NDLI: Study on the Effects of Biologically Active Amino Acids on the Micellization of Anionic Surfactant Sodium Dodecyl Sulfate (SDS) at Different Temperatures

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Study on the Effects of Biologically Active Amino Acids on the Micellization of Anionic Surfactant Sodium Dodecyl Sulfate (SDS) at Different Temperatures

Content Provider	MDPI
Author	Elarbi, Fatima M. Ettarhouni, Zaineb O. Abdussalam-Mohammed, Wanisa Mezoughi, Aysha B.
Copyright Year	2022
Abstract	The micellar properties of the anionic surfactant, sodium dodecyl sulfate (SDS) are modified by the biologically active amino acids. Amino acids (AAs) have experienced a variety of interactions and are proposed to influence SDS micelles due to their nominated hydrophobic interactions. The present study determines the critical micellar concentration (CMC) of SDS in aqueous solutions as well as in amino aqueous solutions. Three amino acids (glutamic acid, histidine, and tryptophan) are considered here. The conductometric measurements were carried out using a wide range of SDS concentrations at different temperatures. Surface tension experiments have also been applied to estimate many surface parameters including surface excess concentration (Γ_max), surface occupied area per surfactant molecule (A_min), surface tension at CMC (γ_cmc), surface pressure at CMC (Π_cmc) and Gibbs free energy of adsorption ( $∆ G_{a d s}^{°}$ ), enthalpy $∆ H_{m}^{°}$ and the critical packing parameter (CPP). Interestingly, CMC values of SDS in water and in aqueous amino acids estimated by the surface tension method are comparable with the corresponding values obtained by the conductance method. The thermodynamic parameters of SDS micellization were also evaluated in both presence and absence of AAs. The additives of AAs work to reduce the CMC values, as well as the SDS thermodynamic parameters. This reduction is highly dependent on the hydrophobicity of the AA side chain. Negative values of $∆ G_{m}^{°}$ , $∆ H_{m}^{°}$ elucidate that micellization of SDS in the presence of amino acids is thermodynamically spontaneous and exothermic. The outcomes here might be utilized for pharmaceutical applications to stabilize proteins and inhibit protein aggregation.
Ending Page	155
Page Count	10
Starting Page	146
e-ISSN	26248549
DOI	10.3390/chemistry4010013
Journal	Chemistry
Issue Number	1
Volume Number	4
Language	English
Publisher	MDPI
Publisher Date	2022-03-11
Access Restriction	Open
Subject Keyword	Chemistry Atomic, Molecular and Chemical Physics Anionic Surfactant Amino Acids Sidechains Conductivity Surface Tension Micellization Protein
Content Type	Text
Resource Type	Article

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