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Peptide Nanotubes (peptide + nanotube)

Distribution by Scientific Domains

Chemistry	62%

Selected Abstracts

Manipulation of self-assembly amyloid peptide nanotubes by dielectrophoresis

ELECTROPHORESIS, Issue 24 2008
Jaime Castillo
Abstract Self-assembled amyloid peptide nanotubes (SAPNT) were manipulated and immobilized using dielectrophoresis. Micro-patterned electrodes of Au were fabricated by photolithography and lifted off on a silicon dioxide layer. SAPNT were manipulated by adjusting the amplitude and frequency of the applied voltage. The immobilized SAPNT were evaluated by SEM and atomic force microscopy. The conductivity of the immobilized SAPNT was studied by I,V characterization, for both single SAPNT and bundles. This work illustrates a way to manipulate and integrate biological nanostructures into novel bio-nanoassemblies with concrete applications, such as field-effect transistors, microprobes, microarrays, and biosensing devices. [source]

Peptide Nanotubes: Simple Separation Using Size-Exclusion Columns and Use as Templates for Fabricating One-Dimensional Single Chains of Au Nanoparticles,

ADVANCED MATERIALS, Issue 14 2005
X. Gao
Straight single chains of Au nanoparticles have been synthesized using 10,nm diameter peptide nanotubes as templates (see Figure). The 6,nm Au nanoparticles grow in the gaps between the synthetic peptide coating the nanotubes which regulates the size, dispersity, interparticle distance, and crystallinity of the nanoparticles. The use of longer nanotubes results in longer chains. [source]

Crossbar assembly of antibody-functionalized peptide nanotubes via biomimetic molecular recognition,

JOURNAL OF PEPTIDE SCIENCE, Issue 2 2008
Linglu Yang
Abstract Previously, a large scale assembly of nanowires in a parallel array configuration has been demonstrated, and one type of nanowire could interconnect two electrodes in the high-wire density. However, to assemble nanowires into practical logic-gate configurations in integrated circuits, we need more than the parallel assembly of nanowires. For example, when the assembling nanowires are monopolar semiconductors, logic gates such as AND, OR and NOR are to be assembled necessarily from two types of semiconducting nanowires, n -type and p -type, and some of these nanowires must cross perpendicularly to form a crossbar geometry for the logical operation. In this paper, the crossbar assembly of antibody-functionalized peptide nanotubes was demonstrated by a new biomimetic bottom-up technique. Molecular recognition between antigens and antibodies enabled two types of the antibody-functionalized bionanotubes to place them onto targeted locations on substrates, where their complementary antigens were patterned. When two rectangular pads of antigens, human IgG and mouse IgG, were patterned perpendicularly on an Au substrate by nanolithography and then the antihuman IgG nanotubes and the antimouse IgG nanotubes were incubated on this substrate in solution, these bionanotubes were attached onto corresponding locations to form the crossbar configuration. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd. [source]

Backbone-modified amylin derivatives: implications for amyloid inhibitor design and as template for self-assembling bionanomaterials,

JOURNAL OF PEPTIDE SCIENCE, Issue 11 2007
Ronald C. Elgersma
Abstract This report reviews our approach to the design, synthesis and structural/morphological analysis of backbone-modified amylin(20,29) derivatives. Depending on the position in the peptide backbone and the type of amide bond isostere/modification, the amylin(20,29) peptides behave either as inhibitors of amyloid fibril formation, which are able to retard amyloid formation of native amylin(20,29), or as templates for the formation of self-assembled supramolecular structures. Molecular fine-tuning of the hydrogen-bond accepting/donating properties allows the control over the morphology of the supramolecular aggregation motifs such as helical ribbons and tapes, ribbons progressing to closed peptide nanotubes, (twisted) lamellar sheets or amyloid fibrils. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd. [source]

Self-Assembly of Amylin(20,29) Amide-Bond Derivatives into Helical Ribbons and Peptide Nanotubes rather than Fibrils

CHEMISTRY - A EUROPEAN JOURNAL, Issue 14 2006
Ronald C. Elgersma
Abstract Uncontrolled aggregation of proteins or polypeptides can be detrimental for normal cellular processes in healthy organisms. Proteins or polypeptides that form these amyloid deposits differ in their primary sequence but share a common structural motif: the (anti)parallel , sheet. A well-accepted approach for interfering with ,-sheet formation is the design of soluble ,-sheet peptides to disrupt the hydrogen-bonding network; this ultimately leads to the disassembly of the aggregates or fibrils. Here, we describe the synthesis, spectroscopic analysis, and aggregation behavior, imaged by electron microscopy, of several backbone-modified amylin(20,29) derivatives. It was found that these amylin derivatives were not able to form fibrils and to some extent were able to inhibit fibril growth of native amylin(20,29). However, two of the amylin peptides were able to form large supramolecular assemblies, like helical ribbons and peptide nanotubes, in which ,-sheet formation was clearly absent. This was quite unexpected since these peptides have been designed as soluble ,-sheet breakers for disrupting the characteristic hydrogen-bonding network of (anti)parallel , sheets. The increased hydrophobicity and the presence of essential amino acid side chains in the newly designed amylin(20,29) derivatives were found to be the driving force for self-assembly into helical ribbons and peptide nanotubes. This example of controlled and desired peptide aggregation may be a strong impetus for research on bionanomaterials in which special shapes and assemblies are the focus of interest. [source]

Modulating Charge Transfer through Cyclic D,L -,-Peptide Self-Assembly

CHEMISTRY - A EUROPEAN JOURNAL, Issue 4 2005
W. Seth Horne
Abstract We describe a concise, solid support-based synthetic method for the preparation of cyclic d,l -,-peptides bearing 1,4,5,8-naphthalenetetracarboxylic acid diimide (NDI) side chains. Studies of the structural and photoluminescence properties of these molecules in solution show that the hydrogen bond-directed self-assembly of the cyclic d,l -,-peptide backbone promotes intermolecular NDI excimer formation. The efficiency of NDI charge transfer in the resulting supramolecular assemblies is shown to depend on the length of the linker between the NDI and the peptide backbone, the distal NDI substituent, and the number of NDIs incorporated in a given structure. The design rationale and synthetic strategies described here should provide a basic blueprint for a series of self-assembling cyclic d,l -,-peptide nanotubes with interesting optical and electronic properties. [source]