A comparison study of the interaction between β-lactoglobulin and retinol at two different conditions: spectroscopic and molecular modeling approaches

References

• Anfinsen, C. B. (1973). Principles that govern the folding of protein chains. Science, 181, 223–230.10.1126/science.181.4096.223
   PubMed Web of Science ®Google Scholar
• Baldwin, R. L. (1986). Temperature dependence of the hydrophobic interaction in protein folding. Proceedings of the National Academy of Sciences, 83, 8069–8072.10.1073/pnas.83.21.8069
   PubMed Web of Science ®Google Scholar
• Belatik, A., Hotchandani, S., Carpentier, R., & Tajmir-Riahi, H. A. (2012). Binding sites of retinol and retinoic acid with serum albumins. European Journal of Medicinal Chemistry, 48, 114–123.10.1016/j.ejmech.2011.12.002
   PubMed Web of Science ®Google Scholar
• Belatik, A., Kanakis, C. D., Hotchandani, S., Tarantilis, P. A., Polissiou, M. G., & Tajmir-Riahi, H. A. (2012). Locating the binding sites of retinol and retinoic acid with milk β-lactoglobulin. Journal of Biomolecular Structure & Dynamics, 30, 437–447.
   PubMed Web of Science ®Google Scholar
• Blanch, E. W., Hecht, L., & Barron, L. D. (1999). New insight into the pH-dependent conformational changes in bovine β-lactoglobulin from Raman optical activity. Protein Science, 8, 1362–1367.10.1110/(ISSN)1469-896X
   PubMed Web of Science ®Google Scholar
• 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, 636–646.10.1016/j.jcis.2006.02.049
   PubMed Web of Science ®Google Scholar
• Chamani, J., & Moosavi Movahedi, A. A. (2006). Effect of n-alkyl trimethylammonium bromides on folding and stability of alkaline and acid-denatured cytochrome c: A spectroscopic approach. Journal of Colloid and Interface Science, 297, 561–569.10.1016/j.jcis.2005.11.035
   PubMed Web of Science ®Google Scholar
• Chi, Z., Liu, R., Yang, B., & Zhang, H. (2010). Toxic interaction mechanism between oxytetracycline and bovine hemoglobin. Journal of Hazardous Materials, 180, 741–747.10.1016/j.jhazmat.2010.04.110
   PubMed Web of Science ®Google Scholar
• Dewick, P. M. (2009). Medicinal natural products (3rd ed.). New York, NY: Wiley.10.1002/9780470742761
   Google Scholar
• Ge, F., Chen, C., Liu, D., Han, B., Xiong, X., & Zhao, S. (2010). Study on the interaction between theasinesin and human serum albumin by fluorescence spectroscopy. Journal of Luminescence, 130, 168–173.10.1016/j.jlumin.2009.08.003
   Web of Science ®Google Scholar
• Godovac Zimmermann, J. (1988). The structural motif of ß-lactoglobulin and retinol-binding protein: A basic framework for binding and transport of small hydrophobic molecules? Trends in Biochemical Sciences, 13, 64–66.10.1016/0968-0004(88)90031-X
   PubMed Web of Science ®Google Scholar
• Hamada, D., Kuroda, Y., Tanaka, T., & Goto, Y. (1995). High helical propensity of the peptide fragments derived from beta-lactoglobulin, a predominantly beta-sheet protein. Journal of Molecular Biology, 254, 737–746.10.1006/jmbi.1995.0651
   PubMed Web of Science ®Google Scholar
• Hamada, D., Segawa, S., & Goto, Y. (1996). Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein. Nature Structural Biology, 3, 868–873.10.1038/nsb1096-868
   PubMedGoogle Scholar
• He, L., Wang, X., Liu, B., Wang, J., Sun, Y., Gao, E., & Xu, S. (2011). Study on the interaction between promethazine hydrochloride and bovine serum albumin by fluorescence spectroscopy. Journal of Luminescence, 131, 285–290.10.1016/j.jlumin.2010.10.014
   Web of Science ®Google Scholar
• He, Y., Wang, Y., Tang, L., Liu, H., Chen, W., Zheng, Z., & Zou, G. (2008). Binding of puerarin to human serum albumin: A spectroscopic analysis and molecular dockin. Journal of Fluorescence, 18, 433–442.10.1007/s10895-007-0283-0
   PubMed Web of Science ®Google Scholar
• Itzhaki, L. S., Otzen, D. E., & Fersht, A. R. (1995). The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding. Journal of Molecular Biology, 254, 260–288.10.1006/jmbi.1995.0616
   PubMed Web of Science ®Google Scholar
• Kerec, M., Bogataj, M., Mugerle, B., Gašperlin, M., & Mrhar, A. (2002). Mucoadhesion on pig vesical mucosa: influence of polycarbophil/calcium interactions. International Journal of Pharmaceutics, 241, 135–143.10.1016/S0378-5173(02)00231-4
   PubMed Web of Science ®Google Scholar
• Kontopidis, G., Holt, C., & Sawyer, L. (2004). Invited review: β-lactoglobulin: binding properties, structure, and function. Journal of Dairy Science, 87, 785–796.10.3168/jds.S0022-0302(04)73222-1
   PubMed Web of Science ®Google Scholar
• Kuwajima, K. (1989). The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins: Structure, Function, and Genetics, 6, 87–103.10.1002/(ISSN)1097-0134
   PubMed Web of Science ®Google Scholar
• Kuwata, K., Hoshino, M., Forge, V., Era, S., Goto, Y., & Batt, C. A. (1999). Solution structure and dynamics of bovine β-lactoglobulin A. Protein Science, 8, 2541–2545.
   PubMed Web of Science ®Google Scholar
• Ling, L., Pan, Q., Xi-Wang, Y., Wu-Song, G., & Shun-Xu, Z. (2011). Study on the binding equilibrium between surfactant FC95 and DNA by resonance light-scattering technique. Applied Surface Science, 257, 4547–4551.
   Web of Science ®Google Scholar
• Mihara, H., & Takahashi, Y. (1997). Engineering peptides and proteins that undergo α-to-β transitions. Current Opinion in Structural Biology, 7, 501–508.10.1016/S0959-440X(97)80113-3
   PubMed Web of Science ®Google Scholar
• Minor, D. L., & Kim, P. S. (1996). Context-dependent secondary structure formation of a designed protein sequence. Nature, 380, 730–734.
   PubMed Web of Science ®Google Scholar
• Mottonen, J., Strand, A., Symersky, J., Sweet, R. M., Danley, D., Geoghegan, K. F., Gerard, R. D., & Goldsmith, E. J. (1992). Structural basis of latency in plasminogen activator inhibitor-1. Nature, 355, 270–273.10.1038/355270a0
   PubMed Web of Science ®Google Scholar
• Myers, J. K., Nick Pace, C. N., & Martin Scholtz, J. M. (1995). Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding. Protein Science, 4, 2138–2148.10.1002/pro.v4:10
   PubMed Web of Science ®Google Scholar
• Pace, C. N. (1985). Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods in Enzymology, 131, 266–280.
   Google Scholar
• Perez, M. D., Diaz de Villegas, C., Sanchez, L., Arando, P., Ena, J. M., & Calvo, M. (1989). Interaction of fatty acids with B-lactoglobulin and albumin from Ruminant milk. Journal of Biochemistry, 106, 1094–1097.
   PubMed Web of Science ®Google Scholar
• Pervaiz, S., & Brew, K. (1985). Homology of beta-lactoglobulin, serum retinol-binding protein, and protein HC. Science, 228, 335–337.10.1126/science.2580349
   PubMed Web of Science ®Google Scholar
• Prieto, G., Sabin, J., Ruso, J. M., Gonzalez Perez, A., & Sarmiento, F. (2004). A study of the interaction between proteins and fully-fluorinated and fuly-hydrogenated surfactants by zeta potential measurements. Journal of Colloid and Interface Science, 249, 51–55.
   Google Scholar
• Prusiner, S. B. (1997). Prion diseases and the BSE crisis. Science, 278, 245–251.10.1126/science.278.5336.245
   PubMed Web of Science ®Google Scholar
• Raifen, R., Altman, Y., & Zadik, Z. (1996). Vitamin A levels and growth hormone axis. Hormone Research, 46, 279–281.10.1159/000185101
   PubMed Web of Science ®Google Scholar
• Sahihi, M., Bordbar, A. K., & Ghayeb, Y. (2011). Thermodynamic stability and retinol binding property of β-lactoglobulin in the presence of cationic surfactants. The Journal of Chemical Thermodynamics, 43, 1185–1191.10.1016/j.jct.2011.03.004
   Web of Science ®Google Scholar
• Tanford, C. (1970). Protein denaturation. C. Theoretical models for the mechanism of denaturation. Advances in Protein Chemistry, 24, 1–95.10.1016/S0065-3233(08)60241-7
   PubMedGoogle Scholar
• Uhrínová, S., Smith, M. H., Jameson, G. B., Uhrín, D., Sawyer, L., & Barlow, P. N. (2000). Structural changes accompanying pH-induced dissociation of the beta-Lactoglobulin dimer. Biochemistry, 39, 3565–3574.10.1021/bi992629o
   PubMed Web of Science ®Google Scholar
• Wang, T., Zhao, Z., Wei, B., Zhang, L., & Ji, L. (2010). Spectroscopic investigations on the binding of dibazol to bovine serum albumin. Journal of Molecular Structure, 970, 128–133.10.1016/j.molstruc.2010.02.061
   Web of Science ®Google Scholar
• Wu, S., Xue, H., Sheng, Y., Li, W. W., & Bao, X. (1996). Fluorescence red-edge-excitation effects of human serum albumin. Acta Biochemica et Biophysica Sinica, 28, 418–423.
   Web of Science ®Google Scholar
• Xiahui, Z., & Chengzhi, H. (2007). Polarized synchronous light scattering characterization of the interaction of proteins with sodium dodecyl sulfonate. Chinese Science Bulletin, 52, 456–460.
   Web of Science ®Google Scholar
• Yang, M. C., Guan, H. H., Liu, M. Y., Lin, Y. H., Yang, J. M., Chen, W. L., Chen, C. J., & Mao, S. J. (2008). Crystal structure of a secondary vitamin D3 binding site of milk β-lactoglobulin. Proteins, 71, 1197–1210.
   PubMed Web of Science ®Google Scholar
• Zhang, H., Hassanali, A. A., Shin, Y. K., Kinght, C., & Singer, S. J. (2005). The water-amorphous silica interface: Analysis of the Stern layer and surface conduction. The Journal of Chemical Physics, 134, 24705–24713.
   Web of Science ®Google Scholar