Abstract
Carbon nanomaterials (CNMs), including carbon quantum dots (CQDs), have found widespread use in biomedical research due to their low toxicity, chemical tunability, and tailored applications. Yet, there exists a gap in our understanding of the molecular interactions between biomacromolecules and these novel carbon-centered platforms. Using gelatin-derived CQDs as a model CNM, we have examined the impact of this exemplar nanomaterial on apo-myoglobin (apo-Mb), an oxygen-storage protein. Intrinsic fluorescence measurements revealed that the CQDs induced conformational changes in the tertiary structure of native, partially unfolded, and unfolded states of apo-Mb. Titration with CQDs also resulted in significant changes in the secondary structural elements in both native (holo) and apo-Mb, as evidenced by the circular dichroism (CD) analyses. These changes suggested a transition from isolated helices to coiled-coils during the loss of the helical structure of the apo-protein. Infra-red spectroscopic data further underscored the interactions between the CQDs and the amide backbone of apo-myoglobin. Importantly, the CQDs-driven structural perturbations resulted in compromised heme binding to apo-myoglobin and, therefore, potentially can attenuate oxygen storage and diffusion. However, a cytotoxicity assay demonstrated the continued viability of neuroblastoma cells exposed to these carbon nanomaterials. These results, for the first time, provide a molecular roadmap of the interplay between carbon-based nanomaterial frameworks and biomacromolecules.