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Volumn 7, Issue 9, 2013, Pages 7562-7572

Molecular structure of RADA16-I designer self-assembling peptide nanofibers

Author keywords

molecular modeling; peptide nanofiber design; self assembling peptide; solid state NMR spectroscopy; structure determination

Indexed keywords

INTERMOLECULAR PACKING; MULTIPLE CONFIGURATIONS; NANO-FIBER STRUCTURE; REGENERATIVE MEDICINE; SELF-ASSEMBLING PEPTIDES; SOLID-STATE NMR SPECTROSCOPY; STRUCTURE DETERMINATION; THREE DIMENSIONAL CELL CULTURE;

EID: 84884930643     PISSN: 19360851     EISSN: 1936086X     Source Type: Journal    
DOI: 10.1021/nn401562f     Document Type: Article
Times cited : (121)

References (58)
  • 1
    • 0036139571 scopus 로고    scopus 로고
    • Novel Peptide-Based Biomaterial Scaffolds for Tissue Engineering
    • Holmes, T. C. Novel Peptide-Based Biomaterial Scaffolds for Tissue Engineering Trends. Biotechnol. 2002, 20, 16-21
    • (2002) Trends. Biotechnol. , vol.20 , pp. 16-21
    • Holmes, T.C.1
  • 2
    • 79956206107 scopus 로고    scopus 로고
    • Evaluation of Early and Late Effects into the Acute Spinal Cord Injury of an Injectable Functionalized Self-Assembling Scaffold
    • Cigognini, D.; Satta, A.; Colleoni, B.; Silva, D.; Donega, M.; Antonini, S.; Gelain, F. Evaluation of Early and Late Effects into the Acute Spinal Cord Injury of an Injectable Functionalized Self-Assembling Scaffold PLoS One 2011, 6, 1-15
    • (2011) PLoS One , vol.6 , pp. 1-15
    • Cigognini, D.1    Satta, A.2    Colleoni, B.3    Silva, D.4    Donega, M.5    Antonini, S.6    Gelain, F.7
  • 3
    • 34547929424 scopus 로고    scopus 로고
    • Designer Self-Assembling Peptide Scaffolds for 3-D Tissue Cell Cultures and Regenerative Medicine
    • Gelain, F.; Horii, A.; Zhang, S. G. Designer Self-Assembling Peptide Scaffolds for 3-D Tissue Cell Cultures and Regenerative Medicine Macromol. Biosci. 2007, 7, 544-551
    • (2007) Macromol. Biosci. , vol.7 , pp. 544-551
    • Gelain, F.1    Horii, A.2    Zhang, S.G.3
  • 4
    • 80155147119 scopus 로고    scopus 로고
    • 3D Culture of Adult Mouse Neural Stem Cells within Functionalized Self-Assembling Peptide Scaffolds
    • Cunha, C.; Panseri, S.; Villa, O.; Silva, D.; Gelain, F. 3D Culture of Adult Mouse Neural Stem Cells within Functionalized Self-Assembling Peptide Scaffolds Int. J. Nanomed. 2011, 6, 943-955
    • (2011) Int. J. Nanomed. , vol.6 , pp. 943-955
    • Cunha, C.1    Panseri, S.2    Villa, O.3    Silva, D.4    Gelain, F.5
  • 5
    • 63849135735 scopus 로고    scopus 로고
    • Controlled Release of Functional Proteins through Designer Self-Assembling Peptide Nanofiber Hydrogel Scaffold
    • Koutsopoulos, S.; Unswortha, L. D.; Nagaia, Y.; Zhang, S. G. Controlled Release of Functional Proteins through Designer Self-Assembling Peptide Nanofiber Hydrogel Scaffold Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 4623-4628
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 4623-4628
    • Koutsopoulos, S.1    Unswortha, L.D.2    Nagaia, Y.3    Zhang, S.G.4
  • 6
    • 36249032275 scopus 로고    scopus 로고
    • Biological Designer Self-Assembling Peptide Nanofiber Scaffolds significantly Enhance Osteoblast Proliferation, Differentiation and 3-D Migration
    • Horii, A.; Wang, X. M.; Gelain, F.; Zhang, S. G. Biological Designer Self-Assembling Peptide Nanofiber Scaffolds significantly Enhance Osteoblast Proliferation, Differentiation and 3-D Migration PLoS One 2007, 2, 1-9
    • (2007) PLoS One , vol.2 , pp. 1-9
    • Horii, A.1    Wang, X.M.2    Gelain, F.3    Zhang, S.G.4
  • 7
    • 77955777010 scopus 로고    scopus 로고
    • Significant Type i and Type III Collagen Production from Human Periodontal Ligament Fibroblasts in 3D Peptide Scaffolds without Extra Growth Factors
    • Kumada, Y.; Zhang, S. G. Significant Type I and Type III Collagen Production from Human Periodontal Ligament Fibroblasts in 3D Peptide Scaffolds without Extra Growth Factors PLoS One 2010, 5, 1-7
    • (2010) PLoS One , vol.5 , pp. 1-7
    • Kumada, Y.1    Zhang, S.G.2
  • 8
    • 81255195799 scopus 로고    scopus 로고
    • Design of Self-Assembling Peptides and their Biomedical Applications
    • Liu, J. P.; Zhao, X. J. Design of Self-Assembling Peptides and their Biomedical Applications Nanomedicine 2011, 6, 1621-1643
    • (2011) Nanomedicine , vol.6 , pp. 1621-1643
    • Liu, J.P.1    Zhao, X.J.2
  • 9
  • 10
    • 75749124231 scopus 로고    scopus 로고
    • Hemostatic Efficacy of Biological Self-Assembling Peptide Nanofibers in a Rat Kidney Model
    • Song, H.; Zhang, L. L.; Zhao, X. J. Hemostatic Efficacy of Biological Self-Assembling Peptide Nanofibers in a Rat Kidney Model Macromol. Biosci. 2010, 10, 33-39
    • (2010) Macromol. Biosci. , vol.10 , pp. 33-39
    • Song, H.1    Zhang, L.L.2    Zhao, X.J.3
  • 11
  • 13
    • 70249131175 scopus 로고    scopus 로고
    • In Vivo Engineering of Tissues: Biological Considerations, Challenges, Strategies, and Future Directions
    • Shastri, V. P. In Vivo Engineering of Tissues: Biological Considerations, Challenges, Strategies, and Future Directions Adv. Mater. 2009, 21, 3246-3254
    • (2009) Adv. Mater. , vol.21 , pp. 3246-3254
    • Shastri, V.P.1
  • 14
    • 67049099131 scopus 로고    scopus 로고
    • The Effect of Self-Assembling Peptide RADA16-I on the Growth of Human Leukemia Cells in Vitro and in Nude Mice
    • Tang, C. K.; Shao, X. M.; Sun, B. B.; Huang, W. L.; Zhao, X. J. The Effect of Self-Assembling Peptide RADA16-I on the Growth of Human Leukemia Cells in Vitro and in Nude Mice Int. J. Mol. Sci. 2009, 10, 2136-2145
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 2136-2145
    • Tang, C.K.1    Shao, X.M.2    Sun, B.B.3    Huang, W.L.4    Zhao, X.J.5
  • 15
    • 0036890278 scopus 로고    scopus 로고
    • Emerging Biological Materials through Molecular Self-Assembly
    • Zhang, S. G. Emerging Biological Materials through Molecular Self-Assembly Biotechnol. Adv. 2002, 20, 321-339
    • (2002) Biotechnol. Adv. , vol.20 , pp. 321-339
    • Zhang, S.G.1
  • 16
    • 0026758377 scopus 로고
    • Zuotin, a Putative Z-DNA Binding-Protein in Saccharomyces cerevisiae
    • Zhang, S. G.; Lockshin, C.; Herbert, A.; Winter, E.; Rich, A. Zuotin, a Putative Z-DNA Binding-Protein in Saccharomyces cerevisiae EMBO J. 1992, 11, 3787-3796
    • (1992) EMBO J. , vol.11 , pp. 3787-3796
    • Zhang, S.G.1    Lockshin, C.2    Herbert, A.3    Winter, E.4    Rich, A.5
  • 17
    • 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
    • (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
  • 18
    • 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. S.; Rich, A.; Zhang, S. G. 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.S.4    Rich, A.5    Zhang, S.G.6
  • 19
    • 0029411957 scopus 로고
    • Self-Complementary Oligopeptide Matrices Support Mammalian-Cell Attachment
    • Zhang, S. G.; Holmes, T. C.; Dipersio, C. M.; Hynes, R. O.; Su, X.; Rich, A. Self-Complementary Oligopeptide Matrices Support Mammalian-Cell Attachment Biomaterials 1995, 16, 1385-1393
    • (1995) Biomaterials , vol.16 , pp. 1385-1393
    • Zhang, S.G.1    Holmes, T.C.2    Dipersio, C.M.3    Hynes, R.O.4    Su, X.5    Rich, A.6
  • 21
    • 0033937682 scopus 로고    scopus 로고
    • Conformational Behavior of Ionic Self-Complementary Peptides
    • Altman, M.; Lee, P.; Rich, A.; Zhang, S. G. Conformational Behavior of Ionic Self-Complementary Peptides Protein Sci. 2000, 9, 1095-1105
    • (2000) Protein Sci. , vol.9 , pp. 1095-1105
    • Altman, M.1    Lee, P.2    Rich, A.3    Zhang, S.G.4
  • 24
  • 26
    • 84857506134 scopus 로고    scopus 로고
    • From Short Peptides to Nanofibers to Macromolecular Assemblies in Biomedicine
    • Loo, Y.; Zhang, S.; Hauser, C. A. E. From Short Peptides to Nanofibers to Macromolecular Assemblies in Biomedicine Biotechnol. Adv. 2012, 30, 593-603
    • (2012) Biotechnol. Adv. , vol.30 , pp. 593-603
    • Loo, Y.1    Zhang, S.2    Hauser, C.A.E.3
  • 27
    • 84863019040 scopus 로고    scopus 로고
    • Self-Assembling Peptides as Cell-Interactive Scaffolds
    • Wu, E. C.; Zhang, S. G.; Hauser, C. A. E. Self-Assembling Peptides as Cell-Interactive Scaffolds Adv. Funct. Mater. 2012, 22, 456-468
    • (2012) Adv. Funct. Mater. , vol.22 , pp. 456-468
    • Wu, E.C.1    Zhang, S.G.2    Hauser, C.A.E.3
  • 28
    • 84859406109 scopus 로고    scopus 로고
    • End-to-End Self-Assembly of RADA 16-I Nanofibrils in Aqueous Solutions
    • Arosio, P.; Owczarz, M.; Wu, H.; Butte, A.; Morbidelli, M. End-to-End Self-Assembly of RADA 16-I Nanofibrils in Aqueous Solutions Biophys. J. 2012, 102, 1617-1626
    • (2012) Biophys. J. , vol.102 , pp. 1617-1626
    • Arosio, P.1    Owczarz, M.2    Wu, H.3    Butte, A.4    Morbidelli, M.5
  • 29
    • 80051696463 scopus 로고    scopus 로고
    • An Effective Continuum Approach for Modeling Non-Equilibrium Structural Evolution of Protein Nanofiber Networks
    • Cheng, L.; Englander, O.; Paravastu, A. K.; Oates, W. S. An Effective Continuum Approach for Modeling Non-Equilibrium Structural Evolution of Protein Nanofiber Networks J. Chem. Phys. 2011, 135, 055102-1-055102-15
    • (2011) J. Chem. Phys. , vol.135 , pp. 0551021-05510215
    • Cheng, L.1    Englander, O.2    Paravastu, A.K.3    Oates, W.S.4
  • 30
    • 0035872678 scopus 로고    scopus 로고
    • C-13-C-13 Dipolar Recoupling under very Fast Magic Angle Spinning in Solid-State Nuclear Magnetic Resonance: Applications to Distance Measurements, Spectral Assignments, and High-Throughput Secondary-Structure Determination
    • Ishii, Y. C-13-C-13 Dipolar Recoupling under very Fast Magic Angle Spinning in Solid-State Nuclear Magnetic Resonance: Applications to Distance Measurements, Spectral Assignments, and High-Throughput Secondary-Structure Determination J. Chem. Phys. 2001, 114, 8473-8483
    • (2001) J. Chem. Phys. , vol.114 , pp. 8473-8483
    • Ishii, Y.1
  • 32
    • 57449091884 scopus 로고    scopus 로고
    • Molecular Structural Basis for Polymorphism in Alzheimer's Beta-Amyloid Fibrils
    • Paravastu, A. K.; Leapman, R. D.; Yau, W. M.; Tycko, R. Molecular Structural Basis for Polymorphism in Alzheimer's Beta-Amyloid Fibrils Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 18349-18354
    • (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
  • 34
    • 0033003335 scopus 로고    scopus 로고
    • Protein Backbone Angle Restraints from Searching a Database for Chemical Shift and Sequence Homology
    • Cornilescu, G.; Delaglio, F.; Bax, A. Protein Backbone Angle Restraints from Searching a Database for Chemical Shift and Sequence Homology J. Biomol. NMR 1999, 13, 289-302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 35
    • 33847064253 scopus 로고    scopus 로고
    • Symmetry-Based Constant-Time Homonuclear Dipolar Recoupling in Solid State NMR
    • Tycko, R. Symmetry-Based Constant-Time Homonuclear Dipolar Recoupling in Solid State NMR J. Chem. Phys. 2007, 126, 064506-064506
    • (2007) J. Chem. Phys. , vol.126 , pp. 064506-064506
    • Tycko, R.1
  • 37
    • 0035997080 scopus 로고    scopus 로고
    • Supramolecular Structure in Full-Length Alzheimer's Beta-Amyloid Fibrils: Evidence for a Parallel Beta-Sheet Organization from Solid-State Nuclear Magnetic Resonance
    • Balbach, J. J.; Petkova, A. T.; Oyler, N. A.; Antzutkin, O. N.; Gordon, D. J.; Meredith, S. C.; Tycko, R. Supramolecular Structure in Full-Length Alzheimer's Beta-Amyloid Fibrils: Evidence for a Parallel Beta-Sheet Organization from Solid-State Nuclear Magnetic Resonance Biophys. J. 2002, 83, 1205-1216
    • (2002) Biophys. J. , vol.83 , pp. 1205-1216
    • Balbach, J.J.1    Petkova, A.T.2    Oyler, N.A.3    Antzutkin, O.N.4    Gordon, D.J.5    Meredith, S.C.6    Tycko, R.7
  • 38
    • 30844458347 scopus 로고    scopus 로고
    • SPINEVOLUTION: A Powerful Tool for the Simulation of Solid and Liquid State NMR Experiments
    • Veshtort, M.; Griffin, R. G. SPINEVOLUTION: A Powerful Tool for the Simulation of Solid and Liquid State NMR Experiments J. Magn. Reson. 2006, 178, 248-282
    • (2006) J. Magn. Reson. , vol.178 , pp. 248-282
    • Veshtort, M.1    Griffin, R.G.2
  • 40
    • 34247504580 scopus 로고    scopus 로고
    • Solid-State NMR Study of Amyloid Nanocrystals and Fibrils Formed by the Peptide GNNQQNY from Yeast Prion Protein Sup35p
    • van der Wel, P. C. A.; Lewandowski, J. R.; Griffin, R. G. Solid-State NMR Study of Amyloid Nanocrystals and Fibrils Formed by the Peptide GNNQQNY from Yeast Prion Protein Sup35p J. Am. Chem. Soc. 2007, 129, 5117-5130
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5117-5130
    • Van Der Wel, P.C.A.1    Lewandowski, J.R.2    Griffin, R.G.3
  • 41
    • 78149340576 scopus 로고    scopus 로고
    • Structural Characterization of GNNQQNY Amyloid Fibrils by Magic Angle Spinning NMR
    • van der Wel, P. C. A.; Lewandowski, J. R.; Griffin, R. G. Structural Characterization of GNNQQNY Amyloid Fibrils by Magic Angle Spinning NMR Biochemistry 2010, 49, 9457-9469
    • (2010) Biochemistry , vol.49 , pp. 9457-9469
    • Van Der Wel, P.C.A.1    Lewandowski, J.R.2    Griffin, R.G.3
  • 44
    • 61949248657 scopus 로고    scopus 로고
    • Effect of Dehydration on the Aggregation Kinetics of Two Amyloid Peptides
    • Mukherjee, S.; Chowdhury, P.; 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, P.2    Gai, F.3
  • 45
    • 33750017513 scopus 로고    scopus 로고
    • Molecular Structure of Amyloid Fibrils: Insights from Solid-State NMR
    • Tycko, R. Molecular Structure of Amyloid Fibrils: Insights from Solid-State NMR Q. Rev. Biophys. 2006, 39, 1-55
    • (2006) Q. Rev. Biophys. , vol.39 , pp. 1-55
    • Tycko, R.1
  • 47
    • 0344255649 scopus 로고    scopus 로고
    • Solid State NMR Reveals a pH-Dependent Antiparallel Beta-Sheet Registry in Fibrils Formed by a Beta-Amyloid Peptide
    • Petkova, A. T.; Buntkowsky, G.; Dyda, F.; Leapman, R. D.; Yau, W. M.; Tycko, R. Solid State NMR Reveals a pH-Dependent Antiparallel Beta-Sheet Registry in Fibrils Formed by a Beta-Amyloid Peptide J. Mol. Biol. 2004, 335, 247-260
    • (2004) J. Mol. Biol. , vol.335 , pp. 247-260
    • Petkova, A.T.1    Buntkowsky, G.2    Dyda, F.3    Leapman, R.D.4    Yau, W.M.5    Tycko, R.6
  • 48
    • 79952754330 scopus 로고    scopus 로고
    • Structural Evolution of Iowa Mutant Beta-Amyloid Fibrils from Polymorphic to Homogeneous States under Repeated Seeded Growth
    • Qiang, W.; Yau, W.; Tycko, R. Structural Evolution of Iowa Mutant Beta-Amyloid Fibrils from Polymorphic to Homogeneous States Under Repeated Seeded Growth J. Am. Chem. Soc. 2011, 133, 4018-4029
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 4018-4029
    • Qiang, W.1    Yau, W.2    Tycko, R.3
  • 49
    • 79952938717 scopus 로고    scopus 로고
    • The Japanese Mutant A Beta (Delta E22-A Beta(1-39)) Forms Fibrils Instantaneously, with Low-Thioflavin T Fluorescence: Seeding of Wild-Type A Beta(1-40) into Atypical Fibrils by Delta E22-A Beta(1-39)
    • Cloe, A. L.; Orgel, J.; Sachleben, J. R.; Tycko, R.; Meredith, S. C. The Japanese Mutant A Beta (Delta E22-A Beta(1-39)) Forms Fibrils Instantaneously, with Low-Thioflavin T Fluorescence: Seeding of Wild-Type A Beta(1-40) into Atypical Fibrils by Delta E22-A Beta(1-39) Biochemistry 2011, 50, 2026-2039
    • (2011) Biochemistry , vol.50 , pp. 2026-2039
    • Cloe, A.L.1    Orgel, J.2    Sachleben, J.R.3    Tycko, R.4    Meredith, S.C.5
  • 50
    • 77949765699 scopus 로고    scopus 로고
    • Pathogenic Polyglutamine Tracts Are Potent Inducers of Spontaneous Sup35 and Rnq1 Amyloidogenesis
    • Goehler, H.; Droge, A.; Lurz, R.; Schnoegl, S.; Chernoff, Y. O.; Wanker, E. E. Pathogenic Polyglutamine Tracts Are Potent Inducers of Spontaneous Sup35 and Rnq1 Amyloidogenesis PLoS One 2010, 5, 1-13
    • (2010) PLoS One , vol.5 , pp. 1-13
    • Goehler, H.1    Droge, A.2    Lurz, R.3    Schnoegl, S.4    Chernoff, Y.O.5    Wanker, E.E.6
  • 51
    • 23244449092 scopus 로고    scopus 로고
    • Parallel Beta-Sheets and Polar Zippers in Amyloid Fibrils Formed by Residues 10-39 of the Yeast Prion Protein Ure2p
    • Chan, J. C. C.; Oyler, N. A.; Yau, W. M.; Tycko, R. Parallel Beta-Sheets and Polar Zippers in Amyloid Fibrils Formed by Residues 10-39 of the Yeast Prion Protein Ure2p Biochemistry 2005, 44, 10669-10680
    • (2005) Biochemistry , vol.44 , pp. 10669-10680
    • Chan, J.C.C.1    Oyler, N.A.2    Yau, W.M.3    Tycko, R.4
  • 52
    • 0028283985 scopus 로고
    • Glutamine Repeats as Polar Zippers-Their Possible Role in Inherited Neurodegenerative Diseases
    • Perutz, M. F.; Johnson, T.; Suzuki, M.; Finch, J. T. Glutamine Repeats as Polar Zippers-Their Possible Role in Inherited Neurodegenerative Diseases Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 5355-5358
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 5355-5358
    • Perutz, M.F.1    Johnson, T.2    Suzuki, M.3    Finch, J.T.4
  • 54
  • 55
  • 57
    • 0037132592 scopus 로고    scopus 로고
    • Responsive Hydrogels from the Intramolecular Folding and Self-Assembly of a Designed Peptide
    • Schneider, J. P.; Pochan, D. J.; Ozbas, B.; Rajagopal, K.; Pakstis, L.; Kretsinger, J. Responsive Hydrogels from the Intramolecular Folding and Self-Assembly of a Designed Peptide J. Am. Chem. Soc. 2002, 124, 15030-15037
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 15030-15037
    • Schneider, J.P.1    Pochan, D.J.2    Ozbas, B.3    Rajagopal, K.4    Pakstis, L.5    Kretsinger, J.6
  • 58
    • 0001250543 scopus 로고
    • C-13 Nuclear Magnetic-Resonance of Polymers Spinning at Magic Angle
    • Schaefer, J.; Stejskal, E. C-13 Nuclear Magnetic-Resonance of Polymers Spinning at Magic Angle J. Am. Chem. Soc. 1976, 98, 1031-1032
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 1031
    • Schaefer, J.1    Stejskal, E.2


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