Herein, we report that short peptides are capable of exploiting their anti-parallel registry to access cross-β stacks to expose more than one catalytic residue, exhibiting the traits of advanced binding...
Extant proteins exploit thermodynamically activated negatively
charged coenzymes and hydrotropes to temporally access mechanistically
important conformations that regulate vital biological functions,
from metabolic reactions to expression modulation. Herein, we show
that a short amyloid peptide can bind to a small molecular coenzyme
by exploiting reversible covalent linkage to polymerize and access
catalytically proficient nonequilibrium amyloid microphases. Subsequent
hydrolysis of the activated coenzyme leads to depolymerization, realizing
a variance of the surface charge of the assembly as a function of
time. Such temporal change of surface charge dynamically modulates
catalytic activities of the transient assemblies as observed in highly
evolved modern-day biocatalysts.
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