The Role of Decorated SDS Micelles in Sub-CMC Protein Denaturation and Association

Andersen, Kell K.; Oliveira, Cristiano L. P.; Larsen, Kim Lambertsen; Poulsen, Flemming M.; Callisen, Thomas HÃ ̧nger; Westh, Peter; Pedersen, Jan Skov; Otzen, Daniel E.

doi:10.1016/j.jmb.2009.06.019

Cited by 139 publications

(124 citation statements)

References 67 publications

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“…Both samples featured similar core radii and aspect ratios, whereas the shell thickness in the presence of the peptide was about twice as large as for SDS alone. This suggests that A␤ is attached to the SDS micelle headgroup shell in agreement with previous NMR studies (21) and SAXS studies for surfactant-protein systems (19,22,47). The upturn in intensity at low scattering vector values q for the SDS-A␤ sample (Fig.…”

Section: Structure Of Surfactant-a␤ Co-aggregates Revealed By Saxssupporting

confidence: 90%

“…Prolate or oblate ellipsoidal core-shell models fit the data equally well. Fitting parameters for an oblate ellipsoid (Table 1) are in good agreement with previous studies (46,47). Both samples featured similar core radii and aspect ratios, whereas the shell thickness in the presence of the peptide was about twice as large as for SDS alone.…”

Section: Structure Of Surfactant-a␤ Co-aggregates Revealed By Saxssupporting

confidence: 87%

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Formation of Dynamic Soluble Surfactant-induced Amyloid β Peptide Aggregation Intermediates

Abelein

Kaspersen²,

Nielsen

et al. 2013

Journal of Biological Chemistry

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Background: ␤-Structured oligomers of the amyloid ␤ peptide are considered neurotoxic and on-pathway to amyloid fibril formation. Results: Surfactant-induced co-aggregated oligomers show dynamic rapid exchange with free peptide during a slow fibril formation process. Conclusion: ␤-Structure inducing small molecules kinetically promote peptide assembly into co-aggregates. Significance: Knowledge about molecular mechanisms of peptide aggregation modulators is potentially helpful for therapeutic purposes.

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Section: Structure Of Surfactant-a␤ Co-aggregates Revealed By Saxssupporting

confidence: 90%

Section: Structure Of Surfactant-a␤ Co-aggregates Revealed By Saxssupporting

confidence: 87%

Formation of Dynamic Soluble Surfactant-induced Amyloid β Peptide Aggregation Intermediates

Abelein

Kaspersen²,

Nielsen

et al. 2013

Journal of Biological Chemistry

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show abstract

“…11b,c). It is known that globular proteins have the tendency to unfold when combined with ionic surfactants 30,31 . To test this hypothesis, a 0.008 mM ELP5 solution was combined with the oppositely charged commercial surfactant dodecyltrimethylammonium bromide (DTAB) above its critical micelle concentration (18 mM).…”

Section: Resultsmentioning

confidence: 99%

Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein–peptide system

et al. 2015

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ature uses self-assembly to create a widespread variety of complex structures with elaborate geometries and outstanding properties 1 such as hierarchical order, adaptability, selfhealing and bioactivity. Developing new bioinspired processes based on dynamic self-assembly could facilitate the fabrication of synthetic three-dimensional (3D) materials with enhanced complexity, dynamic properties and functionality 2 . Proteins are particularly attractive building blocks because of their versatility and biofunctionality 3 . Elastin-like polypeptides (ELPs) 4 are recombinant proteins that have generated great interest 5 as a result of their modular structure, bioactivity, ease of design and production, and the possibility to create robust and elastic materials 5,6 . ELPs allow for a tunable molecular design 7 and are based on the tropoelastin recurrent motif Val-Pro-Gly-X-Gly (VPGXG), in which X is any amino acid other than proline 7 . This repeating pentapeptide provides ELPs with a thermoresponsive behaviour. Below a critical transition temperature (T t ), the ELP molecule undergoes a reversible-phase transition wherein the protein is soluble in aqueous solution and becomes highly solvated, surrounded by clatharate-like water structures. Above the T t , the hydrophobic domains dehydrate and the protein chain hydrophobically collapses and aggregates to form a phaseseparated state 8 .The use of natural and synthetic proteins to create functional materials has been hindered by the difficulty in controlling their conformation and nanoscale assembly with the precision required to form macroscopic materials. This limitation has driven the development of simpler and more-predictable peptide-based materials 9,10 . Peptide amphiphiles (PAs), for example, are synthetic molecules that can self-assemble into nanofibres and create functional 3D hydrogels that emulate the fibrous architecture of the extracellular matrix (ECM) 11,12 . Nonetheless, most peptide and/or protein materials are formed through equilibrium-based self-assembly approaches that are capable of generating stable supramolecular structures, but with limited hierarchy and spatiotemporal control, which has hindered their functionality 2 .Novel approaches based on the dynamic self-assembly of inorganic building blocks [13][14][15] , actin self-organization 16 and the combination of top-down processes with peptide self-assembly have been reported recently 17 . In particular, Stupp and co-workers have described a self-assembling membrane system obtained through strong electrostatic interactions between PAs and oppositely charged polysaccharides 18 . However, the possibility to exploit the unique structural and functional properties of proteins to create dynamic hierarchical materials remains an elusive target. In this study, we attempt to overcome this hurdle by using self-assembling peptides to promote protein conformational changes and guide their assembly into complex, yet functional, materials. We report the discovery and development of a protein/peptide system t...

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“…SAXS has been particularly useful when combined with other techniques that constrain modelling, for example ITC or CE which provide protein:surfactant stoichiometries (see 2 for a more detailed discussion). We have proposed a core-shell model for SDS-protein complexes which seems applicable to a growing number of proteins, in which a micellar core is surrounded by a shell of (one or more) protein molecules in a dynamic state 9 . Several such micelles can be joined if one protein is attached to several micelles or if proteins from different clusters interact through their flexible domains, as observed for the aggregationprone protein -synuclein 44 .…”

Section: Shaping Up: Modelling Protein-surfactant Complexes and Protementioning

confidence: 99%

Proteins in a brave new surfactant world

Otzen

2015

Current Opinion in Colloid & Interface Science

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The Role of Decorated SDS Micelles in Sub-CMC Protein Denaturation and Association

Cited by 139 publications

References 67 publications

Formation of Dynamic Soluble Surfactant-induced Amyloid β Peptide Aggregation Intermediates

Formation of Dynamic Soluble Surfactant-induced Amyloid β Peptide Aggregation Intermediates

Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein–peptide system

Proteins in a brave new surfactant world

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