3 research outputs found
Distinct Electrostatic Interactions Govern the Chiro-Optical Properties and Architectural Arrangement of Peptide–Oligothiophene Hybrid Materials
The development of chiral optoelectronic
materials is of great
interest due to their potential of being utilized in electronic devices,
biosensors, and artificial enzymes. Herein, we report the chiral–optical
properties and architectural arrangement of optoelectronic materials
generated from noncovalent self-assembly of a cationic synthetic peptide
and five chemically defined anionic pentameric oligothiophenes. The
peptide–oligothiophene hybrid materials exhibit a three-dimensional
ordered helical structure and optical activity in the π–π*
transition region that are observed due to a single chain induced
chirality of the conjugated thiophene backbone upon interaction with
the peptide. The latter property is highly dependent on electrostatic
interactions between the peptide and the oligothiophene, verifying
that a distinct spacing of the carboxyl groups along the thiophene
backbone is a major chemical determinant for having a hybrid material
with distinct optoelectronic properties. The necessity of the electrostatic
interaction between specific carboxyl functionalities along the thiophene
backbone and the lysine residues of the peptide, as well as the induced
circular dichroism of the thiophene backbone, was also confirmed by
theoretical calculations. We foresee that our findings will aid in
designing optoelectronic materials with dynamic architectonical precisions
as well as offer the possibility to create the next generation of
materials for organic electronics and organic bioelectronics
Evidence for Age-Dependent <i>in Vivo</i> Conformational Rearrangement within Aβ Amyloid Deposits
Deposition
of aggregated Aβ peptide in the brain is one of the major hallmarks
of Alzheimer’s disease. Using a combination of two structurally
different, but related, hypersensitive fluorescent amyloid markers,
LCOs, reporting on separate ultrastructural elements, we show that
conformational rearrangement occurs within Aβ plaques of transgenic
mouse models as the animals age. This important mechanistic insight
should aid the design and evaluation of experiments currently using
plaque load as readout
Evidence for Age-Dependent <i>in Vivo</i> Conformational Rearrangement within Aβ Amyloid Deposits
Deposition
of aggregated Aβ peptide in the brain is one of the major hallmarks
of Alzheimer’s disease. Using a combination of two structurally
different, but related, hypersensitive fluorescent amyloid markers,
LCOs, reporting on separate ultrastructural elements, we show that
conformational rearrangement occurs within Aβ plaques of transgenic
mouse models as the animals age. This important mechanistic insight
should aid the design and evaluation of experiments currently using
plaque load as readout