X. Decellularized Scaffolds Containing Hyaluronic Acid and EGF for Promoting the Recovery of Skin Wounds J. Mater. Sci.: Mater. Med. 2015, 26, 1-10 10.1007/s10856-014-5322-1
    • (2015) J. Mater. Sci.: Mater. Med. , vol.26 , pp. 1-10
    • Wu, Z.1    Tang, Y.2    Fang, H.3    Su, Z.4    Xu, B.5    Lin, Y.6    Zhang, P.7    Wei, X.8
  • 6
    • 84928041053 scopus 로고    scopus 로고
    • Self Healing Hydrogels Composed of Amyloid Nano Fibrils for Cell Culture and Stem Cell Differentiation
    • Jacob, R. S. et al. Self Healing Hydrogels Composed of Amyloid Nano Fibrils for Cell Culture and Stem Cell Differentiation Biomaterials 2015, 54, 97-105 10.1016/j.biomaterials.2015.03.002
    • (2015) Biomaterials , vol.54 , pp. 97-105
    • Jacob, R.S.1
  • 7
    • 84860315046 scopus 로고    scopus 로고
    • Nanomaterials: Amyloids Reflect Their Brighter Side
    • Mankar, S.; Anoop, A.; Sen, S.; Maji, S. K. Nanomaterials: Amyloids Reflect Their Brighter Side Nano Rev. 2011, 2, 6032 10.3402/nano.v2i0.6032
    • (2011) Nano Rev. , vol.2 , pp. 6032
    • Mankar, S.1    Anoop, A.2    Sen, S.3    Maji, S.K.4
  • 9
    • 84969705951 scopus 로고    scopus 로고
    • Biocompatibility Evaluation of Tissue-engineered Decellularized Scaffolds for Biomedical Application
    • Hussein, K. H.; Park, K.-M.; Kang, K.-S.; Woo, H.-M. Biocompatibility Evaluation of Tissue-engineered Decellularized Scaffolds for Biomedical Application Mater. Sci. Eng., C 2016, 67, 766-778 10.1016/j.msec.2016.05.068
    • (2016) Mater. Sci. Eng., C , vol.67 , pp. 766-778
    • Hussein, K.H.1    Park, K.-M.2    Kang, K.-S.3    Woo, H.-M.4
  • 10
    • 84885692358 scopus 로고    scopus 로고
    • Self-Assembled Synthetic Protein Scaffolds: Biosynthesis and Applications
    • Su, W. W.; Han, Z. Self-Assembled Synthetic Protein Scaffolds: Biosynthesis and Applications ECS Trans. 2013, 50, 23-29 10.1149/05028.0023ecst
    • (2013) ECS Trans. , vol.50 , pp. 23-29
    • Su, W.W.1    Han, Z.2
  • 11
    • 84976254425 scopus 로고    scopus 로고
    • Cytochrome c Peroxidase Activity of Heme Bound Amyloid β Peptides
    • Seal, M.; Ghosh, C.; Basu, O.; Dey, S. G. Cytochrome c Peroxidase Activity of Heme Bound Amyloid β Peptides JBIC, J. Biol. Inorg. Chem. 2016, 1-8 10.1007/s00775-016-1367-6
    • (2016) JBIC, J. Biol. Inorg. Chem. , pp. 1-8
    • Seal, M.1    Ghosh, C.2    Basu, O.3    Dey, S.G.4
  • 12
    • 84959290333 scopus 로고    scopus 로고
    • Stability of Transient Cu+Aβ (1-16) Species and Influence of Coordination and Peptide Configuration on Superoxide Formation
    • Mirats, A.; Alí-Torres, J.; Rodríguez-Santiago, L.; Sodupe, M. Stability of Transient Cu+Aβ (1-16) Species and Influence of Coordination and Peptide Configuration on Superoxide Formation Theor. Chem. Acc. 2016, 135, 1-9 10.1007/s00214-016-1836-6
    • (2016) Theor. Chem. Acc. , vol.135 , pp. 1-9
    • Mirats, A.1    Alí-Torres, J.2    Rodríguez-Santiago, L.3    Sodupe, M.4
  • 13
    • 84955486200 scopus 로고    scopus 로고
    • Towards Prebiotic Catalytic Amyloids Using High Throughput Screening
    • Friedmann, M. P.; Torbeev, V.; Zelenay, V.; Sobol, A.; Greenwald, J.; Riek, R. Towards Prebiotic Catalytic Amyloids Using High Throughput Screening PLoS One 2015, 10, e0143948 10.1371/journal.pone.0143948
    • (2015) PLoS One , vol.10 , pp. e0143948
    • Friedmann, M.P.1    Torbeev, V.2    Zelenay, V.3    Sobol, A.4    Greenwald, J.5    Riek, R.6
  • 14
    • 84952837600 scopus 로고    scopus 로고
    • Hybrid Amyloid Membranes for Continuous Flow Catalysis
    • Bolisetty, S.; Arcari, M.; Adamcik, J.; Mezzenga, R. Hybrid Amyloid Membranes for Continuous Flow Catalysis Langmuir 2015, 31, 13867-13873 10.1021/acs.langmuir.5b03205
    • (2015) Langmuir , vol.31 , pp. 13867-13873
    • Bolisetty, S.1    Arcari, M.2    Adamcik, J.3    Mezzenga, R.4
  • 17
    • 84957900711 scopus 로고    scopus 로고
    • Self-Catalyzed Assembly of Peptide Scaffolded Nanozyme as a Dynamic Biosensing System
    • Li, H.; Huang, Y.; Yu, Y.; Li, G.; Karamanos, Y. Self-Catalyzed Assembly of Peptide Scaffolded Nanozyme as a Dynamic Biosensing System ACS Appl. Mater. Interfaces 2016, 8, 2833-2839 10.1021/acsami.5b11567
    • (2016) ACS Appl. Mater. Interfaces , vol.8 , pp. 2833-2839
    • Li, H.1    Huang, Y.2    Yu, Y.3    Li, G.4    Karamanos, Y.5
  • 18
    • 84934915586 scopus 로고    scopus 로고
    • Amyloid-directed Assembly of Nanostructures and Functional Devices for Bionanoelectronics
    • Wang, X.; Li, Y.; Zhong, C. Amyloid-directed Assembly of Nanostructures and Functional Devices for Bionanoelectronics J. Mater. Chem. B 2015, 3, 4953-4958 10.1039/C5TB00374A
    • (2015) J. Mater. Chem. B , vol.3 , pp. 4953-4958
    • Wang, X.1    Li, Y.2    Zhong, C.3
  • 19
    • 84880171424 scopus 로고    scopus 로고
    • Hybrid Nanocomposites of Gold Single-Crystal Platelets and Amyloid Fibrils with Tunable Fluorescence, Conductivity, and Sensing Properties
    • Li, C.; Bolisetty, S.; Mezzenga, R. Hybrid Nanocomposites of Gold Single-Crystal Platelets and Amyloid Fibrils with Tunable Fluorescence, Conductivity, and Sensing Properties Adv. Mater. 2013, 25, 3694-3700 10.1002/adma.201300904
    • (2013) Adv. Mater. , vol.25 , pp. 3694-3700
    • Li, C.1    Bolisetty, S.2    Mezzenga, R.3
  • 20
    • 84892655895 scopus 로고    scopus 로고
    • Versatile Multi-functionalization of Protein Nanofibrils for Biosensor Applications
    • Sasso, L.; Suei, S.; Domigan, L.; Healy, J.; Nock, V.; Williams, M. A. K.; Gerrard, J. A. Versatile Multi-functionalization of Protein Nanofibrils for Biosensor Applications Nanoscale 2014, 6, 1629-1634 10.1039/C3NR05752F
    • (2014) Nanoscale , vol.6 , pp. 1629-1634
    • Sasso, L.1    Suei, S.2    Domigan, L.3    Healy, J.4    Nock, V.5    Williams, M.A.K.6    Gerrard, J.A.7
  • 21
    • 84863715767 scopus 로고    scopus 로고
    • Biodegradable Nanocomposites of Amyloid Fibrils and Graphene with Shape-memory and Enzyme-sensing Properties
    • Li, C.; Adamcik, J.; Mezzenga, R. Biodegradable Nanocomposites of Amyloid Fibrils and Graphene with Shape-memory and Enzyme-sensing Properties Nat. Nanotechnol. 2012, 7, 421-427 10.1038/nnano.2012.62
    • (2012) Nat. Nanotechnol. , vol.7 , pp. 421-427
    • Li, C.1    Adamcik, J.2    Mezzenga, R.3
  • 22
    • 84902831646 scopus 로고    scopus 로고
    • Electrostatic Assembly of Peptide Nanofiber-Biomimetic Silver Nanowires onto Graphene for Electrochemical Sensors
    • Wang, J.; Zhao, X.; Li, J.; Kuang, X.; Fan, Y.; Wei, G.; Su, Z. Electrostatic Assembly of Peptide Nanofiber-Biomimetic Silver Nanowires onto Graphene for Electrochemical Sensors ACS Macro Lett. 2014, 3, 529-533 10.1021/mz500213w
    • (2014) ACS Macro Lett. , vol.3 , pp. 529-533
    • Wang, J.1    Zhao, X.2    Li, J.3    Kuang, X.4    Fan, Y.5    Wei, G.6    Su, Z.7
  • 23
    • 84904013369 scopus 로고    scopus 로고
    • Amyloid-based Nanosensors and Nanodevices
    • Hauser, C. A. E.; Maurer-Stroh, S.; Martins, I. C. Amyloid-based Nanosensors and Nanodevices Chem. Soc. Rev. 2014, 43, 5326-5345 10.1039/C4CS00082J
    • (2014) Chem. Soc. Rev. , vol.43 , pp. 5326-5345
    • Hauser, C.A.E.1    Maurer-Stroh, S.2    Martins, I.C.3
  • 24
    • 84951998358 scopus 로고    scopus 로고
    • Recent Advances in Synthetic Polymer Based Hydrogels for Spinal Cord Repair
    • Trimaille, T.; Pertici, V.; Gigmes, D. Recent Advances in Synthetic Polymer Based Hydrogels for Spinal Cord Repair C. R. Chim. 2016, 19, 157-166 10.1016/j.crci.2015.03.016
    • (2016) C. R. Chim. , vol.19 , pp. 157-166
    • Trimaille, T.1    Pertici, V.2    Gigmes, D.3
  • 25
    • 84921744348 scopus 로고    scopus 로고
    • Engineering Amyloid Fibrils from β-Solenoid Proteins for Biomaterials Applications
    • Peralta, M. D. R. et al. Engineering Amyloid Fibrils from β-Solenoid Proteins for Biomaterials Applications ACS Nano 2015, 9, 449-463 10.1021/nn5056089
    • (2015) ACS Nano , vol.9 , pp. 449-463
    • Peralta, M.D.R.1
  • 26
    • 84890855226 scopus 로고    scopus 로고
    • ″green″ Electronics: Biodegradable and Biocompatible Materials and Devices for Sustainable Future
    • Irimia-Vladu, M. ″Green″ Electronics: Biodegradable and Biocompatible Materials and Devices for Sustainable Future Chem. Soc. Rev. 2014, 43, 588-610 10.1039/C3CS60235D
    • (2014) Chem. Soc. Rev. , vol.43 , pp. 588-610
    • Irimia-Vladu, M.1
  • 27
    • 47049100201 scopus 로고    scopus 로고
    • Amyloids: Not only Pathological Agents but also Ordered Nanomaterials
    • Cherny, I.; Gazit, E. Amyloids: Not Only Pathological Agents but also Ordered Nanomaterials Angew. Chem., Int. Ed. 2008, 47, 4062-4069 10.1002/anie.200703133
    • (2008) Angew. Chem., Int. Ed. , vol.47 , pp. 4062-4069
    • Cherny, I.1    Gazit, E.2
  • 28
    • 0344490335 scopus 로고    scopus 로고
    • Conducting Nanowires Built by Controlled Self-assembly of Amyloid Fibers and Selective Metal Deposition
    • Scheibel, T.; Parthasarathy, R.; Sawicki, G.; Lin, X. M.; Jaeger, H.; Lindquist, S. L. Conducting Nanowires Built by Controlled Self-assembly of Amyloid Fibers and Selective Metal Deposition Proc. Natl. Acad. Sci. U. S. A. 2003, 100, 4527-4532 10.1073/pnas.0431081100
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 4527-4532
    • Scheibel, T.1    Parthasarathy, R.2    Sawicki, G.3    Lin, X.M.4    Jaeger, H.5    Lindquist, S.L.6
  • 29
    • 0038514122 scopus 로고    scopus 로고
    • Exploiting Amyloid Fibril Lamination for Nanotube Self-assembly
    • Lu, K.; Jacob, J.; Thiyagarajan, P.; Conticello, V. P.; Lynn, D. G. Exploiting Amyloid Fibril Lamination for Nanotube Self-assembly J. Am. Chem. Soc. 2003, 125, 6391-6393 10.1021/ja0341642
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6391-6393
    • Lu, K.1    Jacob, J.2    Thiyagarajan, P.3    Conticello, V.P.4    Lynn, D.G.5
  • 30
    • 0037466613 scopus 로고    scopus 로고
    • Casting Metal Nanowires Within Discrete Self-assembled Peptide Nanotubes
    • Reches, M.; Gazit, E. Casting Metal Nanowires Within Discrete Self-assembled Peptide Nanotubes Science 2003, 300, 625-627 10.1126/science.1082387
    • (2003) Science , vol.300 , pp. 625-627
    • Reches, M.1    Gazit, E.2
  • 31
    • 0141765883 scopus 로고    scopus 로고
    • Fabrication of Novel Biomaterials Through Molecular Self-assembly
    • Zhang, S. Fabrication of Novel Biomaterials Through Molecular Self-assembly Nat. Biotechnol. 2003, 21, 1171-1178 10.1038/nbt874
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1171-1178
    • Zhang, S.1
  • 32
    • 33646088595 scopus 로고    scopus 로고
    • Probing the Pressure-Temperature Stability of Amyloid Fibrils Provides New Insights into Their Molecular Properties
    • Meersman, F.; Dobson, C. M. Probing the Pressure-Temperature Stability of Amyloid Fibrils Provides New Insights into Their Molecular Properties Biochim. Biophys. Acta, Proteins Proteomics 2006, 1764, 452-460 10.1016/j.bbapap.2005.10.021
    • (2006) Biochim. Biophys. Acta, Proteins Proteomics , vol.1764 , pp. 452-460
    • Meersman, F.1    Dobson, C.M.2
  • 33
    • 1642563960 scopus 로고    scopus 로고
    • Engineering Amyloidogenicity Towards the Development of Nanofibrillar Materials
    • Hamada, D.; Yanagihara, I.; Tsumoto, K. Engineering Amyloidogenicity Towards the Development of Nanofibrillar Materials Trends Biotechnol. 2004, 22, 93-97 10.1016/j.tibtech.2003.12.003
    • (2004) Trends Biotechnol. , vol.22 , pp. 93-97
    • Hamada, D.1    Yanagihara, I.2    Tsumoto, K.3
  • 35
    • 0027416047 scopus 로고
    • Spontaneous Assembly of a Self-Complementary Oligopeptide to Form a Stable Macroscopic Membrane
    • Zhang, S. G.; Holmes, T.; Lockshin, C.; Rich, A. Spontaneous Assembly of a Self-Complementary Oligopeptide to Form a Stable Macroscopic Membrane Proc. Natl. Acad. Sci. U. S. A. 1993, 90, 3334-3338 10.1073/pnas.90.8.3334
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 3334-3338
    • Zhang, S.G.1    Holmes, T.2    Lockshin, C.3    Rich, A.4
  • 36
    • 54949097679 scopus 로고    scopus 로고
    • Designer Self-assembling Peptide Nanofiber Scaffolds for Adult Mouse Neural Stem Cell 3-dimensional Cultures
    • Gelain, F.; Bottai, D.; Vescovi, A.; Zhang, S. Designer Self-assembling Peptide Nanofiber Scaffolds for Adult Mouse Neural Stem Cell 3-dimensional Cultures PLoS One 2006, 1, e119 10.1371/journal.pone.0000119
    • (2006) PLoS One , vol.1 , pp. e119
    • Gelain, F.1    Bottai, D.2    Vescovi, A.3    Zhang, S.4
  • 38
    • 0014145484 scopus 로고
    • Reconstitution of Amyloid Fibrils from Alkaline Extracts
    • Shiraham, T.; Cohen, A. S. Reconstitution of Amyloid Fibrils from Alkaline Extracts J. Cell Biol. 1967, 35, 459-464 10.1083/jcb.35.2.459
    • (1967) J. Cell Biol. , vol.35 , pp. 459-464
    • Shiraham, T.1    Cohen, A.S.2
  • 39
    • 0035158241 scopus 로고    scopus 로고
    • Studies of the Structure of Insulin Fibrils by Fourier Transform Infrared (FTIR) Spectroscopy and Electron Microscopy
    • Nielsen, L.; Frokjaer, S.; Carpenter, J. F.; Brange, J. Studies of the Structure of Insulin Fibrils by Fourier Transform Infrared (FTIR) Spectroscopy and Electron Microscopy J. Pharm. Sci. 2001, 90, 29-37 10.1002/1520-6017(200101)90:1<29::AID-JPS4>3.0.CO;2-4
    • (2001) J. Pharm. Sci. , vol.90 , pp. 29-37
    • Nielsen, L.1    Frokjaer, S.2    Carpenter, J.F.3    Brange, J.4
  • 43
    • 77952750301 scopus 로고    scopus 로고
    • Alzheimer's Aβ(1-40) Amyloid Fibrils Feature Size-Dependent Mechanical Properties
    • Xu, Z.; Paparcone, R.; Buehler, M. J. Alzheimer's Aβ(1-40) Amyloid Fibrils Feature Size-Dependent Mechanical Properties Biophys. J. 2010, 98, 2053-2062 10.1016/j.bpj.2009.12.4317
    • (2010) Biophys. J. , vol.98 , pp. 2053-2062
    • Xu, Z.1    Paparcone, R.2    Buehler, M.J.3
  • 44
    • 77957909677 scopus 로고    scopus 로고
    • Mutations Alter the Geometry and Mechanical Properties of Alzheimer's A beta(1-40) Amyloid Fibrils
    • Paparcone, R.; Pires, M. A.; Buehler, M. J. Mutations Alter the Geometry and Mechanical Properties of Alzheimer's A beta(1-40) Amyloid Fibrils Biochemistry 2010, 49, 8967-8977 10.1021/bi100953t
    • (2010) Biochemistry , vol.49 , pp. 8967-8977
    • Paparcone, R.1    Pires, M.A.2    Buehler, M.J.3
  • 45
    • 77952079235 scopus 로고    scopus 로고
    • Designed Biomaterials to Mimic the Mechanical Properties of Muscles
    • Lv, S.; Dudek, D. M.; Cao, Y.; Balamurali, M. M.; Gosline, J.; Li, H. Designed Biomaterials to Mimic the Mechanical Properties of Muscles Nature 2010, 465, 69-73 10.1038/nature09024
    • (2010) Nature , vol.465 , pp. 69-73
    • Lv, S.1    Dudek, D.M.2    Cao, Y.3    Balamurali, M.M.4    Gosline, J.5    Li, H.6
  • 46
    • 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 10.1038/nnano.2011.102
    • (2011) Nat. Nanotechnol. , vol.6 , pp. 469-479
    • Knowles, T.P.J.1    Buehler, M.J.2
  • 47
    • 30744433878 scopus 로고    scopus 로고
    • Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid Fibrils
    • Petkova, A. T.; Yau, W.-M.; Tycko, R. Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid Fibrils Biochemistry 2006, 45, 498-512 10.1021/bi051952q
    • (2006) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.-M.2    Tycko, R.3
  • 49
    • 0033849738 scopus 로고    scopus 로고
    • S Review: History of the Amyloid Fibril
    • Sipe, J. D.; Cohen, A. S Review: History of the Amyloid Fibril J. Struct. Biol. 2000, 130, 88-98 10.1006/jsbi.2000.4221
    • (2000) J. Struct. Biol. , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.2
  • 50
    • 67849106670 scopus 로고    scopus 로고
    • Amyloid-β protein Oligomerization and the Importance of Tetramers and Dodecamers in the Aetiology of Alzheimer's Disease
    • Bernstein, S. L. et al. Amyloid-β protein Oligomerization and the Importance of Tetramers and Dodecamers in the Aetiology of Alzheimer's Disease Nat. Chem. 2009, 1, 326-331 10.1038/nchem.247
    • (2009) Nat. Chem. , vol.1 , pp. 326-331
    • Bernstein, S.L.1
  • 52
    • 84867477898 scopus 로고    scopus 로고
    • The Amyloid Beta Peptide: A Chemist's Perspective. Role in Alzheimer's and Fibrillization
    • Hamley, I. W. The Amyloid Beta Peptide: A Chemist's Perspective. Role in Alzheimer's and Fibrillization Chem. Rev. 2012, 112, 5147-5192 10.1021/cr3000994
    • (2012) Chem. Rev. , vol.112 , pp. 5147-5192
    • Hamley, I.W.1
  • 53
    • 84929379712 scopus 로고    scopus 로고
    • Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies
    • Nasica-Labouze, J. et al. Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies Chem. Rev. 2015, 115, 3518-3563 10.1021/cr500638n
    • (2015) Chem. Rev. , vol.115 , pp. 3518-3563
    • Nasica-Labouze, J.1
  • 54
    • 84861022629 scopus 로고    scopus 로고
    • UV Resonance Raman Investigations of Peptide and Protein Structure and Dynamics
    • Oladepo, S. A.; Xiong, K.; Hong, Z.; Asher, S. A.; Handen, J.; Lednev, I. K. UV Resonance Raman Investigations of Peptide and Protein Structure and Dynamics Chem. Rev. 2012, 112, 2604-2628 10.1021/cr200198a
    • (2012) Chem. Rev. , vol.112 , pp. 2604-2628
    • Oladepo, S.A.1    Xiong, K.2    Hong, Z.3    Asher, S.A.4    Handen, J.5    Lednev, I.K.6
  • 55
    • 77952075172 scopus 로고    scopus 로고
    • Structural Variations in the Cross-beta Core of Amyloid Beta Fibrils Revealed by Deep UV Resonance Raman Spectroscopy
    • Popova, L. A.; Kodali, R.; Wetzel, R.; Lednev, I. K. Structural Variations in the Cross-beta Core of Amyloid Beta Fibrils Revealed by Deep UV Resonance Raman Spectroscopy J. Am. Chem. Soc. 2010, 132, 6324-6328 10.1021/ja909074j
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6324-6328
    • Popova, L.A.1    Kodali, R.2    Wetzel, R.3    Lednev, I.K.4
  • 56
    • 77956205734 scopus 로고    scopus 로고
    • Quantitative Methods for Structural Characterization of Proteins Based on Deep UV Resonance Raman Spectroscopy
    • Shashilov, V. A.; Sikirzhytski, V.; Popova, L. A.; Lednev, I. K. Quantitative Methods for Structural Characterization of Proteins Based on Deep UV Resonance Raman Spectroscopy Methods 2010, 52, 23-37 10.1016/j.ymeth.2010.05.004
    • (2010) Methods , vol.52 , pp. 23-37
    • Shashilov, V.A.1    Sikirzhytski, V.2    Popova, L.A.3    Lednev, I.K.4
  • 57
    • 69249175534 scopus 로고    scopus 로고
    • Vibrational Spectroscopy: Biological Applications of Ultraviolet Raman Spectroscopy
    • Uversky, V. N. Permyakov, E. A. Nova Science Publishers, Inc. New York
    • Lednev, I. K. Vibrational Spectroscopy: Biological Applications of Ultraviolet Raman Spectroscopy. In Protein Structures, Methods in Protein Structures and Stability Analysis; Uversky, V. N.; Permyakov, E. A., Eds.; Nova Science Publishers, Inc.: New York, 2007.
    • (2007) Protein Structures, Methods in Protein Structures and Stability Analysis
    • Lednev, I.K.1
  • 58
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A Package for Molecular Simulation and Trajectory Analysis
    • Lindahl, E.; Hess, B.; van der Spoel, D. GROMACS 3.0: A Package for Molecular Simulation and Trajectory Analysis J. Mol. Model. 2001, 7, 306-317 10.1007/s008940100045
    • (2001) J. Mol. Model. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 59
    • 4444282928 scopus 로고    scopus 로고
    • A Biomolecular Force Field Based on the Free Enthalpy of Hydration and Solvation: The GROMOS Force-field Parameter Sets 53A5 and 53A6
    • Oostenbrink, C.; Villa, A.; Mark, A. E.; Van Gunsteren, W. F. A Biomolecular Force Field Based on the Free Enthalpy of Hydration and Solvation: The GROMOS Force-field Parameter Sets 53A5 and 53A6 J. Comput. Chem. 2004, 25, 1656-1676 10.1002/jcc.20090
    • (2004) J. Comput. Chem. , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Mark, A.E.3    Van Gunsteren, W.F.4
  • 61
    • 84858374665 scopus 로고    scopus 로고
    • The Amyloid State of Proteins in Human Diseases
    • Eisenberg, D.; Jucker, M. The Amyloid State of Proteins in Human Diseases Cell 2012, 148, 1188-1203 10.1016/j.cell.2012.02.022
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 62
    • 77955230701 scopus 로고    scopus 로고
    • Understanding Amyloid Aggregation by Statistical Analysis of Atomic Force Microscopy Images
    • Adamcik, J.; Jung, J.-M.; Flakowski, J.; De Los Rios, P.; Dietler, G.; Mezzenga, R. Understanding Amyloid Aggregation by Statistical Analysis of Atomic Force Microscopy Images Nat. Nanotechnol. 2010, 5, 423-428 10.1038/nnano.2010.59
    • (2010) Nat. Nanotechnol. , vol.5 , pp. 423-428
    • Adamcik, J.1    Jung, J.-M.2    Flakowski, J.3    De Los Rios, P.4    Dietler, G.5    Mezzenga, R.6
  • 63
    • 79957477372 scopus 로고    scopus 로고
    • Adjustable Twisting Periodic Pitch of Amyloid Fibrils
    • Adamcik, J.; Mezzenga, R. Adjustable Twisting Periodic Pitch of Amyloid Fibrils Soft Matter 2011, 7, 5437-5443 10.1039/c1sm05382e
    • (2011) Soft Matter , vol.7 , pp. 5437-5443
    • Adamcik, J.1    Mezzenga, R.2
  • 64
    • 84920275973 scopus 로고    scopus 로고
    • Universal Behavior in the Mesoscale Properties of Amyloid Fibrils
    • Assenza, S.; Adamcik, J.; Mezzenga, R.; De Los Rios, P. Universal Behavior in the Mesoscale Properties of Amyloid Fibrils Phys. Rev. Lett. 2014, 113, 268103 10.1103/PhysRevLett.113.268103
    • (2014) Phys. Rev. Lett. , vol.113 , pp. 268103
    • Assenza, S.1    Adamcik, J.2    Mezzenga, R.3    De Los Rios, P.4
  • 65
    • 57449091884 scopus 로고    scopus 로고
    • Molecular Structural Basis for Polymorphism in Alzheimer's β-amyloid Fibrils
    • Paravastu, A. K.; Leapman, R. D.; Yau, W.-M.; Tycko, R. Molecular Structural Basis for Polymorphism in Alzheimer's β-amyloid Fibrils Proc. Natl. Acad. Sci. U. S. A. 2008, 105, 18349-18354 10.1073/pnas.0806270105
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 18349-18354
    • Paravastu, A.K.1    Leapman, R.D.2    Yau, W.-M.3    Tycko, R.4
  • 66
    • 77953429584 scopus 로고    scopus 로고
    • Comparative Study of Polymorphous Alzheimer's A beta(1-40) Amyloid Nanofibrils and Microfibers
    • Paparcone, R.; Sanchez, J.; Buehler, M. J. Comparative Study of Polymorphous Alzheimer's A beta(1-40) Amyloid Nanofibrils and Microfibers J. Comput. Theor. Nanosci. 2010, 7, 1279-1286 10.1166/jctn.2010.1481
    • (2010) J. Comput. Theor. Nanosci. , vol.7 , pp. 1279-1286
    • Paparcone, R.1    Sanchez, J.2    Buehler, M.J.3
  • 67
    • 82655177891 scopus 로고    scopus 로고
    • Nanomechanical Properties of Alpha-synuclein Amyloid Fibrils: A Comparative Study by Nanoindentation, Harmonic Force Microscopy, and Peakforce QNM
    • Sweers, K.; van der Werf, K.; Bennink, M.; Subramaniam, V. Nanomechanical Properties of Alpha-synuclein Amyloid Fibrils: A Comparative Study by Nanoindentation, Harmonic Force Microscopy, and Peakforce QNM Nanoscale Res. Lett. 2011, 6, 270 10.1186/1556-276X-6-270
    • (2011) Nanoscale Res. Lett. , vol.6 , pp. 270
    • Sweers, K.1    Van Der Werf, K.2    Bennink, M.3    Subramaniam, V.4
  • 69
    • 84861416494 scopus 로고    scopus 로고
    • Nanomechanical Properties of Single Amyloid Fibrils
    • Sweers, K. K. M.; Bennink, M. L.; Subramaniam, V. Nanomechanical Properties of Single Amyloid Fibrils J. Phys.: Condens. Matter 2012, 24, 243101 10.1088/0953-8984/24/24/243101
    • (2012) J. Phys.: Condens. Matter , vol.24 , pp. 243101
    • Sweers, K.K.M.1    Bennink, M.L.2    Subramaniam, V.3
  • 70
    • 84874652160 scopus 로고    scopus 로고
    • Nanoprobing of the Effect of Cu2+ Cations on Misfolding, Interaction and Aggregation of Amyloid beta Peptide
    • Lv, Z. J.; Condron, M. M.; Teplow, D. B.; Lyubchenko, Y. L. Nanoprobing of the Effect of Cu2+ Cations on Misfolding, Interaction and Aggregation of Amyloid beta Peptide J. Neuroimmune Pharm. 2013, 8, 262-273 10.1007/s11481-012-9416-6
    • (2013) J. Neuroimmune Pharm. , vol.8 , pp. 262-273
    • Lv, Z.J.1    Condron, M.M.2    Teplow, D.B.3    Lyubchenko, Y.L.4
  • 71
    • 45149110531 scopus 로고    scopus 로고
    • Effects of Hydration on the Mechanical Response of Individual Collagen Fibrils
    • Grant, C. A.; Brockwell, D. J.; Radford, S. E.; Thomson, N. H. Effects of Hydration on the Mechanical Response of Individual Collagen Fibrils Appl. Phys. Lett. 2008, 92, 233902-233904 10.1063/1.2937001
    • (2008) Appl. Phys. Lett. , vol.92 , pp. 233902-233904
    • Grant, C.A.1    Brockwell, D.J.2    Radford, S.E.3    Thomson, N.H.4
  • 73
    • 84916631559 scopus 로고    scopus 로고
    • Mechanical Deformation Mechanisms and Properties of Amyloid Fibrils
    • Choi, B.; Yoon, G.; Lee, S. W.; Eom, K. Mechanical Deformation Mechanisms and Properties of Amyloid Fibrils Phys. Chem. Chem. Phys. 2015, 17, 1379-1389 10.1039/C4CP03804E
    • (2015) Phys. Chem. Chem. Phys. , vol.17 , pp. 1379-1389
    • Choi, B.1    Yoon, G.2    Lee, S.W.3    Eom, K.4
  • 74
    • 79952005178 scopus 로고    scopus 로고
    • Failure of Abeta(1-40) Amyloid Fibrils under Tensile Loading
    • Paparcone, R.; Buehler, M. J. Failure of Abeta(1-40) Amyloid Fibrils Under Tensile Loading Biomaterials 2011, 32, 3367-3374 10.1016/j.biomaterials.2010.11.066
    • (2011) Biomaterials , vol.32 , pp. 3367-3374
    • Paparcone, R.1    Buehler, M.J.2
  • 75
    • 79959631028 scopus 로고    scopus 로고
    • Single-step Direct Measurement of Amyloid Fibrils Stiffness by Peak Force Quantitative Nanomechanical Atomic Force Microscopy
    • 193701-1-193701-3
    • Adamcik, J.; Berquand, A.; Mezzenga, R. Single-step Direct Measurement of Amyloid Fibrils Stiffness by Peak Force Quantitative Nanomechanical Atomic Force Microscopy Appl. Phys. Lett. 2011, 98, 193701-1-193701-3 10.1063/1.3589369
    • (2011) Appl. Phys. Lett. , vol.98
    • Adamcik, J.1    Berquand, A.2    Mezzenga, R.3


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