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www.nature.com/scientificreports/ Figure 5. HPLC/UV elution profiles of HSA with MG mixtures with or without AgNP after 6 days of incubation. (A) Native HSA, (B) HSA–MG mixtures without AgNP, (C) HSA–MG with AgNP (0.09 mM), (D) HSA–MG with AgNP (0.185 mM), and (E) HSA–MG with AgNP (0.27 mM). All readings were taken in triplicate. UV Absorbance was measured at 280 nm. Figure 6. (A) CD profiles of HSA–MG with and without various concentrations of AgNPs incubated at 37 °C for 6 days. All samples were appropriately diluted with deionized water before obtaining the CD profile. Repeat studies revealed no significant difference in CD profiles. (B) FTIR profiles of Amide I and Amide II bands of HSA and MG mixtures with and without AgNPs after 6 days of incubation. All readings were taken in triplicate. divergence at 208 and 222 nm, indicating that reduction of the α-helical content was due to modification of the HSA secondary structure by MG. When compared to CD measurements of the MG-HSA mixture, more α-helical content of the protein was retained in mixtures with increasing levels of AgNPs, indicating that the extent of HSA modification in the presence of AgNPs (0.09, 0.18 and 0.27 mM) was reduced (Fig. 6A). These profiles showed more α-helix content remained in the HSA secondary structure when incubated with 0.18 and 0.27 mM of AgNPs than in mixtures with 0.09 mM of AgNP, indicating that the diminution of structural modification of HSA is a concentration dependent phenomenon. The CD results clearly indicate that AgNPs have a positive effect on α-helixes and help retain the secondary structure of HSA. The Far-UV CD results were further supported by FT-IR spectroscopy. FTIR spectra of MG-HSA mixtures incubated for 6 days with AgNP were analyzed in the range of 1400–1700 cm−1 (Fig. 5B). Secondary structure analysis was based on Amide-I and Amide-II bands within the 1400–2000 cm−1 region after subtraction of the background absorption. In the IR region, the amide I peak position occurs in the 1600–1700 cm−1 region (mainly C=O stretch), while the amide II band was located from 1500–1600 cm−1 (C–N stretch coupled with N–H bend- ing mode), representing the amount of carbonyl and amino bonds in side chains of amino acid residues of the Scientific RepoRts | 6:20414 | DOI: 10.1038/srep20414 7PDF Image | Green synthesis of silver nanoparticles inhibitory effects on AGEs
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