3 research outputs found
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Ultrathin positively charged electrode skin for durable anion-intercalation battery chemistries
The anion-intercalation chemistries of graphite have the potential to construct batteries with promising energy and power breakthroughs. Here, we report the use of an ultrathin, positively charged two-dimensional poly(pyridinium salt) membrane (C2DP) as the graphite electrode skin to overcome the critical durability problem. Large-area C2DP enables the conformal coating on the graphite electrode, remarkably alleviating the electrolyte. Meanwhile, the dense face-on oriented single crystals with ultrathin thickness and cationic backbones allow C2DP with high anion-transport capability and selectivity. Such desirable anion-transport properties of C2DP prevent the cation/solvent co-intercalation into the graphite electrode and suppress the consequent structure collapse. An impressive PF6â-intercalation durability is demonstrated for the C2DP-covered graphite electrode, with capacity retention of 92.8% after 1000 cycles at 1 C and Coulombic efficiencies of > 99%. The feasibility of constructing artificial ion-regulating electrode skins with precisely customized two-dimensional polymers offers viable means to promote problematic battery chemistries
Recommended from our members
Ultrathin positively charged electrode skin for durable anion-intercalation battery chemistries
The anion-intercalation chemistries of graphite have the potential to construct batteries with promising energy and power breakthroughs. Here, we report the use of an ultrathin, positively charged two-dimensional poly(pyridinium salt) membrane (C2DP) as the graphite electrode skin to overcome the critical durability problem. Large-area C2DP enables the conformal coating on the graphite electrode, remarkably alleviating the electrolyte. Meanwhile, the dense face-on oriented single crystals with ultrathin thickness and cationic backbones allow C2DP with high anion-transport capability and selectivity. Such desirable anion-transport properties of C2DP prevent the cation/solvent co-intercalation into the graphite electrode and suppress the consequent structure collapse. An impressive PF6â-intercalation durability is demonstrated for the C2DP-covered graphite electrode, with capacity retention of 92.8% after 1000 cycles at 1 C and Coulombic efficiencies of > 99%. The feasibility of constructing artificial ion-regulating electrode skins with precisely customized two-dimensional polymers offers viable means to promote problematic battery chemistries
Lipid Bilayers Significantly Modulate Cross-Fibrillation of Two Distinct Amyloidogenic Peptides
Amyloid plaques comprising misfolded
proteins are the hallmark
of several incurable diseases, including Alzheimerâs disease,
type-II diabetes, JacobâCreutzfeld disease, and others. While
the exact molecular mechanisms underlying protein misfolding diseases
are still unknown, several theories account for amyloid fiber formation
and their toxic significance. Prominent among those is the âprion
hypothesisâ stipulating that misfolded protein seeds act as
âinfectious agentsâ propagating aggregation of nominally
healthy, native proteins. Recent studies, in fact, have reported that
interactions between different amyloid peptides that are partly sequence-related
might also affect fibrillation pathways and pathogenicity. Here, we
present evidence that two structurally and physiologically unrelated
amyloidogenic peptides, the islet amyloid polypeptide (IAPP, the peptide
comprising the amyloid aggregates in type II diabetes) and an amyloidogenic
determinant of the prion protein (PrP), give rise to a significantly
distinct fibrillation pathway when they are incubated together in
the presence of membrane bilayers. In particular, the experimental
data demonstrate that the lipid bilayer environment is instrumental
in initiating and promoting the assembly of morphologically distinct
fibrillar species. Moreover, cross-fibrillation produced peptide species
exhibiting significantly altered membrane interaction profiles, as
compared to the scenario where the two peptides aggregated separately.
Overall, our data demonstrate that membranes constitute a critical
surface-active medium for promoting interactions between disparate
amyloidogenic peptides, modulating both fibrillation pathways as well
as the biophysical properties of the peptide aggregates. This work
hints that membrane-induced cross-fibrillation of unrelated amyloidogenic
peptides might play an insidious role in the molecular pathologies
of protein misfolding diseases