Investigation of Few-Layer Graphene Ubiquitin Interactions Optical Spectroscopy #WorldResearchAwards


Introduction

Understanding protein–nanoparticle interactions is a rapidly advancing area of research due to its profound implications in biomedicine, biosensing, and nanotechnology. Among various nanomaterials, few-layer graphene (FLG) has attracted significant attention because of its unique physicochemical properties, high surface area, and biocompatibility. Proteins interacting with nanomaterials often undergo conformational changes that can alter their biological function. Ubiquitin, a small yet functionally critical protein involved in protein degradation, signaling, and cellular regulation, serves as an excellent model to study these interactions. Investigating FLG–ubiquitin complexes provides valuable molecular-level insight into how nanomaterials can be safely integrated into biological systems without compromising protein structure or function.

Rationale for Studying FLG–Ubiquitin Interactions

Ubiquitin’s compact structure, well-defined secondary elements, and biological importance make it a suitable probe for nanoparticle interaction studies. FLG prepared via water-based exfoliation offers a clean and biologically relevant platform, free from chemical contaminants that might otherwise influence protein behavior. Studying FLG–ubiquitin complexes helps clarify whether graphene-based nanomaterials can interact with proteins in a controlled and non-destructive manner. Such understanding is essential for designing graphene-enabled biomedical devices, drug delivery systems, and diagnostic tools.

Optical Spectroscopic Approaches

A combination of optical spectroscopic techniques—Raman, FT-IR, UV-Vis, and circular dichroism (CD)—was employed to probe FLG–ubiquitin interactions at the molecular level. Raman spectroscopy provided structural confirmation of FLG, while FT-IR and CD spectroscopy offered insights into protein secondary structure. UV-Vis spectroscopy enabled the detection of micro-environmental changes around aromatic residues. Together, these complementary techniques allowed a comprehensive assessment of both graphene characteristics and protein structural integrity upon complex formation.

Secondary Structure Preservation of Ubiquitin

FT-IR and CD analyses consistently demonstrated that ubiquitin retains its native secondary structure after interaction with FLG. Notably, no formation of disordered structures was observed, indicating that FLG binding does not denature the protein. Quantitative CDPro estimations aligned well with ATR FT-IR data, confirming the stability of α-helix and β-sheet components. These findings are significant, as preservation of protein structure is a key requirement for biomedical applications involving nanomaterials.

Spectroscopic Evidence of Micro-Environmental Changes

UV-Vis spectroscopy revealed a distinct blue (hypsochromic) shift, attributed to changes in the local environment of ubiquitin’s aromatic residues—one tyrosine and two phenylalanines. These residues act as sensitive reporters of nanoparticle interaction, indicating subtle rearrangements in the protein’s micro-environment without global unfolding. CD spectra further showed alterations in protein chirality, suggesting surface-induced conformational adjustments rather than structural disruption.

Implications for Biomedicine and Nanotechnology

The concentration-dependent spectroscopic trends observed in this study highlight controlled and stable FLG–protein interactions. By preserving ubiquitin’s overall structure while inducing measurable yet non-destructive micro-environmental changes, FLG demonstrates strong potential for safe biological integration. These findings support the future use of few-layer graphene in biomedical and nanotechnological applications, including biosensors, therapeutic platforms, and protein–nanomaterial hybrid systems for advanced research and clinical innovation.

Global Particle Physics Excellence Awards


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