Cytochrome C, an
evolutionarily conserved protein, plays
pivotal
roles in cellular respiration and apoptosis. Understanding its molecular
intricacies is essential for both academic inquiry and potential biomedical
applications. This study introduces an advanced single-molecule surface-enhanced
Raman scattering (SM-SERS) system based on DNA origami nanoantennas
(DONAs), optimized to provide unparalleled insights into protein structure
and interactions. Our system effectively detects shifts in the Amide
III band, thereby elucidating protein dynamics and conformational
changes. Additionally, the system permits concurrent observations
of oxidation processes and Amide bands, offering an integrated view
of protein structural and chemical modifications. Notably, our approach
diverges from traditional SM-SERS techniques by de-emphasizing resonance
conditions for SERS excitation, aiming to mitigate challenges like
peak oversaturation. Our findings underscore the capability of our
DONAs to illuminate single-molecule behaviors, even within aggregate
systems, providing clarity on molecular interactions and behaviors.