Effect of chain length on the interactions of sodium N-alkyl prolinates with bovine serum albumin: a spectroscopic investigation and molecular docking simulations
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The interaction of anionic surfactants with serum albumin has emerged as an important area of research and is considered as a model for gaining fundamental insight into surfactant-protein binding, which is useful in both chemical and biological applications. This study involves the interactions of three synthesized proline-based anionic surfactants of varying chain lengths (C8, C10, and C12) with bovine serum albumin (BSA) using different techniques, including fluorescence, 1H NMR, and FT-IR spectroscopy. The study indicated that the binding of the proline surfactants with BSA followed a static quenching process, with an increase in binding ability upon increasing chain length. FT-IR studies revealed a change in the secondary structure of BSA upon binding with the proline surfactant, while 1H NMR investigations indicated the proximity of the long alkyl chain of the surfactant with tryptophan residues of BSA. Molecular docking studies performed on the three proline surfactants with BSA revealed that the surfactants were able to bind in the vicinity of both tryptophan residues (Trp-213 and Trp-134) with an increase in the free energy of binding while increasing the chain length from C8 to C12. Therefore, this study provided a whole view about the interaction of BSA with anionic proline derived surfactants, which can be used as potential ingredients in pharmaceutical products.
KeywordsAnionic surfactants Proline Bovine serum albumin Fluorescence quenching Molecular docking
Computations were performed using facilities provided by the University of Cape Town’s ICTS High-Performance Computing Team: http://hpc.uct.ac.za. One of the authors is thankful to the tertiary education commission for the grant of scholarship scheme.
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Conflict of interest
The authors declare that there is no conflict of interests.
- 3.Moriyama Y, Ohta D, Hachiya K, Mitsui Y, Takeda K (1996) Fluorescence behavior of tryptophan residues of bovine and human serum albumins in ionic surfactant solutions: a comparative study of the two and one tryptophan(s) of bovine and human albumins. J Protein Chem 15(3):265–272. https://doi.org/10.1007/BF01887115CrossRefGoogle Scholar
- 10.Mishra M, Muthuprasanna P, Prabha KS, Rani PS, Babu IAS, Chandiran IS, Arunachalam G, Shalini S (2009) Basics and potential applications of surfactants: a review. Int J Pharm Tech Res 1:1354–1365Google Scholar
- 14.Minic S, Stanic-Vucinic D, Radomirovic M, Radibratovic M, Milcic M, Nikolic M, Velickovic TC (2018) Characterisation and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. Food Chem 239:1090–1099. https://doi.org/10.1016/j.foodchem.2017.07.066CrossRefGoogle Scholar
- 18.Ohta A, Toda K, Morimoto Y, Asakawa T, Miyagishi S (2008) Effect of the side chain of N-acyl amino acid surfactants on micelle formation: an isothermal titration calorimetry study. Colloids Surf A Physicochem Eng Asp 317(1-3):316–322. https://doi.org/10.1016/j.colsurfa.2007.10.028CrossRefGoogle Scholar
- 25.Frisch MJ, Trucks GW, Schlegel HB, Scuseria GE, Robb MA, Cheeseman JR, Scalmani G, Barone V, Mennucci B, Petersson GA, Nakatsuji H, Caricato M, Li X, Hratchian HP, Izmaylov AF, Bloino J, Zheng G, Sonnenberg JL, Hada M, Ehara M, Toyota K, Fukuda R, Hasegawa J, Ishida M, Nakajima T, Honda Y, Kitao O, Nakai H, Vreven T, Montgomery Jr JA, Peralta JE, Ogliaro F, Bearpark M, Heyd JJ, Brothers E, Kudin KN, Staroverov VN, Kobayashi R, Normand J, Raghavachari K, Rendell A, Burant JC, Iyengar SS, Tomasi J, Cossi M, Rega N, Millam JM, Klene M, Knox JE, Cross JB, Bakken V, Adamo C, Jaramillo J, Gomperts R, Stratmann RE, Yazyev O, Austin AJ, Cammi R, Pomelli C, Ochterski JW, Martin RL, Morokuma K, Zakrzewski VG, Voth GA, Salvador P, Dannenberg JJ, Dapprich S, Daniels AD, Farkas Ö, Foresman JB, Ortiz JV, Cioslowski J, Fox DJ (2009) Gaussian 09, Revision D.01 Gaussian, Inc., Wallingford CTGoogle Scholar
- 30.Laskowski RA, Swindells MB (2011) Ligplot+: multiple ligand-protein interaction diagrams for drug discovery. J Chem Inf Model 51:2778–2786Google Scholar
- 31.Baker NA, Sept D, Joseph S, Holst MJ and McCammon JA (2001) Electrostatics of nanosystems: application to microtubules and the ribosome. Proc Natl Acad Sci USA 98(18):10037–10041Google Scholar
- 45.Vishvakarma VK, Patel K, Kumari K, Singh P (2017) Interaction between bovine serum albumin and gemini surfactants molecular docking characterisation. Inf Sci Lett 6:33–38Google Scholar