The FTIR spectrum (Figure 1) confirmed the presence of amide A, amide I, and amide II bands at 3302.09 cm-1, 1661.14 cm-1 and 1530.14 cm-1, respectively, in pure BSA. The spectra of the BSA-Au NCs also showed three prominent bands corresponding to amide A, amide I, and amide II of the dipeptide at 3297.41 cm-1, 1658.18 cm-1 and 1531.34 cm-1, respectively, which clearly demonstrated the dipeptide presence on the Au cluster surfaces. Additionally, a band at 2961.20 cm-1 corresponding to C-H vibrations modes observed in pure BSA can also be observed in BSA-Au NCs.

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