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1
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0037117591
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Beyond molecules: Self-assembly of mesoscopic and macroscopic components
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In addition to offering a general perspective on self-assembly, this excellent review envisions the potential of self-assembly as extending beyond molecules to the realm of macroscopic objects.
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Whitesides G.M., Boncheva M. Beyond molecules: self-assembly of mesoscopic and macroscopic components. Proc Natl Acad Sci USA. 99:2002;4769-4774. In addition to offering a general perspective on self-assembly, this excellent review envisions the potential of self-assembly as extending beyond molecules to the realm of macroscopic objects.
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(2002)
Proc Natl Acad Sci USA
, vol.99
, pp. 4769-4774
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Whitesides, G.M.1
Boncheva, M.2
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2
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0032541038
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Reversible hydrogels from self-assembling artificial proteins
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Petka W.A., Harden J.L., McGrath K.P., Wirtz D., Tirrell D.A. Reversible hydrogels from self-assembling artificial proteins. Science. 281:1998;389-392.
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(1998)
Science
, vol.281
, pp. 389-392
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Petka, W.A.1
Harden, J.L.2
McGrath, K.P.3
Wirtz, D.4
Tirrell, D.A.5
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3
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0034612266
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Extensive neurite outgrowth and active neuronal synapses on peptide scaffolds
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This is the first report of a primary neuron culture in a transportable peptide scaffold where neuronal networks do not adhere onto a solid Petri dish. It also showed full functional activity of neurons, which formed active connections: an important step for neuro-repair. This paper opened a new research avenue: production of movable scaffolds for functional cell culture.
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Holmes T.C., Delacalle S., Su X., Rich A., Zhang S. Extensive neurite outgrowth and active neuronal synapses on peptide scaffolds. Proc Natl Acad Sci USA. 97:2000;6728-6733. This is the first report of a primary neuron culture in a transportable peptide scaffold where neuronal networks do not adhere onto a solid Petri dish. It also showed full functional activity of neurons, which formed active connections: an important step for neuro-repair. This paper opened a new research avenue: production of movable scaffolds for functional cell culture.
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(2000)
Proc Natl Acad Sci USA
, vol.97
, pp. 6728-6733
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Holmes, T.C.1
Delacalle, S.2
Su, X.3
Rich, A.4
Zhang, S.5
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4
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0033637070
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Chemistry at the crossroads
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Excellent concise review of the design of new biological materials.
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Ghadiri M.R., Tirrell D.A. Chemistry at the crossroads. Curr Opin Chem Biol. 4:2000;661-662. Excellent concise review of the design of new biological materials.
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(2000)
Curr Opin Chem Biol
, vol.4
, pp. 661-662
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Ghadiri, M.R.1
Tirrell, D.A.2
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5
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0035954729
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Antibacterial agents based on the cyclic D,L-alpha-peptide architecture
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This report shows that D-, L-amino acids form stacked nanotubes that can insert into membranes and change their properties. These nano porous structures have potential anti-bacterial activity.
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Fernandez-Lopez S., Kim H.S., Choi E.C., Delgado M., Granja J.R., Khasanov A., Kraehenbuehl K., Long G., Weinberger D.A., Wilcoxen K.M., Ghadiri M.R. Antibacterial agents based on the cyclic D,L-alpha-peptide architecture. Nature. 412:2001;452-455. This report shows that D-, L-amino acids form stacked nanotubes that can insert into membranes and change their properties. These nano porous structures have potential anti-bacterial activity.
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(2001)
Nature
, vol.412
, pp. 452-455
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Fernandez-Lopez, S.1
Kim, H.S.2
Choi, E.C.3
Delgado, M.4
Granja, J.R.5
Khasanov, A.6
Kraehenbuehl, K.7
Long, G.8
Weinberger, D.A.9
Wilcoxen, K.M.10
Ghadiri, M.R.11
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6
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0035834113
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Hierarchical self-assembly of chiral rod-like molecules as a model for peptide beta-sheet tapes, ribbons, fibrils, and fibers
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By using an elastic tape model of the fiber, this paper provides theoretical framework for the organization (bundling) of these fibers.
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Aggeli A., Nyrkova I.A., Bell M., Harding R., Carrick L., McLeish T.C.B., Semenov A.N., Boden N. 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. By using an elastic tape model of the fiber, this paper provides theoretical framework for the organization (bundling) of these fibers.
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(2001)
Proc Natl Acad Sci USA
, vol.98
, pp. 11857-11862
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Aggeli, A.1
Nyrkova, I.A.2
Bell, M.3
Harding, R.4
Carrick, L.5
McLeish, T.C.B.6
Semenov, A.N.7
Boden, N.8
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7
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0000590549
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Left-handed helical ribbon intermediates in the self-assembly of a beta-sheet peptide
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This paper reports the observation - via atomic force microscopy and transmission electron microscopy - of left-handed helical ribbons formed by self-assembly of a β-sheet peptide. The structure of such fibers was investigated using molecular dynamics simulation in concomitance with experimental measurements. Such a method may be applied to the design of other self-assembled materials.
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Marini D.M., Hwang W., Lauffenburger D.A., Zhang S., Kamm R.D. Left-handed helical ribbon intermediates in the self-assembly of a beta-sheet peptide. Nano Letters. 2:2002;295-299. This paper reports the observation - via atomic force microscopy and transmission electron microscopy - of left-handed helical ribbons formed by self-assembly of a β-sheet peptide. The structure of such fibers was investigated using molecular dynamics simulation in concomitance with experimental measurements. Such a method may be applied to the design of other self-assembled materials.
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(2002)
Nano Letters
, vol.2
, pp. 295-299
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Marini, D.M.1
Hwang, W.2
Lauffenburger, D.A.3
Zhang, S.4
Kamm, R.D.5
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8
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0034571041
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Self-assembly of a beta-sheet protein governed by relief of electrostatic repulsion relative to van der Waals attraction
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A systematic analysis of the rheological properties of gels formed by a self-assembling peptide shows that assembly happens upon relief of electrostatic repulsion, in agreement with the DLVO theory.
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Caplan M.R., Moore P.N., Zhang S., Kamm R.D., Lauffenburger D.A. Self-assembly of a beta-sheet protein governed by relief of electrostatic repulsion relative to van der Waals attraction. Biomacromolecules. 1:2000;627-631. A systematic analysis of the rheological properties of gels formed by a self-assembling peptide shows that assembly happens upon relief of electrostatic repulsion, in agreement with the DLVO theory.
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(2000)
Biomacromolecules
, vol.1
, pp. 627-631
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Caplan, M.R.1
Moore, P.N.2
Zhang, S.3
Kamm, R.D.4
Lauffenburger, D.A.5
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9
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0037117535
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Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles
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This is the first reported design of a surfactant peptide. These molecularly designed peptides share many properties with phosphate lipids and non-peptidic surfactant molecules. They form well-ordered nanotubes and nanovesicles that could be useful for a number of applications.
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Vauthey S., Santoso S., Gong H., Watson N., Zhang S. Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles. Proc Natl Acad Sci USA. 99:2002;5355-5360. This is the first reported design of a surfactant peptide. These molecularly designed peptides share many properties with phosphate lipids and non-peptidic surfactant molecules. They form well-ordered nanotubes and nanovesicles that could be useful for a number of applications.
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(2002)
Proc Natl Acad Sci USA
, vol.99
, pp. 5355-5360
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Vauthey, S.1
Santoso, S.2
Gong, H.3
Watson, N.4
Zhang, S.5
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10
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0001608018
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Self-assembly of surfactant-like peptides with variable glycine tails to form nanotubes and nanovesicles
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This report further shows that various lengths of glycines as the hydrophobic tail of surfactant peptides also permit the self-assembly of nanostructures.
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Santoso S., Hwang W., Hartman H., Zhang S. Self-assembly of surfactant-like peptides with variable glycine tails to form nanotubes and nanovesicles. Nano Letters. 2:2002;687-691. This report further shows that various lengths of glycines as the hydrophobic tail of surfactant peptides also permit the self-assembly of nanostructures.
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(2002)
Nano Letters
, vol.2
, pp. 687-691
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Santoso, S.1
Hwang, W.2
Hartman, H.3
Zhang, S.4
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11
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0037117483
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Noncovalent self-assembly of a heterotetrameric diiron protein
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Fourhelical bundle coiled-coil proteins that bind two ions are designed. On addition of ferrous ions and oxygen, the protein forms a complex with a UV-visible spectrum closely resembling that of peroxo-bridged diferric species in natural proteins and model compounds.
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Marsh E.N., DeGrado W.F. Noncovalent self-assembly of a heterotetrameric diiron protein. Proc Natl Acad Sci USA. 99:2002;5150-5154. Fourhelical bundle coiled-coil proteins that bind two ions are designed. On addition of ferrous ions and oxygen, the protein forms a complex with a UV-visible spectrum closely resembling that of peroxo-bridged diferric species in natural proteins and model compounds.
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(2002)
Proc Natl Acad Sci USA
, vol.99
, pp. 5150-5154
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Marsh, E.N.1
DeGrado, W.F.2
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12
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0034801533
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Carbon monoxide binding by de novo heme proteins derived from designed combinatorial libraries
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The authors combinatorially selected heme proteins with biological function from a designed artificial protein library. This study has implications in selecting and evolving proteins for particular purposes. Hecht and colleagues have selected many novel artificial proteins in the past few years.
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Moffet D.A., Case M.A., House J.C., Vogel K., Williams R.D., Spiro T.G., McLendon G.L., Hecht M.H. Carbon monoxide binding by de novo heme proteins derived from designed combinatorial libraries. J Am Chem Soc. 123:2001;2109-2115. The authors combinatorially selected heme proteins with biological function from a designed artificial protein library. This study has implications in selecting and evolving proteins for particular purposes. Hecht and colleagues have selected many novel artificial proteins in the past few years.
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(2001)
J Am Chem Soc
, vol.123
, pp. 2109-2115
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Moffet, D.A.1
Case, M.A.2
House, J.C.3
Vogel, K.4
Williams, R.D.5
Spiro, T.G.6
McLendon, G.L.7
Hecht, M.H.8
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13
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0037161668
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Rapidly recovering hydrogel scaffolds from self-assembling diblock copolypeptide amphiphiles
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The authors designed block co-polymer-type proteins with very interesting properties.
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Nowak A.P., Breedveld V., Pakstis L., Ozbas B., Pine D.J., Pochan D., Deming T.J. Rapidly recovering hydrogel scaffolds from self-assembling diblock copolypeptide amphiphiles. Nature. 417:2002;424-428. The authors designed block co-polymer-type proteins with very interesting properties.
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(2002)
Nature
, vol.417
, pp. 424-428
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Nowak, A.P.1
Breedveld, V.2
Pakstis, L.3
Ozbas, B.4
Pine, D.J.5
Pochan, D.6
Deming, T.J.7
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14
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0034621827
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Selection of peptides with semiconductor binding specificity for directed nanocrystal assembly
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This is the first report to use a bacterial phage library to select binding of several semiconducting elements. Phages can also organize these elements in a defined manner.
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Whaley S.R., English D.S., Hu E.L., Barbara P.F., Belcher A.M. Selection of peptides with semiconductor binding specificity for directed nanocrystal assembly. Nature. 405:2000;665-668. This is the first report to use a bacterial phage library to select binding of several semiconducting elements. Phages can also organize these elements in a defined manner.
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(2000)
Nature
, vol.405
, pp. 665-668
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Whaley, S.R.1
English, D.S.2
Hu, E.L.3
Barbara, P.F.4
Belcher, A.M.5
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15
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0037012921
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Ordering of quantum dots using genetically engineered viruses
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The authors show that bacterial phages can organize inorganic nanostructures on their surface. This work opened a new research avenue: interfacing biology with inorganic molecules.
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Lee S.W., Mao C., Flynn C.E., Belcher A.M. Ordering of quantum dots using genetically engineered viruses. Science. 296:2002;892-895. The authors show that bacterial phages can organize inorganic nanostructures on their surface. This work opened a new research avenue: interfacing biology with inorganic molecules.
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(2002)
Science
, vol.296
, pp. 892-895
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Lee, S.W.1
Mao, C.2
Flynn, C.E.3
Belcher, A.M.4
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16
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0035941074
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Self-assembly and mineralization of peptide-amphiphile nanofibers
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By covalently linking polymers and peptide functional motifs, the authors first demonstrated that calcium atoms can be organized in a desired way, allowing the design of new composite biomaterials for bone repair.
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Hartgerink J.D., Beniash E., Stupp S.I. Self-assembly and mineralization of peptide-amphiphile nanofibers. Science. 294:2001;1684-1687. By covalently linking polymers and peptide functional motifs, the authors first demonstrated that calcium atoms can be organized in a desired way, allowing the design of new composite biomaterials for bone repair.
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(2001)
Science
, vol.294
, pp. 1684-1687
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Hartgerink, J.D.1
Beniash, E.2
Stupp, S.I.3
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17
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0037117498
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Peptide-amphiphile nanofibers: A versatile scaffold for the preparation of self-assembling materials
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The authors expand on the concepts developed in [16••] and demonstrate the high potential of their motif in the design of nanomaterials.
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Hartgerink J.D., Beniash E., Stupp S.I. Peptide-amphiphile nanofibers: a versatile scaffold for the preparation of self-assembling materials. Proc Natl Acad Sci USA. 99:2002;5133-5138. The authors expand on the concepts developed in [16••] and demonstrate the high potential of their motif in the design of nanomaterials.
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(2002)
Proc Natl Acad Sci USA
, vol.99
, pp. 5133-5138
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Hartgerink, J.D.1
Beniash, E.2
Stupp, S.I.3
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18
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0034578141
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Reduction-oxidation control of beta-sheet assembly in genetically engineered silk
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Szela S., Avtges P., Valluzzi R., Winkler S., Wilson D., Kirschner D., Kaplan D.L. Reduction-oxidation control of beta-sheet assembly in genetically engineered silk. Biomacromolecules. 1:2000;534-542.
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(2000)
Biomacromolecules
, vol.1
, pp. 534-542
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Szela, S.1
Avtges, P.2
Valluzzi, R.3
Winkler, S.4
Wilson, D.5
Kirschner, D.6
Kaplan, D.L.7
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19
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0034890489
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Genetically directed synthesis and spectroscopic analysis of a protein polymer derived from a flagelliform silk sequence
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Zhou Y., Wu S., Conticello V.P. Genetically directed synthesis and spectroscopic analysis of a protein polymer derived from a flagelliform silk sequence. Biomacromolecules. 2:2001;111-125.
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(2001)
Biomacromolecules
, vol.2
, pp. 111-125
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Zhou, Y.1
Wu, S.2
Conticello, V.P.3
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20
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0035427372
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Silk fibroin: Structural implications of a remarkable amino acid sequence
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This is a structural analysis of silk fibroin with many repeats. This structure has long eluded many high-resolution studies. For anyone interested in the design of new materials, this is an excellent paper to read.
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Zhou C.Z., Confalonieri F., Jacquet M., Perasso R., Li Z.G., Janin J. Silk fibroin: structural implications of a remarkable amino acid sequence. Proteins. 44:2001;119-122. This is a structural analysis of silk fibroin with many repeats. This structure has long eluded many high-resolution studies. For anyone interested in the design of new materials, this is an excellent paper to read.
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(2001)
Proteins
, vol.44
, pp. 119-122
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Zhou, C.Z.1
Confalonieri, F.2
Jacquet, M.3
Perasso, R.4
Li, Z.G.5
Janin, J.6
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22
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0034894236
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Elastomeric polypentapeptides cross-linked into matrixes and fibers
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Urry and colleagues have spent decades engineering protein materials using selected repeating sequences. These biologically engineered materials have paved the way for many applications.
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Lee J., Macosko C.W., Urry D.W. Elastomeric polypentapeptides cross-linked into matrixes and fibers. Biomacromolecules. 2:2001;170-179. Urry and colleagues have spent decades engineering protein materials using selected repeating sequences. These biologically engineered materials have paved the way for many applications.
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(2001)
Biomacromolecules
, vol.2
, pp. 170-179
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Lee, J.1
Macosko, C.W.2
Urry, D.W.3
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23
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0037192459
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Synthesis beyond the molecule
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An excellent review of supramolecular self-assembly. The authors underline the importance of designing a specific chemical function in the formed structures
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Reinhoudt D.N., Crego-Calama M. Synthesis beyond the molecule. Science. 295:2002;2403-2407. An excellent review of supramolecular self-assembly. The authors underline the importance of designing a specific chemical function in the formed structures.
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(2002)
Science
, vol.295
, pp. 2403-2407
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Reinhoudt, D.N.1
Crego-Calama, M.2
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24
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0033915849
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Nanobiotechnology: The fabrication and applications of chemical and biological nanostructures
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A nice review.
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Lowe C.R. Nanobiotechnology: the fabrication and applications of chemical and biological nanostructures. Curr Opin Struct Biol. 10:2000;428-434. A nice review.
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(2000)
Curr Opin Struct Biol
, vol.10
, pp. 428-434
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Lowe, C.R.1
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25
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0032991195
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Building molecular machine systems
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Drexler K.E. Building molecular machine systems. Trends Biotechnol. 17:1999;5-7.
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(1999)
Trends Biotechnol
, vol.17
, pp. 5-7
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Drexler, K.E.1
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26
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0033169046
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Biotechnology as a route to nanotechnology
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A nice review.
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Merkle R.C. Biotechnology as a route to nanotechnology. Trends Biotechnol. 17:1999;271-274. A nice review.
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(1999)
Trends Biotechnol
, vol.17
, pp. 271-274
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Merkle, R.C.1
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27
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0034929090
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Surfactants for novel templating applications
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A nice review.
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Antonietti M. Surfactants for novel templating applications. Curr Opin Coll Inter Sci. 6:2001;244-248. A nice review.
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(2001)
Curr Opin Coll Inter Sci
, vol.6
, pp. 244-248
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Antonietti, M.1
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28
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0033741820
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Crystalline glycylglycine bolaamphiphile tubules and their pH-sensitive structural transformation
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Matsui H., Gologan B. Crystalline glycylglycine bolaamphiphile tubules and their pH-sensitive structural transformation. J Phys Chem B. 104:2000;3383-3386.
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(2000)
J Phys Chem B
, vol.104
, pp. 3383-3386
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Matsui, H.1
Gologan, B.2
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29
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0347608155
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Metallophorphyrin nanotube fabrication using peptide nanotubes as templates
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Matsui H., MacCuspie R. Metallophorphyrin nanotube fabrication using peptide nanotubes as templates. Nano Letters. 1:2001;671-675.
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(2001)
Nano Letters
, vol.1
, pp. 671-675
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Matsui, H.1
MacCuspie, R.2
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30
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0000471892
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Protein tubule immobilization on self-assembled monolayers on Au substrates
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Matsui H., Porrata P., Douberly G.E. Protein tubule immobilization on self-assembled monolayers on Au substrates. Nano Letters. 1:2001;461-464.
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(2001)
Nano Letters
, vol.1
, pp. 461-464
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Matsui, H.1
Porrata, P.2
Douberly, G.E.3
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31
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0034315736
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Theoretical studies on the origin of β-sheet twisting
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Shamovsky I., Ross G.M., Riopelle R.J. Theoretical studies on the origin of β-sheet twisting. J Phys Chem B. 104:2000;11296-11307.
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(2000)
J Phys Chem B
, vol.104
, pp. 11296-11307
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Shamovsky, I.1
Ross, G.M.2
Riopelle, R.J.3
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32
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85031359753
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Supramolecular structure of helical ribbons self-assembled from a beta-sheet peptide
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in press. This paper quantitatively analyzes the structure of an intermediate in peptide self-assembly at atomic detail. The simulation approach developed here is applicable to the analysis of a variety of peptide nanofibers, other nanostructures and beyond.
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Hwang W, Marini DM, Kamm RD, Zhang S: Supramolecular structure of helical ribbons self-assembled from a beta-sheet peptide. J Phys Chem B 2002, 106:in press.This paper quantitatively analyzes the structure of an intermediate in peptide self-assembly at atomic detail. The simulation approach developed here is applicable to the analysis of a variety of peptide nanofibers, other nanostructures and beyond.
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(2002)
J Phys Chem B
, pp. 106
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Hwang, W.1
Marini, D.M.2
Kamm, R.D.3
Zhang, S.4
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33
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0000111757
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Fibril stability in solutions of twisted beta-sheet peptides: A new kind of micellization in chiral systems
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Nyrkova I.A., Semenov A.N., Aggeli A., Boden N. Fibril stability in solutions of twisted beta-sheet peptides: a new kind of micellization in chiral systems. Eur Phys J B. 17:2000;481-497.
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(2000)
Eur Phys J B
, vol.17
, pp. 481-497
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Nyrkova, I.A.1
Semenov, A.N.2
Aggeli, A.3
Boden, N.4
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34
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0002069814
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Self-assembly and structure transformations in living polymers forming fibrils
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Nyrkova I.A., Semenov A.N., Aggeli A., Bell M., Boden N., McLeish T.C.B. Self-assembly and structure transformations in living polymers forming fibrils. Eur Phys J B. 17:2000;499-513.
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(2000)
Eur Phys J B
, vol.17
, pp. 499-513
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Nyrkova, I.A.1
Semenov, A.N.2
Aggeli, A.3
Bell, M.4
Boden, N.5
McLeish, T.C.B.6
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35
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0035797725
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Theory of self-assembled tubules and helical ribbons
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Selinger J.V., Spector M.S., Schnur J.M. Theory of self-assembled tubules and helical ribbons. J Phys Chem B. 105:2001;7157-7169.
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(2001)
J Phys Chem B
, vol.105
, pp. 7157-7169
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Selinger, J.V.1
Spector, M.S.2
Schnur, J.M.3
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36
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0035818094
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Molecular dynamics simulations of octyl glucoside micelles: Dynamic properties
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Bogusz S., Venable R.M., Pastor R.W. Molecular dynamics simulations of octyl glucoside micelles: dynamic properties. J Phy Chem B. 105:2001;8312-8321.
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(2001)
J Phy Chem B
, vol.105
, pp. 8312-8321
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Bogusz, S.1
Venable, R.M.2
Pastor, R.W.3
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37
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0035935803
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Fusion pathways of vesicles: A Brownian dynamics simulation
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Noguchi H., Takasu M. Fusion pathways of vesicles: a Brownian dynamics simulation. J Chem Phys. 115:2001;9547-9551.
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(2001)
J Chem Phys
, vol.115
, pp. 9547-9551
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Noguchi, H.1
Takasu, M.2
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38
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0034246730
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Simulation method of colloidal suspension with hydrodynamic interactions: Fluid particle dynamics
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Tanaka H., Araki T. Simulation method of colloidal suspension with hydrodynamic interactions: fluid particle dynamics. Phys Rev Lett. 85:2000;1338-1341.
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(2000)
Phys Rev Lett
, vol.85
, pp. 1338-1341
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Tanaka, H.1
Araki, T.2
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39
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0003440781
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London and New York: Academic Press. This book reviews the fundamental forces involved in macromolecular systems. The last part deals with self-assembly of lipid systems. Many of the basic concepts necessary for understanding self-assembly are well explained.
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Israelachvili J. Intermolecular and surface forces. 2nd ed :1998;Academic Press, London and New York. This book reviews the fundamental forces involved in macromolecular systems. The last part deals with self-assembly of lipid systems. Many of the basic concepts necessary for understanding self-assembly are well explained.
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(1998)
Intermolecular and surface forces 2nd ed
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Israelachvili, J.1
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40
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0033616587
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In situ atomic force microscopy study of Alzheimer's beta-amyloid peptide on different substrates: New insights into mechanism of beta-sheet formation
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Kowalewski T., Holtzman D.M. In situ atomic force microscopy study of Alzheimer's beta-amyloid peptide on different substrates: new insights into mechanism of beta-sheet formation. Proc Natl Acad Sci USA. 96:1999;3688-3693.
-
(1999)
Proc Natl Acad Sci USA
, vol.96
, pp. 3688-3693
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Kowalewski, T.1
Holtzman, D.M.2
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41
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0037130174
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Amyloid pores from pathogenic mutations
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The authors report the intermediate structure in the self-assembly of alpha-synuclein. These ring-shaped structures might act as pores and puncture the cell membrane, causing neuronal death.
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Lashuel H.A., Hartley D., Petre B.M., Walz T., Lansbury P.T. Jr. Amyloid pores from pathogenic mutations. Nature. 418:2002;291. The authors report the intermediate structure in the self-assembly of alpha-synuclein. These ring-shaped structures might act as pores and puncture the cell membrane, causing neuronal death.
-
(2002)
Nature
, vol.418
, pp. 291
-
-
Lashuel, H.A.1
Hartley, D.2
Petre, B.M.3
Walz, T.4
Lansbury P.T., Jr.5
-
42
-
-
0034616839
-
Protofilaments, filaments, ribbons and fibrils from peptidomimetic self-assembly: Implications for amyloid fibril formation and materials science
-
Lashuel H.A., LaBrenz S.R., Woo L., Serpell L.C., Kelly J.W. Protofilaments, filaments, ribbons and fibrils from peptidomimetic self-assembly: implications for amyloid fibril formation and materials science. J Am Chem Soc. 122:2000;5262-5277.
-
(2000)
J Am Chem Soc
, vol.122
, pp. 5262-5277
-
-
Lashuel, H.A.1
LaBrenz, S.R.2
Woo, L.3
Serpell, L.C.4
Kelly, J.W.5
-
43
-
-
0037162463
-
Self-assembling peptide hydrogel fosters chondrocyte extracellular matrix production and cell division: Implications for cartilage tissue repair
-
This is the first report to use a peptide matrix to encapsulate primary chondrocytes to form a 3D piece cartilage tissue similar to isolated cartilage from animals. The peptide matrix is now used to culture cells in 3D and for tissue repair in regenerative medicine.
-
Kisiday J., Jin M., Kurz B., Hung H., Semino C., Zhang S., Grodzinsky A.J. 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. This is the first report to use a peptide matrix to encapsulate primary chondrocytes to form a 3D piece cartilage tissue similar to isolated cartilage from animals. The peptide matrix is now used to culture cells in 3D and for tissue repair in regenerative medicine.
-
(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
-
44
-
-
0033937682
-
Conformational behavior of ionic self-complementary peptides
-
This paper reports the conformational plasticity of peptides with helical dipoles. They can undergo drastic structural changes between α-helices and β-sheets. Such peptides behave like a 'molecular switch'.
-
Altman M., Lee P., Rich A., Zhang S. Conformational behavior of ionic self-complementary peptides. Protein Sci. 9:2000;1095-1105. This paper reports the conformational plasticity of peptides with helical dipoles. They can undergo drastic structural changes between α-helices and β-sheets. Such peptides behave like a 'molecular switch'.
-
(2000)
Protein Sci
, vol.9
, pp. 1095-1105
-
-
Altman, M.1
Lee, P.2
Rich, A.3
Zhang, S.4
-
45
-
-
3042537628
-
Biological surface engineering: A simple system for cell pattern formation
-
This paper describes a simple method to molecularly engineer functional peptides and to design patterns on surfaces for a number of applications, much like a carpet with designed patterns. Cells and molecules can be precisely organized on surfaces.
-
Zhang S., Yan L., Altman M., Lässle M., Nugent H., Frankel F., Lauffenburger D.A., Whitesides G.M., Rich A. Biological surface engineering: a simple system for cell pattern formation. Biomaterials. 20:1999;1213-1220. This paper describes a simple method to molecularly engineer functional peptides and to design patterns on surfaces for a number of applications, much like a carpet with designed patterns. Cells and molecules can be precisely organized on surfaces.
-
(1999)
Biomaterials
, vol.20
, pp. 1213-1220
-
-
Zhang, S.1
Yan, L.2
Altman, M.3
Lässle, M.4
Nugent, H.5
Frankel, F.6
Lauffenburger, D.A.7
Whitesides, G.M.8
Rich, A.9
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