References
- Bai, Z., Liu, Y., Zhang, P., Guo, J., Ma, Y., Yun, X., & Zhang, F. (2015). Fluorescence resonance energy transfer between bovine serum albumin and fluoresceinamine. Luminescence, 31(3), 688–693. doi:10.1002/bio.3012
- Chamani, J. (2006). Comparison of the conformational stability of the non-native α-helical intermediate of thiol-modified β-lactoglobulin upon interaction with sodium n-alkyl sulfates at two different pH. Journal of Colloid and Interface Science, 299(2), 636–646. doi:10.1016/j.jcis.2006.02.049
- Chamani, J., Moosavi-Movahedi, A. A., Rajabi, O., Gharanfoli, M., Momen-Heravi, M., Hakimelahi, G. H., … Varasteh, A. R. (2006). Cooperative α-helix formation of β-lactoglobulin induced by sodium n-alkyl sulfates. Journal of Colloid and Interface Science, 293(1), 52–60. doi:10.1016/j.jcis.2005.06.015
- Chavoshpour-Natanzi, Z., Sahihi, M., & Gharaghani, S. (2017). Structural stability of β-lactoglobulin in the presence of cetylpyridinum bromide: Spectroscopic and molecular docking studies. Journal of Biomolecular Structure and Dynamics, 1–8. doi:10.1080/07391102.2017.1297254
- da Silva, C. M., da Silva, D. L., Modolo, L. V., Alves, R. B., de Resende, M. A., Martins, C. V., & de Fátima, Â. (2011). Schiff bases: A short review of their antimicrobial activities. Journal of Advanced Research, 2(1), 1–8. doi:10.1016/j.jare.2010.05.004
- Hosainzadeh, A., Gharanfoli, M., Saberi, M. R., & Chamani, J. (2012). Probing the interaction of human serum albumin with bilirubin in the presence of aspirin by multi-spectroscopic, molecular modeling and zeta potential techniques: Insight on binary and ternary systems. Journal of Biomolecular Structure and Dynamics, 29(5), 1013–1050. doi:10.1080/073911012010525029
- Khorsand Ahmadi, S., Mahmoodian Moghadam, M., Mokaberi, P., Reza Saberi, M., & Chamani, J. (2015). A comparison study of the interaction between β-lactoglobulin and retinol at two different conditions: Spectroscopic and molecular modeling approaches. Journal of Biomolecular Structure and Dynamics, 33(9), 1880–1898. doi:10.1080/07391102.2014.977351
- Khorshidifard, M., Rudbari, H. A., Askari, B., Sahihi, M., Farsani, M. R., Jalilian, F., & Bruno, G. (2015). Cobalt (II), copper (II), zinc (II) and palladium (II) Schiff base complexes: Synthesis, characterization and catalytic performance in selective oxidation of sulfides using hydrogen peroxide under solvent-free conditions. Polyhedron, 95, 1–13. doi:10.1016/j.poly.2015.03.041
- Marouzi, S., Rad, A. S., Beigoli, S., Baghaee, P. T., Darban, R. A., & Chamani, J. (2017). Study on effect of lomefloxacin on human holo-transferrin in the presence of essential and nonessential amino acids: Spectroscopic and molecular modeling approaches. International Journal of Biological Macromolecules, 97, 688–699. doi:10.1016/j.ijbiomac.2017.01.047
- Moghaddam, M. M., Pirouzi, M., Saberi, M. R., & Chamani, J. (2014). Comparison of the binding behavior of FCCP with HSA and HTF as determined by spectroscopic and molecular modeling techniques. Luminescence, 29(1), 314–331. doi:10.1002/bio.2546
- Omidvar, Z., Asoodeh, A., & Chamani, J. (2013). Studies on the antagonistic behavior between cyclophosphamide hydrochloride and aspirin with human serum albumin: Time-resolved fluorescence spectroscopy and isothermal titration calorimetry. Journal of Solution Chemistry, 42(5), 1005–1017. doi:10.1007/s10953-013-0009-7
- Omidvar, Z., Parivar, K., Sanee, H., Amiri-Tehranizadeh, Z., Baratian, A., Saberi, M. R., … Chamani, J. (2011). Investigations with spectroscopy, zeta potential and molecular modeling of the non-cooperative behaviour between cyclophosphamide hydrochloride and aspirin upon interaction with human serum albumin: Binary and ternary systems from the view point of multi-drug therapy. Journal of Biomolecular Structure and Dynamics, 29(4), 181–206. doi:10.1080/07391102.2011.10507382
- Papiz, M., Sawyer, L., Eliopoulos, E., North, A., Findlay, J., Sivaprasadarao, R., & Kraulis, P. (1986). The structure of b-lactoglobulin and its similarity to plasma retinol-binding protein. Nature, 324(6095), 383–385. doi:10.1038/324383a0
- Reddy, I. M., Kella, N. K., & Kinsella, J. E. (1988). Structural and conformational basis of the resistance of. beta.-lactoglobulin to peptic and chymotryptic digestion. Journal of Agricultural and Food Chemistry, 36(4), 737–741. doi:10.1021/jf00082a015
- Ross, P. D., & Subramanian, S. (1981). Thermodynamics of protein association reactions: Forces contributing to stability. Biochemistry, 20(11), 3096–3102. doi:10.1021/bi00514a017