Nucleobase-Directed Amyloid Nanotube Assembly

Liu, Peng; Ni, Rong; Mehta, Anil; Childers, W. Seth; Lakdawala, Ami S.; Pingali, Sai Venkatesh; Thiyagarajan, P.; Lynn, David G.

doi:10.1021/ja807425h

Cited by 49 publications

(41 citation statements)

References 40 publications

(88 reference statements)

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“…Further, all of the distances measured indicate clearly that the peptide molecules are arranged in parallel, in-register β-sheets with interstrand 13 C- 13 C distances ranging from 4.41 Å to 4.59 Å with an average error of ±0.11 Å (Figure 7). The double quantum relaxation parameter is found to be in the range of 6-10 ms, which is consistent with the measurements of Liu, et al (9.4 ms) in a similar system (amyloid nanotubes)57. However, we note several important differences between our approach and that of Liu, et al and others in the field.…”

Section: Resultssupporting

confidence: 91%

Accurate Determination of Interstrand Distances and Alignment in Amyloid Fibrils by Magic Angle Spinning NMR

et al. 2010

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Amyloid fibrils are structurally ordered aggregates of proteins whose formation is associated with many neurodegenerative and other diseases. For that reason, their high resolution structures are of considerable interest and have been studied using a wide range of techniques, notably electron microscopy, x-ray diffraction, and magic angle spinning (MAS) NMR. Because of the excellent resolution in the spectra, MAS NMR is uniquely capable of delivering site-specific, atomic resolution information about all levels of amyloid structure: (1) the monomer, which packs into several (2) protofilaments that in turn associate to form a (3) fibril. Building upon our high resolution structure of the monomer of an amyloid-forming peptide from transthyretin (TTR 105-115 ), we introduce single 1-13 C labeled amino acids at seven different sites in the peptide and measure intermolecular carbonyl-carbonyl distances with an accuracy of ~0.11 A. Our results conclusively establish a parallel, in register, topology for the packing of this peptide into a β-sheet and provide constraints essential for the determination of an atomic resolution structure of the fibril. Furthermore, the approach we employ, based on a combination of a double-quantum filtered variant of the DRAWS recoupling sequence and multispin numerical simulations in SPINEVOLUTION, is general and should be applicable to a wide range of systems.

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Section: Resultssupporting

confidence: 91%

Accurate Determination of Interstrand Distances and Alignment in Amyloid Fibrils by Magic Angle Spinning NMR

et al. 2010

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“…By lowering the activation energy barrier, interfaces per se are known to promote amyloidogenesis, too (Stefani 2008). Moreover, oligomers are readily synthesized on certain mineral surfaces (Ferris 1996) and amyloid can spontaneously form fibrillar networks that acts as scaffolds for the amyloid assemblies themselves (Hamley 2007), as well as for other molecules, such as ribonucleotides (Liu et al 2008). Amyloid may also enhance the polymerization of ribonucleotides, and nucleic acids may enhance amyloid formation (Braun et al 2012).…”

Section: Prebiotic Amyloidogenesis: Surface-bound or In Solution?mentioning

confidence: 99%

Origin of life. Primordial genetics: Information transfer in a pre-RNA world based on self-replicating beta-sheet amyloid conformers

Maury

2015

Journal of Theoretical Biology

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The question of the origin of life on Earth can largely be reduced to the question of what was the first molecular replicator system that was able to replicate and evolve under the presumably very harsh conditions on the early Earth. It is unlikely that a functional RNA could have existed under such conditions and it is generally assumed that some other kind of information system preceded the RNA world. Here, I present an informational molecular system that is stable, self-replicative, environmentally responsive, and evolvable under conditions characterized by high temperatures, ultraviolet and cosmic radiation. This postulated pregenetic system is based on the amyloid fold, a functionally unique polypeptide fold characterized by a cross beta-sheet structure in which the beta strands are arranged perpendicular to the fiber axis. Beside an extraordinary structural robustness, the amyloid fold possesses a unique ability to transmit information by a three-dimensional templating mechanism. In amyloidogenesis short peptide monomers are added one by one to the growing end of the fiber. From the same monomeric subunits several structural variants of amyloid may be formed. Then, in a self-replicative mode, a specific amyloid conformer can act as a template and confer its spatially encoded information to daughter molecular entities in a repetitive way. In this process, the specific conformational information, the spatially changed organization, is transmitted; the coding element is the steric zipper structure, and recognition occurs by amino acid side chain complementarity. The amyloid information system fulfills several basic requirements of a primordial evolvable replicator system: (i) it is stable under the presumed primitive Earth conditions, (ii) the monomeric building blocks of the informational polymer can be formed from available prebiotic compounds, (iii) the system is self-assembling and self-replicative and (iv) it is adaptive to changes in the environment and evolvable.

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“…[1][2][3][4][5][6] In particular, a great expectation was placed on the biological and biomedical applications of tubular nanomaterials. [7][8][9] As one of the most important materials of the carbon family, C 60 has many unique properties, such as, fluorescence and biological activities, [10][11][12] which makes it a potential functional material. Recent research focuses on exploring practical applications from nanocrystals with C 60 molecules as building blocks.…”

Section: Introductionmentioning

confidence: 99%

High pressure and high temperature induced polymerization of C60 nanotubes

Liu

Yao

et al. 2011

CrystEngComm

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. et al. (2011) High pressure and high temperature induced polymerization of C 60 nanotubes.CrysteEngComm, 13 (10) Abstract C 60 nanotubes with outer diameters ranging from 400 to 800nm were polymerized at 1.5 GPa, 573 K and 2.0 GPa, 700 K, respectively. Raman and photoluminescence (PL) spectroscopy were employed to characterize the polymeric phases of the treated samples. Both Raman and PL spectra showed that the C 60 nanotubes transformed into the dimer (D) and orthorhombic (O) phases under the two different conditions, respectively. The photoluminescence peaks were tuned from visible to near infrared range. Comparative studies indicated that C 60 nanotubes were more difficult to polymerize than bulk C 60 material under the same conditions due to the nanoscale size effect in the C 60 nanotubes.

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Nucleobase-Directed Amyloid Nanotube Assembly

Cited by 49 publications

References 40 publications

Accurate Determination of Interstrand Distances and Alignment in Amyloid Fibrils by Magic Angle Spinning NMR

Accurate Determination of Interstrand Distances and Alignment in Amyloid Fibrils by Magic Angle Spinning NMR

Origin of life. Primordial genetics: Information transfer in a pre-RNA world based on self-replicating beta-sheet amyloid conformers

High pressure and high temperature induced polymerization of C60 nanotubes

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