“…8, at pH 7.4 BSA molecules bear negative charge surface with potential of about −6.86 mV while −45.9, −34.8, and −27.0 mV for <10, 10-20 and 20-40 nm CNTs, respectively. Based on the fact that carboxylized CNTs interact with proteins through mainly electrostatic forces [23,24], it is assumed that the hydrophobic cavity of BSA, which is positive-charged at pH 7.4, is the main site to interact with the negative-charged CNTs. Trp-212, which originally buried in the hydrophobic cavity of BSA, has high possibility of coming into contact with CNTs, causing synchronous fluorescence spectra shifts at = 60 nm.…”