Solid-State NMR characterization of autofluorescent fibrils formed by the elastin-derived peptide GVGVAGVG.
Biomacromolecules. 2011 May 9;12(5):1546-55
Authors: Sharpe S, Simonetti K, Yau J, Walsh P
Abstract
The characterization of the molecular structure and physical properties of self-assembling peptides is an important aspect of optimizing their utility as scaffolds for biomaterials and other applications. Here we report the formation of autofluorescent fibrils by an octapeptide (GVGVAGVG) derived via a single amino acid substitution in one of the hydrophobic repeat elements of human elastin. This is the shortest and most well-defined peptide so far reported to exhibit intrinsic fluorescence in the absence of a discrete fluorophore. Structural characterization by FTIR and solid-state NMR reveals a predominantly ?-sheet conformation for the peptide in the fibrils, which are likely assembled in an amyloid-like cross-? structure. Investigation of dynamics and the effects of hydration on the peptide are consistent with a rigid, water excluded structure, which has implications for the likely mechanism of intrinsic fibril fluorescence.
Structural Characterization of Polyglutamine Fibrils by Solid-State NMR Spectroscopy.
Structural Characterization of Polyglutamine Fibrils by Solid-State NMR Spectroscopy.
Structural Characterization of Polyglutamine Fibrils by Solid-State NMR Spectroscopy.
J Mol Biol. 2011 Jul 13;
Authors: Schneider R, Schumacher MC, Mueller H, Nand D, Klaukien V, Heise H, Riedel D, Wolf G, Behrmann E, Raunser S, Seidel R, Engelhard M, Baldus M
Protein aggregation via polyglutamine stretches occurs in a number of severe neurodegenerative diseases such as Huntington's disease. We have investigated fibrillar aggregates of polyglutamine peptides...
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07-19-2011 07:52 PM
The Core of Ure2p Prion Fibrils Is Formed by the N-Terminal Segment in a Parallel Cross-? Structure: Evidence from Solid-State NMR.
The Core of Ure2p Prion Fibrils Is Formed by the N-Terminal Segment in a Parallel Cross-? Structure: Evidence from Solid-State NMR.
The Core of Ure2p Prion Fibrils Is Formed by the N-Terminal Segment in a Parallel Cross-? Structure: Evidence from Solid-State NMR.
J Mol Biol. 2011 Apr 8;
Authors: Kryndushkin DS, Wickner RB, Tycko R
Intracellular fibril formation by Ure2p produces the non-Mendelian genetic element in Saccharomyces cerevisiae, making Ure2p a prion protein. We show that solid-state NMR spectra of full-length Ure2p fibrils, seeded...
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04-19-2011 11:01 PM
Solid-state NMR evidence for elastin-like beta-turn structure in spider dragline silk.
Solid-state NMR evidence for elastin-like beta-turn structure in spider dragline silk.
Solid-state NMR evidence for elastin-like beta-turn structure in spider dragline silk.
Chem Commun (Camb). 2010 Sep 28;46(36):6714-6
Authors: Jenkins JE, Creager MS, Butler EB, Lewis RV, Yarger JL, Holland GP
Two-dimensional homo- and heteronuclear solid-state MAS NMR experiments on (13)C/(15)N-proline labeled Argiope aurantia dragline silk provide evidence for an elastin-like beta-turn structure for the repetitive Gly-Pro-Gly-X-X motif prevalent in major...
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12-28-2010 03:31 PM
[NMR paper] Structure distribution in an elastin-mimetic peptide (VPGVG)3 investigated by solid-s
Structure distribution in an elastin-mimetic peptide (VPGVG)3 investigated by solid-state NMR.
Related Articles Structure distribution in an elastin-mimetic peptide (VPGVG)3 investigated by solid-state NMR.
J Am Chem Soc. 2004 Apr 7;126(13):4199-210
Authors: Yao XL, Hong M
Elastin is an extracellular-matrix protein that imparts elasticity to tissues. We have used solid-state NMR to determine a number of distances and torsion angles in an elastin-mimetic peptide, (VPGVG)3, to understand the structural basis of elasticity. C-H and C-N distances...
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11-24-2010 09:51 PM
[NMR paper] Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR
Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR.
Related Articles Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR.
Magn Reson Chem. 2004 Feb;42(2):267-75
Authors: Yao XL, Conticello VP, Hong M
Elastin is the main structural protein that provides elasticity to various tissues and organs in vertebrates. Molecular motions are believed to play a significant role in its elasticity. We have used solid-state NMR spectroscopy to characterize the dynamics of an elastin-mimetic...
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11-24-2010 09:25 PM
[NMR paper] Structure of an elastin-mimetic polypeptide by solid-state NMR chemical shift analysi
Structure of an elastin-mimetic polypeptide by solid-state NMR chemical shift analysis.
Related Articles Structure of an elastin-mimetic polypeptide by solid-state NMR chemical shift analysis.
Biopolymers. 2003 Oct;70(2):158-68
Authors: Hong M, Isailovic D, McMillan RA, Conticello VP
The conformation of an elastin-mimetic recombinant protein, 39, is investigated using solid-state NMR spectroscopy. The protein is extensively labeled with 13C and 15N, and two-dimensional 13C-13C and 15N-13C correlation experiments were carried out to resolve and...
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11-24-2010 09:16 PM
[NMR paper] Solid-state (13)C NMR reveals effects of temperature and hydration on elastin.
Solid-state (13)C NMR reveals effects of temperature and hydration on elastin.
Related Articles Solid-state (13)C NMR reveals effects of temperature and hydration on elastin.
Biophys J. 2002 Feb;82(2):1086-95
Authors: Perry A, Stypa MP, Tenn BK, Kumashiro KK
Elastin is the principal protein component of the elastic fiber in vertebrate tissue. The waters of hydration in the elastic fiber are believed to play a critical role in the structure and function of this largely hydrophobic, amorphous protein. (13)C CPMAS NMR spectra are acquired for...
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11-24-2010 08:49 PM
[NMR paper] An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed
An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed by cold shock protein A.
Related Articles An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed by cold shock protein A.
Pac Symp Biocomput. 2001;:67-78
Authors: Alexandrescu AT
Acid-denatured cold shock protein A (CspA) self-assembles into polymers with properties typical of amyloid fibrils. In the present work, a quenched hydrogen exchange experiment was used to probe the interactions of CspA fibrils with solvent. Exchange...
Solid-State NMR characterization of autofluorescent fibrils formed by the elastin-derived peptide GVGVAGVG.
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