Interaction between Luteinizing Hormone Releasing Hormone and GM1 Doped Cholesterol/Sphingomyelin Vesicles: A Spectroscopic Study

Zarrin Shahzadi, Chaitali Mukhopadhyay*

Fig. A1 Electron micrographs of (A) CHOL/SM vesicles (B) GM1 doped CHOL/SM vesicles at pH 7.4 and 25 C.

Fig. A2 Representative data for SternVolmer analysis of acrylamide (2M) quenching of LHRH (a) in buffer (b) CHOL/SM vesicles (c) GM1 doped CHOL/SM vesicles. The excitation wavelength was 295 nm and emission was monitored as in Fig. 2. (peptide: vesicles = 1:100 mol/mol).

Fig. A3 Representative data for SternVolmer analysis of iodide (2M) quenching of LHRH (a) in buffer (b) CHOL/SM vesicles (c) GM1 doped CHOL/SM vesicles. The excitation wavelength was 295 nm and emission was monitored as in Fig. 2. (peptide: vesicles = 1:100 mol/mol).

Fig. A4 Double reciprocal plot of 1/F against 1/[vesicles] to evaluate the binding anity constant Ka of peptide LHRH with CHOL/SM and GM1 doped CHOL/SM vesicles in a 20 mM phosphate buer, pH 7.4 at 298 K. The peptide concentration was kept fixed at 5 106 M and vesicles concentrations were varied from 0 to 60 105 M.