Figure 2 UV–vis spectra of pure BSA, BSA-AuCl 4 − , and BSA-Au nanocomplexes. (a) Low magnification and (b) high magnification. The interaction between BSA and gold nanocomplexes has also been investigated using a circular dichroism (CD) spectropolarimeter. Figure 3 shows the CD spectra of pure BSA, BSA-AuCl4 −, and BSA-Au nanocomplexes.

The pure BSA showed a positive absorption band at 190 nm and two negative absorption bands at 209 and 222 nm [10]. When a certain amount of AuCl4 − was added into the pure BSA solutions, the bands at 190, 209, and 222 nm almost disappeared, which can be attributed to the strong chelation between the AuCl4 − ions and BSA molecules. The result indicated that the peptide TGF-beta inhibitor chain in the α-helix structure of BSA extended and became a linear primary structure. Along with the extension of the peptide chain, LY3023414 in vitro more and more aromatic amino acid residues were exposed from the interior of BSA, so the changes were also very obvious in the UV spectra. After the formation of BSA-Au nanocomplexes, the positive peak at 190 nm ascended and the two negative peaks at 209 and 222 nm declined, which suggested that the conformation of the secondary structures of BSA was partially recuperative.

The above results are in accord with the UV–vis spectra. Figure 3 CD spectra of pure BSA, BSA-AuCl 4 − , and BSA-Au nanocomplexes. To further investigate the interaction between BSA and gold nanocomplexes, fluorescence spectra were recorded on a Hitachih FL-4600 spectrofluorimeter (Hitachi Ltd., Tokyo, Japan). For protein with intrinsic fluorescence, more specific local information can be obtained by selectively exciting the tryptophan (Trp) residues. A BSA molecule possesses two Trp residues [21]. One is located on the bottom of hydrophobic pocket in domain II (Trp-213), while another is located on the surface of the molecule in domain I (Trp-134) [22]. Figure 4a shows the www.selleckchem.com/products/BI-2536.html emission spectra of tryptophan residues of pure BSA, BSA-AuCl4

−, and BSA-Au nanocomplexes. The choice of 280 nm as the excitation wavelength was to avoid the MYO10 contribution from tyrosine residues. As shown, the fluorescence intensity was found to decrease with the addition of the AuCl4 − ions and the formation of gold nanocomplexes, while the emission maximum shifted from 350 to 380 nm (BSA-AuCl4 −) and 370 nm (BSA-Au nanocomplexes). These different fluorescent characteristics actually reflected different conformational states of BSA, which agree with CD spectra. The results also indicated that there are strong interactions between the Trp residues of BSA and AuCl4 −/gold nanocomplexes. The as-prepared BSA-Au nanocomplexes in different concentrations of BSA solution have a similar photoemission peak at approximately 588 nm, which implied that the nanocomplexes can be used as fluorescence probes for cell imaging. Figure 4 Fluorescence emission spectra.