Sat, 26 Jul 2008 07:27:18 BST CiteULike: kirinli's library [22 articles] http://www.citeulike.org/user/kirinli CiteULike.org en-gb Copyright © 2004-2008 citeulike.org http://www.citeulike.org/user/kirinli/article/2475135 <i></i> http://aps.unmc.edu/AP/main.php 2008-03-05T20:27:25-00:00 bioactive http://www.citeulike.org/user/kirinli/article/2475129 <i></i> http://www.aps.unmc.edu/ap/main.php 2008-03-05T20:25:11-00:00 no-tag http://www.citeulike.org/user/kirinli/article/2475116 <i></i> http://www.patentec.com/data/class/530.html#2 2008-03-05T20:22:18-00:00 bioactive http://www.citeulike.org/user/kirinli/article/2474926 <i>Trends in Microbiology, Vol. 8, No. 9. (1 September 2000), pp. 402-410.</i><br /><br />Cationic antimicrobial peptides are found in all living species. A single animal can contain >24 different antimicrobial peptides, which fall into four structural classes. These peptides are produced in large quantities at sites of infection and/or inflammation and can have broad-spectrum antibacterial, antifungal, antiviral, antiprotozoan and antisepsis properties. In addition, they interact directly with host cells to modulate the inflammatory process and innate defences. The role of cationic antimicrobial peptides in innate host defences Robert Hancock Gill Diamond doi:10.1016/S0966-842X(00)01823-0 Trends in Microbiology, Vol. 8, No. 9. (1 September 2000), pp. 402-410. 2008-03-05T19:41:54-00:00 2000 Trends in Microbiology 8 9 402 410 bioactive http://www.citeulike.org/user/kirinli/article/2474748 <i>Nat Biotech, Vol. 18, No. 4. (April 2000), pp. 415-419.</i> Enzymatic incorporation of bioactive peptides into fibrin matrices enhances neurite extension Jason Schense Jocelyne Bloch Patrick Aebischer Jeffrey Hubbell doi:10.1038/74473 Nat Biotech, Vol. 18, No. 4. (April 2000), pp. 415-419. 2008-03-05T19:11:10-00:00 2000 Nat Biotech 18 4 415 419 bioactive peptide http://www.citeulike.org/user/kirinli/article/968993 <i>PNAS, Vol. 97, No. 12. (6 June 2000), pp. 6728-6733.</i><br /><br />10.1073/pnas.97.12.6728 Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds Todd Holmes Sonsoles de Lacalle Xing Su Guosong Liu Alexander Rich Shuguang Zhang doi:10.1073/pnas.97.12.6728 PNAS, Vol. 97, No. 12. (6 June 2000), pp. 6728-6733. 2006-11-30T17:38:33-00:00 2000 PNAS 97 12 6728 6733 positively references http://www.citeulike.org/user/kirinli/article/2445315 <i>Biomaterials, Vol. 16, No. 18. (December 1995), pp. 1385-1393.</i><br /><br />A new class of ionic self-complementary oligopeptides is described, two members of which have been designated RAD16 and EAK16. These oligopeptides consist of regular repeats of alternating ionic hydrophilic and hydrophobic amino acids and associate to form stable [beta]-sheet structures in water. The addition of buffers containing millimolar amounts of monovalent salts or the transfer of a peptide solution into physiological solutions results in the spontaneous assembly of the oligopeptides into a stable, macroscopic membranous matrix. The matrix is composed of ordered filaments which form porous enclosures. A variety of mammalian cell types are able to attach to both RAD16 and EAK16 membranous matrices. These matrices provide a novel experimental system for analysing mechanisms of in vitro cell attachment and may have applications in in vivo studies of tissue regeneration, tissue transplantation and wound healing. Self-complementary oligopeptide matrices support mammalian cell attachment Shuguang Zhang Todd Holmes Michael Dipersio Richard Hynes Xing Su Alexander Rich doi:10.1016/0142-9612(95)96874-Y Biomaterials, Vol. 16, No. 18. (December 1995), pp. 1385-1393. 2008-02-28T21:54:44-00:00 1995 Biomaterials 16 18 1385 1393 positively references http://www.citeulike.org/user/kirinli/article/2445313 <i>Proceedings of the National Academy of Sciences, Vol. 98, No. 3. (30 January 2001), pp. 1200-1205.</i><br /><br />10.1073/pnas.031577698 Polymer-based gene delivery with low cytotoxicity by a unique balance of side-chain termini David Putnam Christine Gentry Daniel Pack Robert Langer doi:10.1073/pnas.031577698 Proceedings of the National Academy of Sciences, Vol. 98, No. 3. (30 January 2001), pp. 1200-1205. 2008-02-28T21:53:21-00:00 2001 Proceedings of the National Academy of Sciences 98 3 1200 1205 positively references http://www.citeulike.org/user/kirinli/article/2445308 <i>Biomaterials, Vol. 23, No. 1. (January 2002), pp. 219-227.</i><br /><br />In order to elucidate design principles for biocompatible materials that can be created by in situ transformation from self-assembling oligopeptides, we investigate a class of oligopeptides that can self-assemble in salt solutions to form three-dimensional matrices. This class of peptides possesses a repeated sequence of amino acid residues with the type: hydrophobic/negatively-charged/hydrophobic/positively-charged. We systematically vary three chief aspects of this sequence type: (1) the hydrophobic side chains; (2) the charged side-chains; and (3) the number of repeats. Employing a rheometric assay to judge matrix formation, we determine the critical concentration of NaCl salt solution required to drive transformation from viscous state to gel state. We find that increasing side-chain hydrophobicity decreases the critical salt concentration in accord with our previous validation of DLVO theory for explaining this self-assembly phenomenon Caplan et al. (Biomacromolecules 1 (2000) 627). Further, we find that increasing the number of repeats yields a biphasic dependence--first decreasing, then increasing, the critical salt concentration. We believe that this result is likely due to an unequal competition between a greater hydrophobic (favorable) effect and a greater entropic (unfavorable) effect as the peptide length is increased. Finally, we find that we can use this understanding to rationally alter the charged side-chains to create a self-assembling oligopeptide sequence that at pH 7 remains viscous in the absence of salt but gels in the presence of physiological salt concentrations, a highly useful property for technological applications. Control of self-assembling oligopeptide matrix formation through systematic variation of amino acid sequence Michael Caplan Elissa Schwartzfarb Shuguang Zhang Roger Kamm Douglas Lauffenburger doi:10.1016/S0142-9612(01)00099-0 Biomaterials, Vol. 23, No. 1. (January 2002), pp. 219-227. 2008-02-28T21:51:04-00:00 2002 Biomaterials 23 1 219 227 positively references http://www.citeulike.org/user/kirinli/article/2445305 <i>Biomacromolecules, Vol. 3, No. 4. (8 July 2002), pp. 710-723.</i><br /><br />Abstract: To address the need for bioactive materials toward clinical applications in wound healing and tissue regeneration, an artificial protein was created by recombinant DNA methods and modified by grafting of poly(ethylene glycol) diacrylate. Subsequent photopolymerization of the acrylate-containing precursors yielded protein-graft-poly(ethylene glycol) hydrogels. The artificial protein contained repeating amino acid sequences based on fibrinogen and anti-thrombin III, comprising an RGD integrin-binding motif, two plasmin degradation sites, and a heparin-binding site. Two-dimensional adhesion studies showed that the artificial protein had specific integrin-binding capability based on the RGD motif contained in its fibrinogen-based sequence. Furthermore, heparin bound strongly to the protein's anti-thrombin III-based region. Protein-graft-poly(ethylene glycol) hydrogels were plasmin degradable, had Young's moduli up to 3.5 kPa, and supported three-dimensional outgrowth of human fibroblasts. Cell attachment in three dimensions resulted from specific cell-surface integrin binding to the material's RGD sequence. Hydrogel penetration by cells involved serine-protease mediated matrix degradation in temporal and spatial synchrony with cellular outgrowth. Protein-graft-poly(ethylene glycol) hydrogels represent a new and versatile class of biomimetic hybrid materials that hold clinical promise in serving as implants to promote wound healing and tissue regeneration. Biologically Engineered Protein-graft-Poly(ethylene glycol) Hydrogels: A Cell Adhesive and Plasmin-Degradable Biosynthetic Material for Tissue Repair S Halstenberg A Panitch S Rizzi H Hall JA Hubbell doi:10.1021/bm015629o Biomacromolecules, Vol. 3, No. 4. (8 July 2002), pp. 710-723. 2008-02-28T21:49:09-00:00 2002 Biomacromolecules 3 4 710 723 positively references http://www.citeulike.org/user/kirinli/article/2445303 <i>Mol Ther, Vol. 1, No. 1. (January 2000), pp. 12-15.</i> Tissue Engineering Robert Langer doi:10.1006/mthe.1999.0003 Mol Ther, Vol. 1, No. 1. (January 2000), pp. 12-15. 2008-02-28T21:47:57-00:00 2000 Mol Ther 1 1 12 15 no-tag http://www.citeulike.org/user/kirinli/article/2445301 <i>Science, Vol. 296, No. 5573. (31 May 2002), pp. 1673-1676.</i><br /><br />10.1126/science.1066102 Biodegradable, Elastic Shape-Memory Polymers for Potential Biomedical Applications Andreas Lendlein Robert Langer doi:10.1126/science.1066102 Science, Vol. 296, No. 5573. (31 May 2002), pp. 1673-1676. 2008-02-28T21:46:41-00:00 2002 Science 296 5573 1673 1676 positively references http://www.citeulike.org/user/kirinli/article/2445298 <i>Biopolymers, Vol. 47, No. 2. (1998), pp. 143-151.</i> Proteinlike molecular architecture: biomaterial applications for inducing cellular receptor binding and signal transduction Gregg Fields Biopolymers, Vol. 47, No. 2. (1998), pp. 143-151. 2008-02-28T21:44:18-00:00 1998 Biopolymers 47 2 143 151 positively references http://www.citeulike.org/user/kirinli/article/2445293 <i>Nature, Vol. 417, No. 6887. (23 May 2002), pp. 424-428.</i> Rapidly recovering hydrogel scaffolds from self-assembling diblock copolypeptide amphiphiles Andrew Nowak Victor Breedveld Lisa Pakstis Bulent Ozbas David Pine Darrin Pochan Timothy Deming Nature, Vol. 417, No. 6887. (23 May 2002), pp. 424-428. 2008-02-28T21:40:29-00:00 2002 Nature 417 6887 424 428 positively references http://www.citeulike.org/user/kirinli/article/2391372 <i>Science, Vol. 281, No. 5375. (17 July 1998), pp. 389-392.</i><br /><br />10.1126/science.281.5375.389 Reversible Hydrogels from Self-Assembling Artificial Proteins Wendy Petka James Harden Kevin Mcgrath Denis Wirtz David Tirrell doi:10.1126/science.281.5375.389 Science, Vol. 281, No. 5375. (17 July 1998), pp. 389-392. 2008-02-17T20:17:14-00:00 1998 Science 281 5375 389 392 positively references http://www.citeulike.org/user/kirinli/article/2445278 <i>Science, Vol. 263, No. 5154. (25 March 1994), pp. 1715-1720.</i><br /><br />Significant opportunities and challenges exist in the creation and characterization of biomaterials. Materials have been designed for contact with blood, as replacements for soft and hard tissues, as adhesives, and as dental materials. Current methods of synthesis and characterization of these materials are outlined. Approaches for controlling the interface between tissue and biomaterials and ways in which the engineered materials may contribute to medicine are considered. 10.1126/science.8134835 New challenges in biomaterials NA Peppas R Langer doi:10.1126/science.8134835 Science, Vol. 263, No. 5154. (25 March 1994), pp. 1715-1720. 2008-02-28T21:31:24-00:00 1994 Science 263 5154 1715 1720 positively references http://www.citeulike.org/user/kirinli/article/2445272 <i>Science, Vol. 300, No. 5619. (25 April 2003), pp. 625-627.</i><br /><br />Tubular nanostructures are suggested to have a wide range of applications in nanotechnology. We report our observation of the self-assembly of a very short peptide, the Alzheimer's beta-amyloid diphenylalanine structural motif, into discrete and stiff nanotubes. Reduction of ionic silver within the nanotubes, followed by enzymatic degradation of the peptide backbone, resulted in the production of discrete nanowires with a long persistence length. The same dipeptide building block, made of D-phenylalanine, resulted in the production of enzymatically stable nanotubes. 10.1126/science.1082387 Casting Metal Nanowires Within Discrete Self-Assembled Peptide Nanotubes Meital Reches Ehud Gazit doi:10.1126/science.1082387 Science, Vol. 300, No. 5619. (25 April 2003), pp. 625-627. 2008-02-28T21:26:21-00:00 2003 Science 300 5619 625 627 peptide self-assembly http://www.citeulike.org/user/kirinli/article/440524 <i>Science, Vol. 295, No. 5564. (29 March 2002), pp. 2418-2421.</i><br /><br />Self-assembly is the autonomous organization of components into patterns or structures without human intervention. Self-assembling processes are common throughout nature and technology. They involve components from the molecular (crystals) to the planetary (weather systems) scale and many different kinds of interactions. The concept of self-assembly is used increasingly in many disciplines, with a different flavor and emphasis in each. Self-assembly at all scales. GM Whitesides B Grzybowski doi:10.1126/science.1070821 Science, Vol. 295, No. 5564. (29 March 2002), pp. 2418-2421. 2005-12-17T14:15:26-00:00 2002 Science 1095-9203 295 5564 2418 2421 peptide self-assembly http://www.citeulike.org/user/kirinli/article/2445233 <i>Science, Vol. 260, No. 5110. (14 May 1993), pp. 920-926.</i><br /><br />The loss or failure of an organ or tissue is one of the most frequent, devastating, and costly problems in human health care. A new field, tissue engineering, applies the principles of biology and engineering to the development of functional substitutes for damaged tissue. This article discusses the foundations and challenges of this interdisciplinary field and its attempts to provide solutions to tissue creation and repair. 10.1126/science.8493529 Tissue engineering R Langer JP Vacanti doi:10.1126/science.8493529 Science, Vol. 260, No. 5110. (14 May 1993), pp. 920-926. 2008-02-28T21:02:44-00:00 1993 Science 260 5110 920 926 biomedical engineering http://www.citeulike.org/user/kirinli/article/969008 <i>PNAS, Vol. 99, No. 8. (16 April 2002), pp. 5355-5360.</i><br /><br />Several surfactant-like peptides undergo self-assembly to form nanotubes and nanovesicles having an average diameter of 30-50 nm with a helical twist. The peptide monomer contains 7-8 residues and has a hydrophilic head composed of aspartic acid and a tail of hydrophobic amino acids such as alanine, valine, or leucine. The length of each peptide is [approx]2 nm, similar to that of biological phospholipids. Dynamic light-scattering studies showed structures with very discrete sizes. The distribution becomes broader over time, indicating a very dynamic process of assembly and disassembly. Visualization with transmission electron microscopy of quick-freeze/deep-etch sample preparation revealed a network of open-ended nanotubes and some vesicles, with the latter being able to "fuse" and "bud" out of the former. The structures showed some tail sequence preference. Many three-way junctions that may act as links between the nanotubes have been observed also. Studies of peptide surfactant molecules have significant implications in the design of nonlipid biological surfactants and the understanding of the complexity and dynamics of the self-assembly processes. 10.1073/pnas.072089599 Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles Sylvain Vauthey Steve Santoso Haiyan Gong Nicki Watson Shuguang Zhang doi:10.1073/pnas.072089599 PNAS, Vol. 99, No. 8. (16 April 2002), pp. 5355-5360. 2006-11-30T17:49:44-00:00 2002 PNAS 99 8 5355 5360 peptide self-assembly http://www.citeulike.org/user/kirinli/article/2444449 <i>Langmuir, Vol. 19, No. 10. (2003), pp. 4332-4337.</i> Positively Charged Surfactant-like Peptides Self-assemble into Nanostructures Geoffrey Langmuir, Vol. 19, No. 10. (2003), pp. 4332-4337. 2008-02-28T17:59:37-00:00 2003 Langmuir 19 10 4332 4337 peptide http://www.citeulike.org/user/kirinli/article/2444414 <i>Current Opinion in Structural Biology, Vol. 15, No. 4. (August 2005), pp. 453-463.</i><br /><br />Important challenges in biomaterials design include predicting the formation of large-scale self-assembled structures based on local atomic-level interactions and then endowing such structures with the ability to respond sensitively to environmental cues. This responsiveness is referred to as smartness. With the advent of key technological advances in imaging, peptides have recently begun to be exploited for their potential use as biomaterials, such as filaments and fibrils, hydrogels, surfactants and peptide hybrids. Peptides offer attractive features, principally because of our detailed understanding of their ability to fold into specific structures, and the rich chemistry with which their structure and function can be manipulated for environmental response. Peptides as novel smart materials Robert Fairman Karin Akerfeldt doi:10.1016/j.sbi.2005.07.005 Current Opinion in Structural Biology, Vol. 15, No. 4. (August 2005), pp. 453-463. 2008-02-28T17:43:34-00:00 2005 Current Opinion in Structural Biology 15 4 453 463 peptide self-assembly