Amyloid formation characteristics of GNNQQNY from yeast prion protein Sup35 and its seeding with heterogeneous polypeptides

Haratake, Mamoru; Takiguchi, T.; Masuda, Naho; Yoshida, Sakura; Fuchigami, Takeshi; Nakayama, Morio

doi:10.1016/j.colsurfb.2016.10.011

Cited by 10 publications

(12 citation statements)

References 46 publications

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“…The two termini of each GNNQQNY peptide chain are charged (NH 3 + and COO À ) to mimic the neutral experimental pH condition. 62 Each system consists of eight peptide chains with random coil conformation for each chain. The eight GNNQQNY chains were placed randomly in a 6.7 Â 6.7 Â 6.7 nm 3 box lled with SPC water molecules.…”

Section: Initial Conformations Of Gnn and Gnn + C 60 Systemsmentioning

confidence: 99%

Inhibitory effect of hydrophobic fullerenes on the β-sheet-rich oligomers of a hydrophilic GNNQQNY peptide revealed by atomistic simulations

Lei

Xie

et al. 2017

RSC Adv.

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Section: Initial Conformations Of Gnn and Gnn + C 60 Systemsmentioning

confidence: 99%

Inhibitory effect of hydrophobic fullerenes on the β-sheet-rich oligomers of a hydrophilic GNNQQNY peptide revealed by atomistic simulations

Lei

Xie

et al. 2017

RSC Adv.

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“…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%

“…[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. [26][27][28][29][30] Among all these amyloid-like peptides, Aβ [16][17][18][19][20][21][22] with the sequence of KLVFFAE might be the most widely studied one. 31 A lot of work have been done on this peptide, but its bolaamphiphilic feature, ie, 2 hydrophilic heads connected by a hydrophobic section, has not received enough attention.…”

Section: Introductionmentioning

confidence: 99%

Amyloid‐like aggregation of designer bolaamphiphilic peptides: Effect of hydrophobic section and hydrophilic heads

Qiu

Tang

Chen

2017

Journal of Peptide Science

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Amyloid-like aggregation of natural proteins or polypeptides is an important process involved in many human diseases as well as some normal biological functions. Plenty of works have been done on this ubiquitous phenomenon, but the molecular mechanism of amyloid-like aggregation has not been fully understood yet. In this study, we showed that a series of designer bolaamphiphilic peptides could undergo amyloid-like aggregation even though they didn't possess typical β-sheet secondary structure. Through systematic amino acid substitution, we found that for the self-assembling ability, the number and species of amino acid in hydrophobic section could be variable as long as enough hydrophobic interaction is provided, while different polar amino acids as the hydrophilic heads could change the self-assembling nanostructures with their aggregating behaviors affected by pH value change. Based on these results, novel self-assembling models and aggregating mechanisms were proposed, which might provide new insight into the molecular basis of amyloid-like aggregation.

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“…Addition of seeds eliminated the lag-phase by spontaneously reducing the monomer concentration to 25% within 3-4 h of incubation (figure 2B). This is mainly because the added aggregates act as templates for monomer addition, thereby drives the aggregation via the elongation-phase [29,34,[63][64][65][66][67].…”

Section: Resultsmentioning

confidence: 99%

GNNQQNY: Methodology for biophysical and structural understanding of aggregation

Burra

Maina

Serpell

et al. 2022

Preprint

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GNNQQNY sequence offers crucial information about the formation and structure of an amyloid fibril. In this study, we demonstrate a reproducible solubilisation protocol where the reduction of pH to 2.0 resulted in the generation of GNNQQNY monomers. The subsequent ultracentrifugation step removes the residual insoluble peptide from the homogeneous solution. This procedure ensures and allows the peptides to remain monomers till their aggregation is triggered by adjusting the pH to 7.2. The aggregation kinetics analysis showed a distinct lag-phase that is concentration-dependent, indicating nucleation-dependent aggregation kinetics. Nucleation kinetics analysis suggested a critical nucleus of size ~7 monomers at physiological conditions. The formed nucleus acts as a template for further self-assembly leading to the formation of highly ordered amyloid fibrils. These findings suggest that the proposed solubilisation protocol provides the basis for understanding the kinetics and thermodynamics of amyloid nucleation and elongation in GNNQQNY sequences. This procedure can also be used for solubilising such small amyloidogenic sequences for their biophysical studies.

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Amyloid formation characteristics of GNNQQNY from yeast prion protein Sup35 and its seeding with heterogeneous polypeptides

Cited by 10 publications

References 46 publications

Inhibitory effect of hydrophobic fullerenes on the β-sheet-rich oligomers of a hydrophilic GNNQQNY peptide revealed by atomistic simulations

Inhibitory effect of hydrophobic fullerenes on the β-sheet-rich oligomers of a hydrophilic GNNQQNY peptide revealed by atomistic simulations

Amyloid‐like aggregation of designer bolaamphiphilic peptides: Effect of hydrophobic section and hydrophilic heads

GNNQQNY: Methodology for biophysical and structural understanding of aggregation

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