2011
DOI: 10.1016/j.jcis.2011.04.046
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Self-assembly of short amyloidogenic peptides at the air–water interface

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Cited by 11 publications
(13 citation statements)
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“…The remarkable hysteresis observed in the case of PyA3UA is suggestive of irreversible changes caused by compression of the peptide film, probably due to formation of heterogeneous 3D aggregates. 35 Further differences are made evident by considering the variation of the surface compressibility modulus of the two compounds during formation of the peptide films. The surface compressibility factor (K) is defined as 1Basically, the higher the value of K, the tighter is the lateral packing of the molecules.…”
Section: Peptide Film Formation At the Air/water Interfacementioning
confidence: 99%
“…The remarkable hysteresis observed in the case of PyA3UA is suggestive of irreversible changes caused by compression of the peptide film, probably due to formation of heterogeneous 3D aggregates. 35 Further differences are made evident by considering the variation of the surface compressibility modulus of the two compounds during formation of the peptide films. The surface compressibility factor (K) is defined as 1Basically, the higher the value of K, the tighter is the lateral packing of the molecules.…”
Section: Peptide Film Formation At the Air/water Interfacementioning
confidence: 99%
“…These short peptides could self-assemble into typical amyloid fibrils on their own and played determinative roles for the amyloidogenic property of their full-length versions. [12][13][14][15][16][17][18][19] On the other hand, some de novo designed short peptides have also shown the ability to form amyloid fibrils, providing useful models for investigating the molecular basis of this intriguing process. [20][21][22][23][24][25] Although these peptides were still quite different from each other considering their exact amino acid sequences, a large proportion of them showed a common feature of amphiphilic structure, suggesting the essential role of hydrophobic interaction in the formation of amyloid fibrils.…”
Section: Introductionmentioning
confidence: 99%
“…It was widely accepted that A β aggregates are generated by a nucleation-dependent polymerization mechanism, which is composed of two steps: the nucleation of A β peptides into short fibrils and the extension of the fibril ends by attachment with monomers [53]. In another work reported by Nagaraj et al, it has been shown that the AWI also influences the aggregation of shorter amyloidogenic peptides through enhanced self-assembly [54]. These works provide evidence that the AWI plays an essential role in the formation of A β -fibrils at a low concentration, in turn suggesting that the interference from the AWI should be carefully considered for a more precise evaluation of protein amyloidosis modulated by biological interfaces in vitro.…”
Section: Hydrophobic–hydrophilic Interfaces Triggered Accumulationmentioning
confidence: 99%