title: Comprehensive spectroscopic studies on the interaction of biomolecules with surfactant detached multi-walled carbon nanotubes.
abstract: This paper investigates the interaction of ten diverse biomolecules with surfactant detached Multi-Walled Carbon Nanotubes (MWCNTs) using multiple spectroscopic methods. Declining fluorescence intensity of biomolecules in combination with the hyperchromic effect in UV-Visible spectra confirmed the existence of the ground state complex formation. Quenching mechanism remains static and non-fluorescent. 3D spectral data of biomolecules suggested the possibilities of disturbances to the aromatic microenvironment of tryptophan and tyrosine residues arising out of CNTs interaction. Amide band Shifts corresponding to the secondary structure of biomolecules were observed in the of FTIR and FT-Raman spectra. In addition, there exists an increased Raman intensity of tryptophan residues of biomolecules upon interaction with CNTs. Hence, the binding of the aromatic structures of CNTs with the aromatic amino acid residues, in a particular, tryptophan was evidenced. Far UV Circular spectra have showed the loss of alpha-helical contents in biomolecules upon interaction with CNTs. Near UV CD spectra confirmed the alterations in the tryptophan positions of the peptide backbone. Hence, our results have demonstrated that the interaction of biomolecules with OH-MWCNTs would involve binding cum structural changes and alteration to their aromatic micro-environment.
authors.affiliation: Centre for Nanobiotechnology, VIT University, Vellore -632014, Tamil Nadu, India.
authors.forename: Gajalakshmi
authors.initials: G
authors.lastname: Sekar
authors.affiliation: Centre for Nanobiotechnology, VIT University, Vellore -632014, Tamil Nadu, India.
authors.forename: Amitava
authors.initials: A
authors.lastname: Mukherjee
authors.affiliation: Centre for Nanobiotechnology, VIT University, Vellore -632014, Tamil Nadu, India. Electronic address: nchandra40@hotmail.com.
authors.forename: Natarajan
authors.initials: N
authors.lastname: Chandrasekaran
mesh_terms: D000818:Animals; D006454:Hemoglobins / Q000737:chemistry*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D009113:Muramidase / Q000737:chemistry*; D037742:Nanotubes, Carbon / Q000737:chemistry*; D011136:Polysorbates / Q000737:chemistry; D017433:Protein Structure, Secondary; D012709:Serum Albumin / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared; D013059:Spectrum Analysis, Raman; D013501:Surface-Active Agents / Q000737:chemistry; D014364:Tryptophan / Q000737:chemistry; D014443:Tyrosine / Q000737:chemistry; D000516:alpha-Amylases / Q000737:chemistry*
chemical_list: D006454:Hemoglobins; D037742:Nanotubes, Carbon; D011136:Polysorbates; D012709:Serum Albumin; D013501:Surface-Active Agents; D014443:Tyrosine; D014364:Tryptophan; D000516:alpha-Amylases; D009113:Muramidase
keywords: Aromatic; Conformational; Fluorescence; Hydrophobicity; Secondary