Structure of cis-[PdCl2L] (L = 1,4,7-trithiacyclononane)

Blake, Alexander J.; Holder, Alan J.; Roberts, Yvonne V.; Schröder, Martin

doi:10.1107/s0108270187010254

Cited by 21 publications

(28 citation statements)

References 3 publications

(3 reference statements)

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“…A plausible model to explain ¢bril formation would be that in the absence of the head to establish registration, oligomers can form through out of register interactions leading to long unbranched sub-proto¢laments. These sub-proto¢laments could then associate into proto¢laments as proposed for amyloid ¢brils formed from other proteins or peptides [3,4].…”

Section: Resultsmentioning

confidence: 99%

“…Numerous diseases such as Alzheimer's disease, maturity onset diabetes and transmissible spongiform encephalopathies are associated with deposition of insoluble ¢brils named amyloid ¢brils in tissues [2]. Current models of amyloid ¢brils propose that the ¢brils adopt a cross-L-structure with Lstrands perpendicular to the ¢ber axis [3,4]. This cross-L-structure seems to be a structural motif common to all amyloid ¢brils independent of sequence or structural folds of the proteins the ¢brils originate from [4].…”

Section: Introductionmentioning

confidence: 99%

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A peptide from the adenovirus fiber shaft forms amyloid‐type fibrils

et al. 2000

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The fiber protein of adenovirus consists of a Cterminal globular head, a shaft and a short N-terminal tail. The crystal structure of a stable domain comprising the head plus a part of the shaft of human adenovirus type 2 fiber has recently been solved at 2.4 A î resolution Nature 401, 935^938]. A peptide corresponding to the portion of the shaft immediately adjacent to the head (residues 355^396) has been synthesized chemically. The peptide failed to assemble correctly and instead formed amyloid-type fibrils as assessed by electron microscopy, Congo red binding and X-ray diffraction. Peptides corresponding to the fiber shaft could provide a model system to study mechanisms of amyloid fibril formation.z 2000 Federation of European Biochemical Societies.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A peptide from the adenovirus fiber shaft forms amyloid‐type fibrils

et al. 2000

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“…The structures of in vivo aggregated proteins have been analyzed by Fourier transform infrared (FT-IR) spectroscopy, X-ray di¡raction, electron microscopy (EM), and solid-state nuclear magnetic resonance (NMR). The spectroscopic techniques are in wide use for L-amyloid, in which cross L-structures lead to formation of an insoluble ¢lament (FT-IR [22], X-ray [23], EM [24], liquid NMR [25], solid-state NMR [26]); however, fewer approaches have been applied to inclusion bodies because of their heterogeneous structures. For the heterogeneous aggregates, FT-IR spectroscopy is often used to analyze the secondary structure, using the bands corresponding to amide bond stretching [7,9,22].…”

Section: Introductionmentioning

confidence: 99%

Structural characteristics and refolding of in vivo aggregated hyperthermophilic archaeon proteins

et al. 2003

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Several recombinant proteins in inclusion bodies expressed in Escherichia coli have been measured by Fourier transform infrared and solid-state nuclear magnetic resonance spectra to provide the secondary structural characteristics of the proteins from hyperthermophilic archaeon Pyrococcus horikoshii OT3 (hyperthermophilic proteins) in inclusion bodies. The L L-strand-rich single chain Fv fragment (scFv) and K K-helix-rich interleukin (IL)-4 lost part of the native-like secondary structure in inclusion bodies, while the inclusion bodies composed of the hyperthermophilic proteins of which the native form is K K-helix rich, are predominated by K K-helix structure. Further, the secondary structure of the recombinant proteins solubilized from inclusion bodies by detergent or denaturant was observed by circular dichroism (CD) spectra. The solubilization induced the denaturation of the secondary structure for scFv and IL-4, whereas the solubilized hyperthermophilic proteins have retained the K K-helix structure with the CD properties resembling those of their native forms. This indicates that the hyperthermophilic proteins form native-like secondary structure in inclusion bodies. Refolding of several hyperthermophilic proteins from in vivo aggregated form without complete denaturation could be accomplished by solubilization with lower concentration (e.g. 2 M) of guanidine hydrochloride and removal of the denaturant via stepwise dialysis. This supports the existence of proteins with nativelike structure in inclusion bodies and suggests that non-native association between the secondary structure elements leads to in vivo aggregation. We propose a refolding procedure on the basis of the structural properties of the aggregated archaeon proteins.

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“…[1][2][3][4][5] Abbildung 4 zeigt eine verdrillte, aus vier b-Faltblattsträngen bestehende Fibrille mit einer Cross-b-Struktur. Fibrillen haben oft eine Helixstruktur; Beispiele sind Transthyretin, [32] die SH3-Domäne von Phosphatidylinositol-3'-kinase [33] und Rinderinsulin [34] (weitere Beispiele sind in Lit. [5] aufgeführt).…”

Section: Struktur Von Fibrillenunclassified

“…[173] Eine Fibrillenbildung war nur zu beobachten, wenn die Ladung der Peptide AE 1 betrug. Die Peptide bildeten eine Cross-b-Struktur mit vier antiparallelen b-Faltblättern, die parallel zur Achse der Protofilamente angeordnet waren, ähnlich dem Modell von Blake und Serpell [32] (allerdings gab es keine Anzeichen für eine Verdrillung der b-Faltblätter).…”

Section: Fibrillenbildung Von De Novo Hergestellten Peptidenunclassified

Bildung von Peptidfibrillen

Hamley

2007

Angewandte Chemie

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Die Bildung von Peptidfibrillen spielt eine bedeutende Rolle bei vielen Krankheiten, die durch Amyloidablagerungen verursacht werden. Intensiv erforscht wird die Bildung von Fibrillen aber auch wegen ihres großen Anwendungspotenzials in der Bionanotechnologie, wo Hydrogele aus Peptidfibrillen als Zellgerüste und als Substrate für funktionelle und responsive Biomaterialien, Biosensoren und Nanodrähte Anwendung finden können. In diesem Aufsatz werden die grundlegenden Aspekte der Selbstorganisation von Peptiden zu Fibrillen behandelt. Sowohl natürliche amyloidbildende Peptide als auch synthetische Verbindungen, z. B. Peptidfragmente, Copolymere und Amphiphile, werden diskutiert.

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Structure of cis-[PdCl2L] (L = 1,4,7-trithiacyclononane)

Abstract: Abstract.[PdCI2 (

Cited by 21 publications

References 3 publications

A peptide from the adenovirus fiber shaft forms amyloid‐type fibrils

A peptide from the adenovirus fiber shaft forms amyloid‐type fibrils

Structural characteristics and refolding of in vivo aggregated hyperthermophilic archaeon proteins

Bildung von Peptidfibrillen

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