Since the applications of CNTs are rapidly increasing in the biomedical field, their interaction studies with proteins structural and functional aspects remains significant for elucidating their biocompatibility in vivo. Hence, in this work, we have probed the binding parameters of almost ten diverse biomolecules with the tween 20 dispersed Single-Walled Carbon Nanotubes (SWCNTs) using spectroscopic techniques. Hyperchromicity of the biomolecules UV-Visible spectra and declining intrinsic fluorescence in the presence of mounting concentrations of SWCNTs confirmed complex formation in a ground state with static quenching mechanism. Synchronous spectra of biomolecules observed with the Δλ shift fixed at 15 and 60 nm convinced the binding probability of CNTs with biomolecules occurring close to that of tyrosine and the tryptophan residues. Similarly, 3D scan spectra of biomolecules contour and bird's eye view plot tend to show variation in the intensity and the Excitation: Emission pattern upon interaction with that of SWCNTs. Also, the significant losses of secondary structural elements of biomolecules upon binding with CNTs surface evidenced binding induced conformational changes. UV-Visible spectra of SWCNTs upon interaction with mounting concentrations of biomolecules showed a gradual decrease in its Plasmon band that governs Proteins-CNTs corona formation occurring due to the aggregation of biomolecules on the surface of CNTs. The threat behind the amyloid fibrillation is the aggregation of biomolecules leading to their misfolding and disordered protein synthesis. Hence, the binding induced conformational changes in the biomolecules upon interaction with SWCNTs must be understood in a detailed manner. © 2017 American Scientific Publishers.