Carbon nanotubes (CNTs) with unique and outstanding properties were expected to revolutionize various aspects of the biomedical sector. Interaction studies of proteins with functionalized CNTs would shed light on their toxicological aspects upon entering the human body. Hyperchromicity of the UV-Visible spectra and declining fluorescence potential of HSA on interaction with CNTs suggested ground state complex to exist between them. Synchronous and 3D spectral features of CNT-HSA system proposed their possible binding site to occur nearby Trp and Tyr residues. FTIR and FT-Raman spectra showed a shift in the amide band region that proportionate the possible alteration to occur in the alpha-helical structures. CD far and near spectra showed loss of alpha-helical structures and shift in the Trp position of the polypeptide backbone. CNT's UV and FTIR band showed shift on interaction with HSA, which conveys the possible aggregation of CNTs in the presence of protein. The promoting role of CNTs against HSA fibril formation has been confirmed by spectroscopic and microscopic evaluations. Secondary conformational changes, besides the existence of increased beta-sheet structures of HSA amyloid fibrils, remain similar to the amyloid behavior of Prion protein. Hence, HSA fibril-CNT interface predominates the possible mechanism for several amyloid-related disorders concerning their toxic accumulations in the body. © 2016 Elsevier B.V. All rights reserved.