메뉴 건너뛰기




Volumn 15, Issue 4, 2005, Pages 453-463

Peptides as novel smart materials

Author keywords

[No Author keywords available]

Indexed keywords

BIOMATERIAL; HYBRID PROTEIN; PEPTIDE; SURFACTANT;

EID: 23044431605     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2005.07.005     Document Type: Review
Times cited : (228)

References (91)
  • 1
    • 0037192505 scopus 로고    scopus 로고
    • Self-assembly at all scales
    • G.M. Whitesides, and B. Grzybowski Self-assembly at all scales Science 295 2002 2418 2421
    • (2002) Science , vol.295 , pp. 2418-2421
    • Whitesides, G.M.1    Grzybowski, B.2
  • 2
    • 0026433721 scopus 로고
    • Molecular self-assembly and nanochemistry: A chemical strategy for the synthesis of nanostructures
    • G.M. Whitesides, J.P. Mathias, and C.T. Seto Molecular self-assembly and nanochemistry: a chemical strategy for the synthesis of nanostructures Science 254 1991 1312 1319
    • (1991) Science , vol.254 , pp. 1312-1319
    • Whitesides, G.M.1    Mathias, J.P.2    Seto, C.T.3
  • 3
    • 0037192455 scopus 로고    scopus 로고
    • Toward self-organization and complex matter
    • J.M. Lehn Toward self-organization and complex matter Science 295 2002 2400 2403
    • (2002) Science , vol.295 , pp. 2400-2403
    • Lehn, J.M.1
  • 4
    • 0000562064 scopus 로고
    • Induction of peptide conformation at apolar water interfaces.1. a study with model peptides of defined hydrophobic periodicity
    • W.F. DeGrado, and J.D. Lear Induction of peptide conformation at apolar water interfaces.1. a study with model peptides of defined hydrophobic periodicity J Am Chem Soc 107 1985 7684 7689
    • (1985) J Am Chem Soc , vol.107 , pp. 7684-7689
    • Degrado, W.F.1    Lear, J.D.2
  • 5
    • 4143141192 scopus 로고    scopus 로고
    • Self-assembling peptides and proteins for nanotechnological applications
    • K. Rajagopal, and J.P. Schneider Self-assembling peptides and proteins for nanotechnological applications Curr Opin Struct Biol 14 2004 480 486 A well-written review article with special focus on de novo designed self-assembling peptides that form hydrogels.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 480-486
    • Rajagopal, K.1    Schneider, J.P.2
  • 6
    • 0034254720 scopus 로고    scopus 로고
    • Sticky-end assembly of a designed peptide fiber provides insight into protein fibrillogenesis
    • M.J. Pandya, G.M. Spooner, M. Sunde, J.R. Thorpe, A. Rodger, and D.N. Woolfson Sticky-end assembly of a designed peptide fiber provides insight into protein fibrillogenesis Biochemistry 39 2000 8728 8734
    • (2000) Biochemistry , vol.39 , pp. 8728-8734
    • Pandya, M.J.1    Spooner, G.M.2    Sunde, M.3    Thorpe, J.R.4    Rodger, A.5    Woolfson, D.N.6
  • 8
    • 3343012154 scopus 로고    scopus 로고
    • Rational design of a nanoscale helical scaffold derived from self-assembly of a dimeric coiled coil motif
    • Y. Zimenkov, V.P. Conticello, L. Guo, and P. Thiyagarajan Rational design of a nanoscale helical scaffold derived from self-assembly of a dimeric coiled coil motif Tetrahedron 60 2004 7237 7246
    • (2004) Tetrahedron , vol.60 , pp. 7237-7246
    • Zimenkov, Y.1    Conticello, V.P.2    Guo, L.3    Thiyagarajan, P.4
  • 9
    • 23044460531 scopus 로고    scopus 로고
    • Towards the development of peptide nanofilaments and nanoropes as smart materials
    • in press.
    • Wagner DE, Phillips CL, Lee LS, Ali WM, Nybakken EN, Crawford ED, Schwab AD, Smith WF, Fairman R: Towards the development of peptide nanofilaments and nanoropes as smart materials. Proc Natl Acad Sci USA 2005, in press. A study focusing on the design and synthesis of coiled-coil filaments, with an explicit focus on smart behavior. The filaments are characterized both in solution and on a surface.
    • (2005) Proc Natl Acad Sci USA
    • Wagner, D.E.1    Phillips, C.L.2    Lee, L.S.3    Ali, W.M.4    Nybakken, E.N.5    Crawford, E.D.6    Schwab, A.D.7    Smith, W.F.8    Fairman, R.9
  • 10
    • 1442359484 scopus 로고    scopus 로고
    • Shift of fibril-forming ability of the designed alpha-helical coiled-coil peptides into the physiological pH region
    • T.N. Melnik, V. Villard, V. Vasiliev, G. Corradin, A.V. Kajava, and S.A. Potekhin Shift of fibril-forming ability of the designed alpha-helical coiled-coil peptides into the physiological pH region Protein Eng 16 2003 1125 1130
    • (2003) Protein Eng , vol.16 , pp. 1125-1130
    • Melnik, T.N.1    Villard, V.2    Vasiliev, V.3    Corradin, G.4    Kajava, A.V.5    Potekhin, S.A.6
  • 11
    • 9444231571 scopus 로고    scopus 로고
    • Engineered and designed peptide-based fibrous biomaterials
    • C.E. MacPhee, and D.N. Woolfson Engineered and designed peptide-based fibrous biomaterials Curr Opin Solid State Mat Sci 8 2004 141 149
    • (2004) Curr Opin Solid State Mat Sci , vol.8 , pp. 141-149
    • MacPhee, C.E.1    Woolfson, D.N.2
  • 12
    • 0036667735 scopus 로고    scopus 로고
    • Designing supramolecular protein assemblies
    • T.O. Yeates, and J.E. Padilla Designing supramolecular protein assemblies Curr Opin Struct Biol 12 2002 464 470
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 464-470
    • Yeates, T.O.1    Padilla, J.E.2
  • 13
    • 0041707928 scopus 로고    scopus 로고
    • Belt and braces: A peptide-based linker system of de novo design
    • M.G. Ryadnov, B. Ceyhan, C.M. Niemeyer, and D.N. Woolfson Belt and braces: a peptide-based linker system of de novo design J Am Chem Soc 125 2003 9388 9394
    • (2003) J Am Chem Soc , vol.125 , pp. 9388-9394
    • Ryadnov, M.G.1    Ceyhan, B.2    Niemeyer, C.M.3    Woolfson, D.N.4
  • 14
    • 0041305916 scopus 로고    scopus 로고
    • Introducing branches into a self-assembling peptide fiber
    • M.G. Ryadnov, and D.N. Woolfson Introducing branches into a self-assembling peptide fiber Angew Chem Int Ed Engl 42 2003 3021 3023 A nice example of the use of orthogonal chemistry to create very well defined branched fibrils.
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 3021-3023
    • Ryadnov, M.G.1    Woolfson, D.N.2
  • 15
    • 0037844737 scopus 로고    scopus 로고
    • Engineering the morphology of a self-assembling protein fibre
    • M.G. Ryadnov, and D.N. Woolfson Engineering the morphology of a self-assembling protein fibre Nat Mater 2 2003 329 332 The very clever use of orthogonal chemistry to create branched peptides that can introduce kinks and waves into peptide fibrils. This provides a mechanism to allow patterning of irregularly shaped surfaces with a high persistence length material.
    • (2003) Nat Mater , vol.2 , pp. 329-332
    • Ryadnov, M.G.1    Woolfson, D.N.2
  • 17
  • 18
    • 2942630633 scopus 로고    scopus 로고
    • Fiber recruiting peptides: Noncovalent decoration of an engineered protein scaffold
    • M.G. Ryadnov, and D.N. Woolfson Fiber recruiting peptides: noncovalent decoration of an engineered protein scaffold J Am Chem Soc 126 2004 7454 7455
    • (2004) J Am Chem Soc , vol.126 , pp. 7454-7455
    • Ryadnov, M.G.1    Woolfson, D.N.2
  • 19
    • 3342991494 scopus 로고    scopus 로고
    • Experimental investigation of protein folding and misfolding
    • C.M. Dobson Experimental investigation of protein folding and misfolding Methods 34 2004 4 14
    • (2004) Methods , vol.34 , pp. 4-14
    • Dobson, C.M.1
  • 20
    • 13844281391 scopus 로고    scopus 로고
    • Design of model systems for amyloid formation: Lessons for prediction and inhibition
    • M.T. Pastor, A. Esteras-Chopo, and M. Lopez de la Paz Design of model systems for amyloid formation: lessons for prediction and inhibition Curr Opin Struct Biol 15 2005 57 63
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 57-63
    • Pastor, M.T.1    Esteras-Chopo, A.2    Lopez De La Paz, M.3
  • 23
    • 0033937682 scopus 로고    scopus 로고
    • Conformational behavior of ionic self-complementary peptides
    • M. Altman, P. Lee, A. Rich, and S. Zhang Conformational behavior of ionic self-complementary peptides Protein Sci 9 2000 1095 1105
    • (2000) Protein Sci , vol.9 , pp. 1095-1105
    • Altman, M.1    Lee, P.2    Rich, A.3    Zhang, S.4
  • 24
    • 0034665227 scopus 로고    scopus 로고
    • Mutational analysis of designed peptides that undergo structural transition from α helix to β sheet and amyloid fibril formation
    • Y. Takahashi, A. Ueno, and H. Mihara Mutational analysis of designed peptides that undergo structural transition from α helix to β sheet and amyloid fibril formation Structure 8 2000 915 925
    • (2000) Structure , vol.8 , pp. 915-925
    • Takahashi, Y.1    Ueno, A.2    Mihara, H.3
  • 25
    • 0037155826 scopus 로고    scopus 로고
    • A designed system for assessing how sequence affects α to β conformational transitions in proteins
    • B. Ciani, E.G. Hutchinson, R.B. Sessions, and D.N. Woolfson A designed system for assessing how sequence affects α to β conformational transitions in proteins J Biol Chem 277 2002 10150 10155
    • (2002) J Biol Chem , vol.277 , pp. 10150-10155
    • Ciani, B.1    Hutchinson, E.G.2    Sessions, R.B.3    Woolfson, D.N.4
  • 29
    • 0034680365 scopus 로고    scopus 로고
    • Controlling beta-sheet assembly in genetically engineered silk by enzymatic phosphorylation/dephosphorylation
    • S. Winkler, D. Wilson, and D.L. Kaplan Controlling beta-sheet assembly in genetically engineered silk by enzymatic phosphorylation/dephosphorylation Biochemistry 39 2000 12739 12746
    • (2000) Biochemistry , vol.39 , pp. 12739-12746
    • Winkler, S.1    Wilson, D.2    Kaplan, D.L.3
  • 31
    • 0034023387 scopus 로고    scopus 로고
    • Conformational transitions in model silk peptides
    • D. Wilson, R. Valluzzi, and D. Kaplan Conformational transitions in model silk peptides Biophys J 78 2000 2690 2701
    • (2000) Biophys J , vol.78 , pp. 2690-2701
    • Wilson, D.1    Valluzzi, R.2    Kaplan, D.3
  • 32
    • 14044250010 scopus 로고    scopus 로고
    • 13C cross-polarization/magic-angle spinning NMR study
    • 13C cross-polarization/magic-angle spinning NMR study Biomacromolecules 6 2005 468 474 This careful structural study of the role of simple sequence motifs in regulating the transition between silk I and silk II forms builds on previous solid work from this laboratory.
    • (2005) Biomacromolecules , vol.6 , pp. 468-474
    • Asakura, T.1    Ohgo, K.2    Ishida, T.3    Taddei, P.4    Monti, P.5    Kishore, R.6
  • 33
    • 0042737803 scopus 로고    scopus 로고
    • 13C-cross-polarization/magic angle spinning NMR spectroscopic and thermal characterization of poly(alanine-glycine) as model for silk I Bombyx mori fibroin
    • 13C-cross-polarization/magic angle spinning NMR spectroscopic and thermal characterization of poly(alanine-glycine) as model for silk I Bombyx mori fibroin Biopolymers 72 2003 329 338
    • (2003) Biopolymers , vol.72 , pp. 329-338
    • Monti, P.1    Taddei, P.2    Freddi, G.3    Ohgo, K.4    Asakura, T.5
  • 34
    • 0038451228 scopus 로고    scopus 로고
    • Structure determination of a peptide model of the repeated helical domain in Samia cynthia ricini silk fibroin before spinning by a combination of advanced solid-state NMR methods
    • Y. Nakazawa, and T. Asakura Structure determination of a peptide model of the repeated helical domain in Samia cynthia ricini silk fibroin before spinning by a combination of advanced solid-state NMR methods J Am Chem Soc 125 2003 7230 7237
    • (2003) J Am Chem Soc , vol.125 , pp. 7230-7237
    • Nakazawa, Y.1    Asakura, T.2
  • 35
    • 7544240159 scopus 로고    scopus 로고
    • Raman study of poly(alanine-glycine)-based peptides containing tyrosine, valine, and serine as model for the semicrystalline domains of Bombyx mori silk fibroin
    • P. Taddei, T. Asakura, J. Yao, and P. Monti Raman study of poly(alanine-glycine)-based peptides containing tyrosine, valine, and serine as model for the semicrystalline domains of Bombyx mori silk fibroin Biopolymers 75 2004 314 324
    • (2004) Biopolymers , vol.75 , pp. 314-324
    • Taddei, P.1    Asakura, T.2    Yao, J.3    Monti, P.4
  • 36
  • 37
    • 0037466613 scopus 로고    scopus 로고
    • Casting metal nanowires within discrete self-assembled peptide nanotubes
    • M. Reches, and E. Gazit Casting metal nanowires within discrete self-assembled peptide nanotubes Science 300 2003 625 627 An insightful approach to casting nanowires. The idea of coating the interior of a peptide nanotube with ionic silver was clever and creative. This work opens up a wide range of possibilities for future smart design of nanowires and nanocircuits.
    • (2003) Science , vol.300 , pp. 625-627
    • Reches, M.1    Gazit, E.2
  • 38
    • 0037146030 scopus 로고    scopus 로고
    • Au nanowire fabrication from sequenced histidine-rich peptide
    • R. Djalali, Y.F. Chen, and H. Matsui Au nanowire fabrication from sequenced histidine-rich peptide J Am Chem Soc 124 2002 13660 13661
    • (2002) J Am Chem Soc , vol.124 , pp. 13660-13661
    • Djalali, R.1    Chen, Y.F.2    Matsui, H.3
  • 41
    • 0035834113 scopus 로고    scopus 로고
    • Hierarchical self-assembly of chiral rod-like molecules as a model for peptide beta-sheet tapes, ribbons, fibrils, and fibers
    • A. Aggeli, I.A. Nyrkova, M. Bell, R. Harding, L. Carrick, T.C. McLeish, A.N. Semenov, and N. Boden Hierarchical self-assembly of chiral rod-like molecules as a model for peptide beta-sheet tapes, ribbons, fibrils, and fibers Proc Natl Acad Sci USA 98 2001 11857 11862
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11857-11862
    • Aggeli, A.1    Nyrkova, I.A.2    Bell, M.3    Harding, R.4    Carrick, L.5    McLeish, T.C.6    Semenov, A.N.7    Boden, N.8
  • 42
    • 0345550440 scopus 로고    scopus 로고
    • Structures of helical beta-tapes and twisted ribbons: The role of side-chain interactions on twist and bend behavior
    • C.W.G. Fishwick, A.J. Beevers, L.M. Carrick, C.D. Whitehouse, A. Aggeli, and N. Boden Structures of helical beta-tapes and twisted ribbons: the role of side-chain interactions on twist and bend behavior Nano Lett 3 2003 1475 1479 This beautiful molecular dynamics study provides insights into the origins of the twist, bend and helical pitch of the tape-like β-sheet structures formed by the de novo designed sequences investigated by this group.
    • (2003) Nano Lett , vol.3 , pp. 1475-1479
    • Fishwick, C.W.G.1    Beevers, A.J.2    Carrick, L.M.3    Whitehouse, C.D.4    Aggeli, A.5    Boden, N.6
  • 44
    • 0141765883 scopus 로고    scopus 로고
    • Fabrication of novel biomaterials through molecular self-assembly
    • S. Zhang Fabrication of novel biomaterials through molecular self-assembly Nat Biotechnol 21 2003 1171 1178 One of the more comprehensive reviews on the recent work by Zhang and co-workers.
    • (2003) Nat Biotechnol , vol.21 , pp. 1171-1178
    • Zhang, S.1
  • 45
    • 4043175498 scopus 로고    scopus 로고
    • Design of molecular biological materials using peptide motifs
    • S.G. Zhang, and X.J. Zhao Design of molecular biological materials using peptide motifs J Mater Chem 14 2004 2082 2086 A good review with specific focus on the self-assembling properties of peptide Lego®.
    • (2004) J Mater Chem , vol.14 , pp. 2082-2086
    • Zhang, S.G.1    Zhao, X.J.2
  • 46
    • 0037162463 scopus 로고    scopus 로고
    • Self-assembling peptide hydrogel fosters chondrocyte extracellular matrix production and cell division: Implications for cartilage tissue repair
    • J. Kisiday, M. Jin, B. Kurz, H. Hung, C. Semino, S. Zhang, and A.J. Grodzinsky Self-assembling peptide hydrogel fosters chondrocyte extracellular matrix production and cell division: Implications for cartilage tissue repair Proc Natl Acad Sci USA 99 2002 9996 10001
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9996-10001
    • Kisiday, J.1    Jin, M.2    Kurz, B.3    Hung, H.4    Semino, C.5    Zhang, S.6    Grodzinsky, A.J.7
  • 47
    • 0037132592 scopus 로고    scopus 로고
    • Responsive hydrogels from the intramolecular folding and self-assembly of a designed peptide
    • J.P. Schneider, D.J. Pochan, B. Ozbas, K. Rajagopal, L. Pakstis, and J. Kretsinger Responsive hydrogels from the intramolecular folding and self-assembly of a designed peptide J Am Chem Soc 124 2002 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
  • 48
    • 4744350913 scopus 로고    scopus 로고
    • Salt-triggered peptide folding and consequent self-assembly into hydrogels with tunable modulus
    • B. Ozbas, J. Kretsinger, K. Rajagopal, J.P. Schneider, and D.J. Pochan Salt-triggered peptide folding and consequent self-assembly into hydrogels with tunable modulus Macromolecules 37 2004 7331 7337
    • (2004) Macromolecules , vol.37 , pp. 7331-7337
    • Ozbas, B.1    Kretsinger, J.2    Rajagopal, K.3    Schneider, J.P.4    Pochan, D.J.5
  • 49
    • 0141596163 scopus 로고    scopus 로고
    • Thermally reversible hydrogels via intramolecular folding and consequent self-assembly of a de novo designed peptide
    • D.J. Pochan, J.P. Schneider, J. Kretsinger, B. Ozbas, K. Rajagopal, and L. Haines Thermally reversible hydrogels via intramolecular folding and consequent self-assembly of a de novo designed peptide J Am Chem Soc 125 2003 11802 11803
    • (2003) J Am Chem Soc , vol.125 , pp. 11802-11803
    • Pochan, D.J.1    Schneider, J.P.2    Kretsinger, J.3    Ozbas, B.4    Rajagopal, K.5    Haines, L.6
  • 51
    • 0035941074 scopus 로고    scopus 로고
    • Self-assembly and mineralization of peptide-amphiphile nanofibers
    • J.D. Hartgerink, E. Beniash, and S.I. Stupp Self-assembly and mineralization of peptide-amphiphile nanofibers Science 294 2001 1684 1688
    • (2001) Science , vol.294 , pp. 1684-1688
    • Hartgerink, J.D.1    Beniash, E.2    Stupp, S.I.3
  • 52
    • 5644287379 scopus 로고    scopus 로고
    • Semiconductor-encapsulated peptide-amphiphile nanofibers
    • E.D. Sone, and S.I. Stupp Semiconductor-encapsulated peptide-amphiphile nanofibers J Am Chem Soc 126 2004 12756 12757 The same peptide amphiphile fiber system that was used in earlier studies to promote the nucleation of hydroxyapatite [51] was used to mineralize semiconducting CdS particles onto its surface.
    • (2004) J Am Chem Soc , vol.126 , pp. 12756-12757
    • Sone, E.D.1    Stupp, S.I.2
  • 53
    • 0036139571 scopus 로고    scopus 로고
    • Novel peptide-based biomaterial scaffolds for tissue engineering
    • T.C. Holmes Novel peptide-based biomaterial scaffolds for tissue engineering Trends Biotechnol 20 2002 16 21
    • (2002) Trends Biotechnol , vol.20 , pp. 16-21
    • Holmes, T.C.1
  • 54
    • 1442281238 scopus 로고    scopus 로고
    • Selective differentiation of neural progenitor cells by high-epitope density nanofibers
    • G.A. Silva, C. Czeisler, K.L. Niece, E. Beniash, D.A. Harrington, J.A. Kessler, and S.I. Stupp Selective differentiation of neural progenitor cells by high-epitope density nanofibers Science 303 2004 1352 1355 This is an interesting paper of particular significance to the field of tissue regeneration. A self-assembling peptide amphiphile, tagged with a neurite-promoting laminin epitope, was used for the purpose of inducing neural progenitor cells to differentiate into neurons.
    • (2004) Science , vol.303 , pp. 1352-1355
    • Silva, G.A.1    Czeisler, C.2    Niece, K.L.3    Beniash, E.4    Harrington, D.A.5    Kessler, J.A.6    Stupp, S.I.7
  • 55
    • 16344364905 scopus 로고    scopus 로고
    • American Chemical Society meeting. Nanofibers seed blood vessels
    • R.F. Service American Chemical Society meeting. Nanofibers seed blood vessels Science 308 2005 44 45
    • (2005) Science , vol.308 , pp. 44-45
    • Service, R.F.1
  • 56
    • 14644438367 scopus 로고    scopus 로고
    • Presentation and recognition of biotin on nanofibers formed by branched peptide amphiphiles
    • M.O. Guler, S. Soukasene, J.F. Hulvat, and S.I. Stupp Presentation and recognition of biotin on nanofibers formed by branched peptide amphiphiles Nano Lett 5 2005 249 252
    • (2005) Nano Lett , vol.5 , pp. 249-252
    • Guler, M.O.1    Soukasene, S.2    Hulvat, J.F.3    Stupp, S.I.4
  • 57
    • 12844286898 scopus 로고    scopus 로고
    • Self-assembled peptide amphiphile nanofibers conjugated to MRI contrast agents
    • S.R. Bull, M.O. Guler, R.E. Bras, T.J. Meade, and S.I. Stupp Self-assembled peptide amphiphile nanofibers conjugated to MRI contrast agents Nano Lett 5 2005 1 4
    • (2005) Nano Lett , vol.5 , pp. 1-4
    • Bull, S.R.1    Guler, M.O.2    Bras, R.E.3    Meade, T.J.4    Stupp, S.I.5
  • 58
    • 0034001783 scopus 로고    scopus 로고
    • Peptide-mediated cellular delivery
    • J.J. Schwartz, and S. Zhang Peptide-mediated cellular delivery Curr Opin Mol Ther 2 2000 162 167
    • (2000) Curr Opin Mol Ther , vol.2 , pp. 162-167
    • Schwartz, J.J.1    Zhang, S.2
  • 59
    • 0038237370 scopus 로고    scopus 로고
    • Positively charged surfactant-like peptides self-assemble into nanostructures
    • G. von Maltzahn, S. Vauthey, S. Santoso, and S.U. Zhang Positively charged surfactant-like peptides self-assemble into nanostructures Langmuir 19 2003 4332 4337 The properties of a series of positively charged surfactant peptides that self-assemble to form interesting micellar tubes and spheres are investigated. These constructs are envisioned to be useful in gene delivery.
    • (2003) Langmuir , vol.19 , pp. 4332-4337
    • Von Maltzahn, G.1    Vauthey, S.2    Santoso, S.3    Zhang, S.U.4
  • 60
    • 33544464905 scopus 로고    scopus 로고
    • Delivering the goods: Gene therapy without the virus
    • J. Gorman Delivering the goods: gene therapy without the virus Sci News 163 2003 43 44
    • (2003) Sci News , vol.163 , pp. 43-44
    • Gorman, J.1
  • 61
    • 4344576758 scopus 로고    scopus 로고
    • Fabrication of molecular materials using peptide construction motifs
    • X. Zhao, and S. Zhang Fabrication of molecular materials using peptide construction motifs Trends Biotechnol 22 2004 470 476
    • (2004) Trends Biotechnol , vol.22 , pp. 470-476
    • Zhao, X.1    Zhang, S.2
  • 64
    • 1642453555 scopus 로고    scopus 로고
    • Helical supramolecules and fibers utilizing leucine zipper-displaying dendrimers
    • M. Zhou, D. Bentley, and I. Ghosh Helical supramolecules and fibers utilizing leucine zipper-displaying dendrimers J Am Chem Soc 126 2004 734 735 A rare example of dendrimer design that incorporates structural considerations in the peptide component. There are many opportunities now to take advantage of such a system to design smart behavior.
    • (2004) J Am Chem Soc , vol.126 , pp. 734-735
    • Zhou, M.1    Bentley, D.2    Ghosh, I.3
  • 66
    • 0028330850 scopus 로고
    • Electrostatic interactions control the parallel and antiparallel orientation of alpha-helical chains in two-stranded alpha-helical coiled-coils
    • O.D. Monera, C.M. Kay, and R.S. Hodges Electrostatic interactions control the parallel and antiparallel orientation of alpha-helical chains in two-stranded alpha-helical coiled-coils Biochemistry 33 1994 3862 3871
    • (1994) Biochemistry , vol.33 , pp. 3862-3871
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 67
    • 0029008590 scopus 로고
    • A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil
    • K.J. Lumb, and P.S. Kim A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil Biochemistry 34 1995 8642 8648
    • (1995) Biochemistry , vol.34 , pp. 8642-8648
    • Lumb, K.J.1    Kim, P.S.2
  • 68
    • 0041696586 scopus 로고    scopus 로고
    • Nanoscale structure of poly(ethylene glycol) hybrid block copolymers containing amphiphilic beta-strand peptide sequences
    • A. Rosler, H.A. Klok, I.W. Hamley, V. Castelletto, and O.O. Mykhaylyk Nanoscale structure of poly(ethylene glycol) hybrid block copolymers containing amphiphilic beta-strand peptide sequences Biomacromolecules 4 2003 859 863
    • (2003) Biomacromolecules , vol.4 , pp. 859-863
    • Rosler, A.1    Klok, H.A.2    Hamley, I.W.3    Castelletto, V.4    Mykhaylyk, O.O.5
  • 69
    • 2442532695 scopus 로고    scopus 로고
    • Structure and dynamics of self-assembled poly(ethylene glycol) based coiled-coil nano-objects
    • G.W. Vandermeulen, D. Hinderberger, H. Xu, S.S. Sheiko, G. Jeschke, and H.A. Klok Structure and dynamics of self-assembled poly(ethylene glycol) based coiled-coil nano-objects ChemPhysChem 5 2004 488 494
    • (2004) ChemPhysChem , vol.5 , pp. 488-494
    • Vandermeulen, G.W.1    Hinderberger, D.2    Xu, H.3    Sheiko, S.S.4    Jeschke, G.5    Klok, H.A.6
  • 70
    • 13444267957 scopus 로고    scopus 로고
    • PEG-based hybrid block copolymers containing alpha-helical coiled coil peptide sequences: Control of self-assembly and preliminary biological evaluation
    • G.W.M. Vandermeulen, C. Tziatzios, R. Duncan, and H.A. Klok PEG-based hybrid block copolymers containing alpha-helical coiled coil peptide sequences: control of self-assembly and preliminary biological evaluation Macromolecules 38 2005 761 769
    • (2005) Macromolecules , vol.38 , pp. 761-769
    • Vandermeulen, G.W.M.1    Tziatzios, C.2    Duncan, R.3    Klok, H.A.4
  • 71
    • 4544230234 scopus 로고    scopus 로고
    • Peptide/protein hybrid materials: Enhanced control of structure and improved performance through conjugation of biological and synthetic polymers
    • G.W. Vandermeulen, and H.A. Klok Peptide/protein hybrid materials: enhanced control of structure and improved performance through conjugation of biological and synthetic polymers Macromol Biosci 4 2004 383 398
    • (2004) Macromol Biosci , vol.4 , pp. 383-398
    • Vandermeulen, G.W.1    Klok, H.A.2
  • 72
    • 14044274349 scopus 로고    scopus 로고
    • α-Helix formation in a photoswitchable peptide tracked from picoseconds to microseconds by time-resolved IR spectroscopy
    • J. Bredenbeck, J. Helbing, J.R. Kumita, G.A. Woolley, and P. Hamm α-Helix formation in a photoswitchable peptide tracked from picoseconds to microseconds by time-resolved IR spectroscopy Proc Natl Acad Sci USA 102 2005 2379 2384 The latest example of the power of what can be learned by incorporating a reversible photoswitch into peptides and proteins. The ability to study very fast processes with this system is almost unparalleled. The development of the use of azobenzene for photoswitching in proteins is a wonderful story and each of the papers cited in this review deserve recognition.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 2379-2384
    • Bredenbeck, J.1    Helbing, J.2    Kumita, J.R.3    Woolley, G.A.4    Hamm, P.5
  • 74
    • 0141885404 scopus 로고    scopus 로고
    • The kinetics of helix unfolding of an azobenzene cross-linked peptide probed by nanosecond time-resolved optical rotatory dispersion
    • E. Chen, J.R. Kumita, G.A. Woolley, and D.S. Kliger The kinetics of helix unfolding of an azobenzene cross-linked peptide probed by nanosecond time-resolved optical rotatory dispersion J Am Chem Soc 125 2003 12443 12449
    • (2003) J Am Chem Soc , vol.125 , pp. 12443-12449
    • Chen, E.1    Kumita, J.R.2    Woolley, G.A.3    Kliger, D.S.4
  • 75
    • 0036009333 scopus 로고    scopus 로고
    • Using an azobenzene cross-linker to either increase or decrease peptide helix content upon trans-to-cis photoisomerization
    • D.G. Flint, J.R. Kumita, O.S. Smart, and G.A. Woolley Using an azobenzene cross-linker to either increase or decrease peptide helix content upon trans-to-cis photoisomerization Chem Biol 9 2002 391 397
    • (2002) Chem Biol , vol.9 , pp. 391-397
    • Flint, D.G.1    Kumita, J.R.2    Smart, O.S.3    Woolley, G.A.4
  • 76
    • 0036655377 scopus 로고    scopus 로고
    • Photo-control of peptide helix content by an azobenzene cross-linker: Steric interactions with underlying residues are not critical
    • J.R. Kumita, D.G. Flint, O.S. Smart, and G.A. Woolley Photo-control of peptide helix content by an azobenzene cross-linker: steric interactions with underlying residues are not critical Protein Eng 15 2002 561 569
    • (2002) Protein Eng , vol.15 , pp. 561-569
    • Kumita, J.R.1    Flint, D.G.2    Smart, O.S.3    Woolley, G.A.4
  • 78
    • 9244244782 scopus 로고    scopus 로고
    • Reversible photocontrol of peptide helix content: Adjusting thermal stability of the cis state
    • N. Pozhidaeva, M.E. Cormier, A. Chaudhari, and G.A. Woolley Reversible photocontrol of peptide helix content: adjusting thermal stability of the cis state Bioconjug Chem 15 2004 1297 1303
    • (2004) Bioconjug Chem , vol.15 , pp. 1297-1303
    • Pozhidaeva, N.1    Cormier, M.E.2    Chaudhari, A.3    Woolley, G.A.4
  • 79
    • 0037778822 scopus 로고    scopus 로고
    • A water-soluble azobenzene cross-linker for photocontrol of peptide conformation
    • Z. Zhang, D.C. Burns, J.R. Kumita, O.S. Smart, and G.A. Woolley A water-soluble azobenzene cross-linker for photocontrol of peptide conformation Bioconjug Chem 14 2003 824 829
    • (2003) Bioconjug Chem , vol.14 , pp. 824-829
    • Zhang, Z.1    Burns, D.C.2    Kumita, J.R.3    Smart, O.S.4    Woolley, G.A.5
  • 80
    • 0037795660 scopus 로고    scopus 로고
    • Achieving photo-control of protein conformation and activity: Producing a photo-controlled leucine zipper
    • J.R. Kumita, D.G. Flint, G.A. Woolley, and O.S. Smart Achieving photo-control of protein conformation and activity: producing a photo-controlled leucine zipper Faraday Discuss 122 2003 89 103 171-190
    • (2003) Faraday Discuss , vol.122 , pp. 89-103
    • Kumita, J.R.1    Flint, D.G.2    Woolley, G.A.3    Smart, O.S.4
  • 81
    • 23044438711 scopus 로고    scopus 로고
    • Self-assembling porphyrin-modified peptides
    • J.R. Dunetz, C. Sandstrom, E.R. Young, P. Baker, S.A. Van Name, T. Cathopoulos, R. Fairman, J.C. de Paula, and K.S. Åkerfeldt Self-assembling porphyrin-modified peptides Org Lett 7 2005 2559 2561 This work represents the first reported example of a peptide-porphyrin hybrid that self-assembles in a pH- and temperature-dependent manner to form an organized and unique structure. The construct has potential in electronic and light-harvesting applications.
    • (2005) Org Lett , vol.7 , pp. 2559-2561
    • Dunetz, J.R.1    Sandstrom, C.2    Young, E.R.3    Baker, P.4    Van Name, S.A.5    Cathopoulos, T.6    Fairman, R.7    De Paula, J.C.8    Åkerfeldt, K.S.9
  • 82
    • 13444302392 scopus 로고    scopus 로고
    • Computational de novo design and characterization of a four-helix bundle protein that selectively binds a nonbiological cofactor
    • F.V. Cochran, S.P. Wu, W. Wang, V. Nanda, J.G. Saven, M.J. Therien, and W.F. Degrado Computational de novo design and characterization of a four-helix bundle protein that selectively binds a nonbiological cofactor J Am Chem Soc 127 2005 1346 1347
    • (2005) J Am Chem Soc , vol.127 , pp. 1346-1347
    • Cochran, F.V.1    Wu, S.P.2    Wang, W.3    Nanda, V.4    Saven, J.G.5    Therien, M.J.6    Degrado, W.F.7
  • 83
    • 0033992155 scopus 로고    scopus 로고
    • Self-assembled complexes of oligopeptides and metalloporphyrins: Measurements of the reorganization and electronic interaction energies for photoinduced electron-transfer reactions
    • M. Aoudia, A.B. Guliaev, N.B. Leontis, and M.A.J. Rodgers Self-assembled complexes of oligopeptides and metalloporphyrins: measurements of the reorganization and electronic interaction energies for photoinduced electron-transfer reactions Biophys Chem 83 2000 121 140
    • (2000) Biophys Chem , vol.83 , pp. 121-140
    • Aoudia, M.1    Guliaev, A.B.2    Leontis, N.B.3    Rodgers, M.A.J.4
  • 84
    • 0037999855 scopus 로고    scopus 로고
    • Self-assembling of the porphyrin-linked acyclic penta- and heptapeptides in aqueous trifluoroethanol
    • T. Arai, M. Inudo, T. Ishimatsu, C. Akamatsu, Y. Tokusaki, T. Sasaki, and N. Nishino Self-assembling of the porphyrin-linked acyclic penta- and heptapeptides in aqueous trifluoroethanol J Org Chem 68 2003 5540 5549
    • (2003) J Org Chem , vol.68 , pp. 5540-5549
    • Arai, T.1    Inudo, M.2    Ishimatsu, T.3    Akamatsu, C.4    Tokusaki, Y.5    Sasaki, T.6    Nishino, N.7
  • 86
    • 8844258037 scopus 로고    scopus 로고
    • Peptide self-assembly as a model of proteins in the pre-genomic world
    • I. Ghosh, and J. Chmielewski Peptide self-assembly as a model of proteins in the pre-genomic world Curr Opin Chem Biol 8 2004 640 644
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 640-644
    • Ghosh, I.1    Chmielewski, J.2
  • 87
    • 0141620313 scopus 로고    scopus 로고
    • Peptide self-replication enhanced by a proline kink
    • X. Li, and J. Chmielewski Peptide self-replication enhanced by a proline kink J Am Chem Soc 125 2003 11820 11821
    • (2003) J Am Chem Soc , vol.125 , pp. 11820-11821
    • Li, X.1    Chmielewski, J.2
  • 88
    • 0042821707 scopus 로고    scopus 로고
    • Challenges in the design of self replicating peptides
    • X. Li, and J. Chmielewski Challenges in the design of self replicating peptides Org Biomol Chem 1 2003 901 904
    • (2003) Org Biomol Chem , vol.1 , pp. 901-904
    • Li, X.1    Chmielewski, J.2
  • 91
    • 17944373131 scopus 로고    scopus 로고
    • Toward intelligent molecular machines: Directed motions of biological and artificial molecules and assemblies
    • K. Kinbara, and T. Aida Toward intelligent molecular machines: directed motions of biological and artificial molecules and assemblies Chem Rev 105 2005 1377 1400 An interesting and broad review highlighting the significant recent advances that have been made in understanding the inner workings of biological nanomachines. Artificial molecular machines, consisting of interlocked catenanes and rotaxanes with movable components, are also discussed and compared to their biological counterparts.
    • (2005) Chem Rev , vol.105 , pp. 1377-1400
    • Kinbara, K.1    Aida, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.