Peptide Nanotubes and Beyond

Hartgerink, Jeffrey D.; Clark, Thomas D.; Ghadiri, Mojtaba

doi:10.1002/(sici)1521-3765(19980807)4:8<1367::aid-chem1367>3.0.co;2-b

Cited by 245 publications

(144 citation statements)

References 42 publications

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“…The selfassembly is largely governed by the simultaneous formation of hydrogen bonds between complementary fragments, resulting in either β-sheet-like structures or nanotubes [22][23][24][25]. In addition to hydrogen bonding these supramolecular structures require additional van der Waals (hydrophobic) and/or ionic interactions between side chains to provide the required stability.…”

Section: Self-assembled Molecules Instead Of True Polymersmentioning

confidence: 99%

Multimeric glycotherapeutics: New paradigm

et al. 2004

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The general principle of anti-adhesion therapy is the inhibition of microorganism adhesion to the host cell with the help of a soluble receptor analog. Despite an evident attractiveness of the concept and its long existence, the therapeutics of the 'post-antibiotic era' have not yet appeared. This can be explained by the contradictoriness of requirements for anti-adhesion drugs: to be efficient a drug must be multivalent, i.e. large molecule, but to obtain FDA approval it should be a small molecule. A way to overcome this contradiction is self-assembly of glycopeptides. The carbohydrate part of glycopeptide is responsible for binding with the lectin of microorganisms, whereas a simple peptide part is responsible for an association to the so-called tectomers. Depending on the structure, tectomers are formed either spontaneously or upon promotion of a microorganism. In particular, sialopeptide, which is capable of converting to a tectomer only in the presence of the influenza virus, has been obtained. Thus, the new strategy of anti-adhesion therapy can be formulated as follows: (1) identification of oligosaccharide-receptor for a particular virus (bacteria); (2) optimization of the peptide part; (3) conventional trials. The expected advantages of this strategy are the following: (i) no polymer; (ii) a virion completely covered with a tectomer, i.e. blocking is both complete and irreversible; (iii) rapid and rational lead identification and optimization; (iv) minimum side effects; (v) potential for microorganism resistance to natural receptor is lower than in the case of mimetics.

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Section: Self-assembled Molecules Instead Of True Polymersmentioning

confidence: 99%

Multimeric glycotherapeutics: New paradigm

et al. 2004

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“…2 Moreover, the discovery that control can be afforded via regulation of stable quaternary structures has accelerated the development of nanoscale devices with broad application in science and technology. [3][4][5] Seminal work on natural and designed coiled coil proteins has revealed critical insights into the fundamental parameters that govern α-peptide assembly and conformation. [6][7][8] A next goal is to elucidate the molecular rules governing the aqueous assembly of non-proteinaceous quaternary structure, a critical step in developing new and unique materials with potential as nanomaterials, drugs, and enzymatic platforms.…”

Section: Introductionmentioning

confidence: 99%

Biophysical and Structural Characterization of a Robust Octameric β-Peptide Bundle

et al. 2007

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Proteins composed of α-amino acids are essential components of the machinery required for life. Stanley Miller's renowned electric discharge experiment provided evidence that an environment of methane, ammonia, water, and hydrogen was sufficient to produce α-amino acids. This reaction also generated other potential protein building blocks such as the β-amino acid β-glycine (also known as β-alanine); however, the potential of these species to form complex ordered structures that support functional roles has not been widely investigated. In this report we apply a variety of biophysical techniques, including circular dichroism, differential scanning calorimetry, analytical ultracentrifugation, NMR and X-ray crystallography, to characterize the oligomerization of two 12-mer β 3 -peptides, Acid-1Y and Acid-1Y*. Like the previously reported β 3 -peptide Zwit-1F, Acid-1Y and Acid-1Y* fold spontaneously into discrete, octameric quaternary structures that we refer to as β-peptide bundles. Surprisingly, the Acid-1Y octamer is more stable than the analogous Zwit-1F octamer, in terms of both its thermodynamics and kinetics of unfolding. The structure of Acid-1Y, reported here to 2.3 Å resolution, provides intriguing hypotheses for the increase in stability. To summarize, in this work we provide additional evidence that nonnatural β-peptide oligomers can assemble into cooperatively folded structures with potential application in enzyme design, and as medical tools and nanomaterials. Furthermore, these studies suggest that nature's selection of α-amino acid precursors was not based solely on their ability to assemble into stable oligomeric structures.

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“…Important principles of self-assembly are chemical complementarity and structural compatibility through weak and noncovalent interactions. Different construction units, such as well ordered nanofiber scaffolds [233,234], peptide nanotubes [235][236][237], segmented surface assembling peptides as a 'molecular carpet' [238][239][240] and dipolar molecules with changeable conformation as a 'molecular switch' [241][242][243], can be realized by specially designed peptide units and sequences. However, the realization of peptide scaffolds by molecular self-assembly is extremely extensive and it depends on elaborate techniques.…”

Section: Self-assembly Systemsmentioning

confidence: 99%

Design and preparation of polymeric scaffolds for tissue engineering

Weigel

Schinkel

Lendlein

2006

Expert Review of Medical Devices

208

154

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Polymeric scaffolds for tissue engineering can be prepared with a multitude of different techniques. Many diverse approaches have recently been under development. The adaptation of conventional preparation methods, such as electrospinning, induced phase separation of polymer solutions or porogen leaching, which were developed originally for other research areas, are described. In addition, the utilization of novel fabrication techniques, such as rapid prototyping or solid free-form procedures, with their many different methods to generate or to embody scaffold structures or the usage of selfassembly systems that mimic the properties of the extracellular matrix are also described. These methods are reviewed and evaluated with specific regard to their utility in the area of tissue engineering.Expert Rev. Med. Devices 3(6), 835-851 (2006) The technology of tissue engineering aims to generate new or substitute damaged or malfunctioning tissue or organs and could well become an alternative method to whole organ transplantation [1][2][3][4][5][6]. In the last decade particularly, enormous advances have been made in the area of tissue regeneration for therapeutical purposes. Tissue engineering is an interdisciplinary research area in which principles of material science/engineering and cell biology/life science are combined. The methods of tissue engineering have been applied to different types of tissue, including skin [7][8][9][10][11], bone [12][13][14][15][16], liver [17][18][19][20][21], intestine [22][23][24][25][26][27], esophagus [28][29][30][31][32], valve leaflets [33][34][35][36], muscle [37][38][39] and tongue [40][41][42], the vascular system [43][44][45][46][47], for craniofacial defects [48][49][50], tendons and ligaments [51][52][53][54][55], cartilage [56][57][58][59][60] and nerve tissue [61][62][63][64][65]. Since the early commercialization of tissue-engineered applications, for example, the work of Bell and colleagues [66], research with stem cells [3,[67][68][69] and the use of growth factors [70][71][72][73] that support cell differentiation and proliferation, have provided new opportunities in the field of tissue engineering. At present, tissue engineering methods generally require the use of a porous scaffold that serves as a matrix for initial cell attachment and subsequently for tissue formation in vitro and in vivo. Up to now scaffolds made from biomaterials have temporarily substituted the extracellular matrix (ECM). Such biomaterials can be of natural origin, such as organic collagen [74][75][76], fibrin glue [77][78][79], hyaluronic acid [80][81][82] or the inorganic-like coralline [83,84]. Synthetic polymeric materials have also been investigated, including, for example, aliphatic, copolyesters [85][86][87], polyhydroxyalkanoates [88][89][90] and polyethylene glycol [91,92], or inorganic materials, such as hydroxyapatite [48,93,94], tricalciumphosphate [95,96], glass ceramics and glass [97][98][99].The intrinsic material properties, such as the mechanical [100] or thermal [101,102] be...

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Peptide Nanotubes and Beyond

Cited by 245 publications

References 42 publications

Multimeric glycotherapeutics: New paradigm

Multimeric glycotherapeutics: New paradigm

Biophysical and Structural Characterization of a Robust Octameric β-Peptide Bundle

Design and preparation of polymeric scaffolds for tissue engineering

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