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. 2015 Jul 6;5:11951. doi: 10.1038/srep11951

Figure 3. Binding studies of VG16KRKP with LPS.

Figure 3

(A) Intrinsic tryptophan fluorescence emission spectra of VG16A or VG16KRKP in the absence and presence of LPS micelle. (B) Upper panel showing endothermic heat of reaction vs. time (minute) upon interaction of VG16KRKP with LPS micelle. The lower panel shows enthalpy change per mole of peptide injection vs. molar ratio (peptide:LPS) for VG16KRKP. In this experiment, 50 μM of LPS micelle was titrated against 200 μM of peptide, VG16KRKP. TEM images of LPS micelle (C) alone and (D) in the presence of VG16KRKP. Scale bar = 1 μm. (E) 31P NMR spectra of the phosphates of LPS micelle in presence of MnCl2 in free form and upon addition of increasing concentrations of VG16KRKP signifying the fragmentation of LPS micelles, as evident from the reduction in intensity.