Current trends in protein-surfactant interactions: A review

Fatma, Ishrat; Sharma, Vivek; Thakur, Ramesh; Kumar, Ashish

doi:10.1016/j.molliq.2021.117344

Cited by 31 publications

(15 citation statements)

References 162 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Research on protein–surfactant interactions has a long history owing to their importance in the pharmaceutical, food, and cosmetics industries. − Sodium dodecyl sulfate (SDS), an anionic detergent known to unfold globular proteins, is most commonly used in these studies as a representative surfactant. ,,, …”

Section: Introductionmentioning

confidence: 99%

Circular Dichroism Spectra of α-Chymotrypsin–SDS Solutions Depend on the Procedure of Their Preparation

et al. 2022

View full text Add to dashboard Cite

We recorded the far- and near-UV circular dichroism (CD) spectra of solutions of α-chymotrypsin and sodium dodecyl sulfate (SDS) with the final surfactant concentration significantly above the critical micellization concentration. Solutions were prepared using three different procedures. The reference procedure was to mix the chymotrypsin solution with the SDS solution once, immediately achieving the final SDS concentration. In alternative procedures, the protein solutions initially contained some SDS and were mixed with pure SDS solutions at a concentration to provide the same final surfactant as the reference mixing. We demonstrate that the supplementation to the selected final concentration of SDS of the pure chymotrypsin solution leads to different CD spectra than the supplementation to this final concentration of SDS in the chymotrypsin solution containing a small concentration of a few millimolar SDS. These differences disappear when the initial concentration of SDS in the protein solution, which we then supplement to the indicated final concentration, is higher. This suggests the irreversibility of the processes caused by the addition of SDS to chymotrypsin and the influence of the initial amount of this surfactant on the processes occurring with its further addition to the solution. For quantitative analysis of far-UV CD spectra in terms of populations of protein secondary structure elements, we used four well-established software packages. All programs consistently indicate that the observed differences in the far-UV CD spectra can be explained by the differences in the increase in the population of helical forms in chymotrypsin under the influence of SDS.

show abstract

Section: Introductionmentioning

confidence: 99%

Circular Dichroism Spectra of α-Chymotrypsin–SDS Solutions Depend on the Procedure of Their Preparation

et al. 2022

View full text Add to dashboard Cite

show abstract

“…Essentially, the self-aggregation study of mixed surfactant–PE compositions is necessary for a comprehensive description of their solution behavior and functional activity. The knowledge gained can provide a better understanding of optimizing the composition and properties of nanocontainers based on surfactants and PEs; The systems based on surfactant and natural PE are of great importance, e.g., the interaction of cationic surfactants with globular proteins-albumins-is widely studied due to the bioapplication perspective [ 33 , 34 , 35 ]. Albumins are blood transport proteins and have unique properties (commercial availability, water solubility, biodegradability, biogenicity, and ability to accumulate in tumor tissues), which makes them promising candidates for the development of protein-based nanocontainers [ 36 , 37 ].…”

Section: Introductionmentioning

confidence: 99%

“…Albumins are blood transport proteins and have unique properties (commercial availability, water solubility, biodegradability, biogenicity, and ability to accumulate in tumor tissues), which makes them promising candidates for the development of protein-based nanocontainers [ 36 , 37 ]. Complexation involving cationic surfactant–protein systems is of considerable interest since the interaction of proteins with amphiphilic molecules can lead to compaction or unfolding of the proteins, which is an important property for medicine and pharmacology [ 33 ]; Human serum albumin (HSA) is one of the most important plasma proteins. It consists of 585 amino acid residues with three α-helical domains, stabilized by disulfide bonds [ 36 , 38 ].…”

Section: Introductionmentioning

confidence: 99%

Role of Polyanions and Surfactant Head Group in the Formation of Polymer–Colloid Nanocontainers

et al. 2023

View full text Add to dashboard Cite

Objectives. This study was aimed at the investigation of the supramolecular systems based on cationic surfactants bearing cyclic head groups (imidazolium and pyrrolidinium) and polyanions (polyacrylic acid (PAA) and human serum albumin (HSA)), and factors governing their structural behavior to create functional nanosystems with controlled properties. Research hypothesis. Mixed PE–surfactant complexes based on oppositely charged species are characterized by multifactor behavior strongly affected by the nature of both components. It was expected that the transition from a single surfactant solution to an admixture with PE might provide synergetic effects on structural characteristics and functional activity. To test this assumption, the concentration thresholds of aggregation, dimensional and charge characteristics, and solubilization capacity of amphiphiles in the presence of PEs have been determined by tensiometry, fluorescence and UV-visible spectroscopy, and dynamic and electrophoretic light scattering. Results. The formation of mixed surfactant–PAA aggregates with a hydrodynamic diameter of 100–180 nm has been shown. Polyanion additives led to a decrease in the critical micelle concentration of surfactants by two orders of magnitude (from 1 mM to 0.01 mM). A gradual increase in the zeta potential of HAS–surfactant systems from negative to positive value indicates that the electrostatic mechanism contributes to the binding of components. Additionally, 3D and conventional fluorescence spectroscopy showed that imidazolium surfactant had little effect on HSA conformation, and component binding occurs due to hydrogen bonding and Van der Waals interactions through the tryptophan amino acid residue of the protein. Surfactant–polyanion nanostructures improve the solubility of lipophilic medicines such as Warfarin, Amphotericin B, and Meloxicam. Perspectives. Surfactant–PE composition demonstrated beneficial solubilization activity and can be recommended for the construction of nanocontainers for hydrophobic drugs, with their efficacy tuned by the variation in surfactant head group and the nature of polyanions.

show abstract

“…Proteins are biomolecules that consist of various amino acid residues connected with each other through peptide bonds and play an important role in every biological process. − Surfactants are amphiphilic moieties that consist of a charged hydrophilic head as well as an uncharged hydrophobic alkyl chain . Currently, the study of the interactions between proteins and surfactants is increasing day by day due to their increased applications in numerous fields like pharmaceuticals, detergents, food industry, and many more. − A protein–surfactant complex behaves as a model system to recognize the types of interactions present in the natural phenomenon, predominantly in cellular membranes having protein moieties, whose molecular structure is similar to that of surfactant moieties. , Thus, most of the studies comprising a protein–surfactant complex reflect the activity of proteins. Moreover, the surface tension of blood serums, which is a combination of albumins as well as low-molecular-weight surface active moieties, was utilized as an analytical device for renal disorders .…”

Section: Introductionmentioning

confidence: 99%

Interaction Behavior of N-Lauroyl Sarcosine Sodium Salt (NLSS) and Benzethonium Chloride (BC) in Aqueous Human Serum Albumin (HSA) at Different Temperatures: A Volumetric and Acoustic Study

et al. 2022

Self Cite

View full text Add to dashboard Cite

Density and speed of sound values of N-lauroyl sarcosine sodium salt (NLSS) and benzethonium chloride (BC) in mixed aqueous mixtures of human serum albumin (HSA) at three equidistant temperatures (298.15, 308.15, and 318.15 K) have been measured. Using density and speed of sound data, various thermodynamic and acoustic parameters like apparent molar volumes (V ϕ), partial molar volumes (V ϕ °), partial molar volumes of transfer (Δtr V ϕ °), dependence of partial molar volume on temperature, Helper’s constant, apparent molar isentropic compressibility (K ϕ,S), partial molar isentropic compressibility (K ϕ,S °), partial molar isentropic compressibility of transfer (Δtr K ϕ,S °), hydration number, and pair–triplet interaction coefficients have been determined. The cosphere overlap model was used to analyze several kinds of molecular interactions present in the studied systems, and it was found that two types of interactions were present in the studied system, i.e., ion–hydrophilic and hydrophilic–hydrophilic interactions. Negative values of Helper’s constant revealed that both NLSS and BC behave as structure breakers.

show abstract

Current trends in protein-surfactant interactions: A review

Cited by 31 publications

References 162 publications

Circular Dichroism Spectra of α-Chymotrypsin–SDS Solutions Depend on the Procedure of Their Preparation

Circular Dichroism Spectra of α-Chymotrypsin–SDS Solutions Depend on the Procedure of Their Preparation

Role of Polyanions and Surfactant Head Group in the Formation of Polymer–Colloid Nanocontainers

Interaction Behavior of N-Lauroyl Sarcosine Sodium Salt (NLSS) and Benzethonium Chloride (BC) in Aqueous Human Serum Albumin (HSA) at Different Temperatures: A Volumetric and Acoustic Study

Contact Info

Product

Resources

About