Facial Symmetry in Protein Self-Assembly

Mehta, Anil; Lu, Kun Ping; Childers, W. Seth; Ling, Yan; Dublin, Steven N.; Dong, Jijun; Snyder, James P.; Pingali, Sai Venkatesh; Thiyagarajan, P.; Lynn, David G.

doi:10.1021/ja801511n

Cited by 240 publications

(517 citation statements)

References 59 publications

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“…For example, synthetic lipids such as amphiphilic molecules that append sugar, peptide, and nucleic acid moieties as hydrophilic headgroups (24) form hollow cylindrical architectures that can be further used to incorporate metal particles. Also, since the discovery of amyloid-related diseases, scientists have realized that proteins, but also small peptides, have the general property of forming fibers/nanotubes through a self-assembly process (25,26). Therefore, small peptides based on protein sequences have been widely studied for their ability to form well-defined nano-architectures, in particular those forming β-sheet stabilized nanotubes and fibers (27) or fibrous materials from α-helical peptides (28,29).…”

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confidence: 99%

Control of peptide nanotube diameter by chemical modifications of an aromatic residue involved in a single close contact

Tarabout

Roux

Gobeaux

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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Supramolecular self-assembly is an attractive pathway for bottomup synthesis of novel nanomaterials. In particular, this approach allows the spontaneous formation of structures of well-defined shapes and monodisperse characteristic sizes. Because nanotechnology mainly relies on size-dependent physical phenomena, the control of monodispersity is required, but the possibility of tuning the size is also essential. For self-assembling systems, shape, size, and monodispersity are mainly settled by the chemical structure of the building block. Attempts to change the size notably by chemical modification usually end up with the loss of self-assembly. Here, we generated a library of 17 peptides forming nanotubes of monodisperse diameter ranging from 10 to 36 nm. A structural model taking into account close contacts explains how a modification of a few Å of a single aromatic residue induces a fourfold increase in nanotube diameter. The application of such a strategy is demonstrated by the formation of silica nanotubes of various diameters.size control | mineralization | structural approach | size prediction

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mentioning

confidence: 99%

Control of peptide nanotube diameter by chemical modifications of an aromatic residue involved in a single close contact

Tarabout

Roux

Gobeaux

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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“…Thus, a higher order geometrical restraint appears to be at play in the DA-(OV)4 structures. This could, for example, arise from a curvature in the "ribbons" such that they form closed nanotubes as has been observed for other amyloids (29)(30)(31). This interpretation would also explain the complete .…”

Section: Resultsmentioning

confidence: 72%

Cooperative induction of ordered peptide and fatty acid aggregates

Riek

Greenwald

Kwiatkowski

et al. 2018

Preprint

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Interactions between biological membranes and disease-associated amyloids are well documented and their prevalence suggests that an inherent affinity exists between these two distinct molecular assemblies. Within the framework of our research project on amyloids and the origins of life, we hypothesized here that such interactions could increase both the sequence and structure space of peptide amyloids in a heterogeneous system and that if cooperative in nature, the interaction could be advantageous to the propagation of these entities in a prebiotic context. Thus, we have investigated the interplay between vesicle-forming fatty acids and amyloidogenic peptides, the respective precursors of lipids and proteins. Individually they are able to form ordered structures under a limited range of conditions with the bilayer of fatty acid vesicles and the cross-β core of amyloids both being repetitive structures that could in principle support a cooperative interaction. Here we report that an 8-residue basic peptide that can form an amphipathic β-strand, that is soluble at neutral pH and that can form amyloids above its pI at pH 11, is also able to cooperatively form novel co-aggregates of diverse structure with and in the context of simple fatty acids at neutral pH. Below the critical vesicle concentration (CVC) the mixtures of fatty acid and peptide yield a flocculent precipitate with an underlying β-structure. Above the CVC, the mixtures yield ribbon or tube-like structures that bear some of the hallmarks of amyloids yet have associated with them a significant amount of fatty acids, likely in a bilayer structure. In the context of the origin of cellular life these results expand the phase space of both peptides and fatty acids while providing a simple yet robust physical connection between two distinct biological entities relevant for life.

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“…The minimum at 214 nm indicates a b-sheet structure. [7] The second minimum at 232 nm results from the stacking of aromatic amino acids and has been reported previously for modified Ab peptide fragments in an aqueous solution. the first minimum at 214 nm is consistent with b-sheet structure [7] and the second minimum at 232 nm is due to the stacking of aromatic amino acids.…”

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confidence: 55%

“…Studies have shown that early stage aggregates contribute to Ab neurotoxicity and are potentially viable drug targets. [1][2][3] Several fragments of Ab, such as Ab [18][19][20][21][22][23][24][25][26][27][28] , [4] Ab , [5] Ab [16][17][18][19][20][21][22] , [6,7] and Ab 16-20 [8] have been shown to form amyloid fibrils. Recent studies on the hydrophobic core Ab [16][17][18][19][20] suggested that the Lys-Leu-Val-Phe-Phe peptide sequence is critical for fibril formation.…”

Section: Introductionmentioning

confidence: 99%

“…In general, a strong bsheet signature with a minimum at 214 nm was observed. [7] Variable temperature CD experiments for compounds [1][2][3][4] show that the CD intensity at 214 nm is decreasing dramatically with an increase in temperature from 25 8C to 708C, suggesting a weakening of hydrogen bonds at higher temperatures (see the Supporting Information). Next, the CD spectra of compounds 1-4 were measured in a mixture of 50 % CH 3 CN/ tris buffer at pH 8.5 in order to enhance the solubility of Fcpeptides, while maintaining an aqueous environment.…”

mentioning

confidence: 99%

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Electrochemical “Signal‐On” Reporter for Amyloid Aggregates

2011

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The synthesis and characterization of four new Ferrocene (Fc) bioconjugates, bearing a podant (Lys)-Leu-Val-Phe-Phe motif, namely the hydrophobic sequence of amyloid-β-peptides (Aβ), is reported. The Fc-peptide conjugates are characterized by a reversible redox activity and the ability to undergo hydrophobic and hydrogen bonding interactions. Biomolecular interactions between Fc-bioconjugates with Aβ(12-28) fragments were studied by circular dichroism (CD), transmission electron microscopy (TEM), and electrochemistry. All four Fc-peptides interacted favourable with Aβ(12-28) and prevented fibril formation, the extent of which depended on the length of the peptide and the nature of the C-terminal group. The aggregates obtained for the Aβ(12-28)/Fc-peptide mixtures range from short fibrils to spherical aggregates. We demonstrated that in solution the peptide sequence and peptide charge affect the biomolecular interactions. Fc-peptide interactions with immobilized Aβ(12-28)-Cys films on Au surfaces were detected by measuring the current response of the Fc redox process. The formal redox potential, E(0), at ~440 (10) mV and i(pc)/i(pa) at 0.9 were observed characteristic for the monosubstituted Fc-derivative undergoing a one-electron redox process. On the surface, methyl ester-protected Fc-peptides (1 and 3) interacted only weakly with Aβ(12-28)-Cys films, giving rise to minimal redox activity. In contrast, charged Fc-peptides (2 and 4) gave a significant electrochemical readout following the interaction with Aβ(12-28)-Cys films. Interestingly, the Fc-peptide charge dictates the surface-assisted interactions, while hydrophobic and ionic effects contribute to the overall solution behaviour of the Fc-bioconjugates with Aβ(12-28).

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Facial Symmetry in Protein Self-Assembly

Cited by 240 publications

References 59 publications

Control of peptide nanotube diameter by chemical modifications of an aromatic residue involved in a single close contact

Control of peptide nanotube diameter by chemical modifications of an aromatic residue involved in a single close contact

Cooperative induction of ordered peptide and fatty acid aggregates

Electrochemical “Signal‐On” Reporter for Amyloid Aggregates

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