Structural and Conformational
Dynamics of Self-Assembling
Bioactive β‑Sheet Peptide Nanostructures Decorated with
Multivalent RNA-Binding Peptides
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Abstract
Understanding the dynamic behavior of nanostructural
systems is
important during the development of controllable and tailor-made nanomaterials.
This is particularly true for nanostructures that are intended for
biological applications because biomolecules are usually highly dynamic
and responsive to external stimuli. In this Article, we investigated
the structural and conformational dynamics of self-assembling bioactive
β-sheet peptide nanostructures using electron paramagnetic resonance
(EPR) spectroscopy. The model peptide nanostructures are characterized
by the cross-β spine of β-ribbon fibers and multiple RNA-binding
bioactive peptides that constitute the shell of the nanostructures.
We found first, that bioactive peptides at the shell of β-ribbon
nanostructure have a mobility similar to that of an isolated monomeric
peptide. Second, the periphery of the cross-β spine is more
immobile than the distal part of surface-displayed bioactive peptides.
Third, the rotational dynamics of short and long fibrils are similar;
that is, the mobility is largely independent of the extent of aggregation.
Fourth, peptides that constitute the shell are affected first by the
external environment at the initial stage. The cross-β spine
resists its external environment to a certain extent and abruptly
disintegrates when the perturbation reaches a certain degree. Our
results provide an overall picture of β-sheet peptide nanostructure
dynamics, which should be useful in the development of dynamic self-assembled
peptide nanostructures