Tuning of protein-surfactant interaction to modify the resultant structure

Mehan, Sumit; Aswal, Vinod K.; Kohlbrecher, J.

doi:10.1103/physreve.92.032713

Cited by 21 publications

(28 citation statements)

References 55 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The non-ionic surfactant Triton X-100 consists of a polydisperse preparation of p -(1,1,3,3-tetramethylbutyl) phenyl) poly (oxyethylene) with 10 oxyethylene units per molecule on average [24]. Nonionic surfactants such as Triton X-100 interact with proteins through hydrophobic interactions and are therefore often tolerated by proteins [25].…”

Section: Introductionmentioning

confidence: 99%

KnowVolution of the Polymer-Binding Peptide LCI for Improved Polypropylene Binding

et al. 2018

View full text Add to dashboard Cite

The functionalization of polymer surfaces by polymer-binding peptides offers tremendous opportunities for directed immobilization of enzymes, bioactive peptides, and antigens. The application of polymer-binding peptides as adhesion promoters requires reliable and stable binding under process conditions. Molecular modes of interactions between material surfaces, peptides, and solvent are often not understood to an extent that enables (semi-) rational design of polymer-binding peptides, hindering the full exploitation of their potential. Knowledge-gaining directed evolution (KnowVolution) is an efficient protein engineering strategy that facilitates tailoring protein properties to application demands through a combination of directed evolution and computational guided protein design. A single round of KnowVolution was performed to gain molecular insights into liquid chromatography peak I peptide, 47 aa (LCI)-binding to polypropylene (PP) in the presence of the competing surfactant Triton X-100. KnowVolution yielded a total of 8 key positions (D19, S27, Y29, D31, G35, I40, E42, and D45), which govern PP-binding in the presence of Triton X-100. The recombination of two of the identified amino acid substitutions (Y29R and G35R; variant KR-2) yielded a 5.4 ± 0.5-fold stronger PP-binding peptide compared to LCI WT in the presence of Triton X-100 (1 mM). The LCI variant KR-2 shows a maximum binding capacity of 8.8 ± 0.1 pmol/cm2 on PP in the presence of Triton X-100 (up to 1 mM). The KnowVolution approach enables the development of polymer-binding peptides, which efficiently coat and functionalize PP surfaces and withstand surfactant concentrations that are commonly used, such as in household detergents.

show abstract

Section: Introductionmentioning

confidence: 99%

KnowVolution of the Polymer-Binding Peptide LCI for Improved Polypropylene Binding

et al. 2018

View full text Add to dashboard Cite

show abstract

“…It is a firmly established fact that ionic surfactants such as sodium dodecyl sulfate (SDS) or dodecyltrimethylammonium bromide (DTAB) could denature proteins at low concentrations relative to other denaturants such as urea or guanidinium chloride. 7−11 On the contrary, nonionic surfactants only play a minor role in the denaturation of some proteins. 12,13 The emerging scientific interest consists of the detailed understanding of protein–surfactant interactions to follow the pathway of unfolding and refolding of the protein.…”

Section: Introductionmentioning

confidence: 99%

Unfolding and Refolding of Protein by a Combination of Ionic and Nonionic Surfactants

et al. 2018

Self Cite

View full text Add to dashboard Cite

The interaction of protein and surfactant yields protein–surfactant complexes which have a wide range of applications in the cosmetics, foods, and pharmaceutical industries among others. Ionic and nonionic surfactants are known to interact differently with the protein. The interplay of electrostatic and hydrophobic interactions governs the resultant structure of protein–surfactant complexes. The present study enlightens the paramount role of the hydrophobic interaction, tuned by the hydrophobic tail length of ionic surfactants, in the unfolding of anionic bovine serum albumin (BSA) protein. The unfolding of BSA in the presence of four different tail-length cationic surfactants, that is, C10TAB, C12TAB, C14TAB, and C16TAB, has been investigated by small-angle neutron scattering and dynamic light scattering. All cationic surfactants unfold the protein at a certain concentration range. The propensity of protein unfolding increases with increasing the hydrophobic tail length. The denatured structure of BSA upon addition of cationic surfactants is characterized by the random flight model representing a beads-on-a-string chain-like complex. The unfolded protein binds the surfactant micelles in the protein–surfactant cluster. The micelles get elongated with the increasing concentration of cationic surfactants, whereas the number of micelles per cluster is decreased. In the final stage, the protein–surfactant cluster merges to one large micelle with unfolded protein wrapping the micelle surface. The pathway of protein unfolding is described in terms of the changes in the micellar size, the number of micelles formed per cluster, the separation between the micelles in the cluster, the aggregation number of micelles, and the number of proteins per cluster. The protein–surfactant interaction is further examined in the presence of a nonionic surfactant, that is, C12E10. The nonionic surfactant significantly suppresses the interaction of BSA protein with ionic surfactants by forming mixed micelles. As a result of the mixed micelles formation by ionic–nonionic surfactants, the ionic surfactant moves out from the unfolded BSA protein, and this enables the protein to refold back to its native structure. The propensity of mixed micelle-driven refolding of proteins is significantly changed with changing the tail length of the ionic surfactant.

show abstract

“…There are three main forces that drive the protein–surfactant interaction: (1) electrostatic, (2) hydrophobic and (3) Van der Waals (Mackie and Wilde 2005 ; Li and Lee 2019 ). The dominant interaction is determined by the nature of both molecules and their concentration (Mehan et al 2015 ; Li and Lee 2019 ). These molecular interactions have an influence on the native structure of proteins promoting or preventing denaturation, aggregation and loss of enzymatic activity among other factors (Mehan et al 2015 ).…”

Section: Surfactant–protein Interactionsmentioning

confidence: 99%

“…The dominant interaction is determined by the nature of both molecules and their concentration (Mehan et al 2015 ; Li and Lee 2019 ). These molecular interactions have an influence on the native structure of proteins promoting or preventing denaturation, aggregation and loss of enzymatic activity among other factors (Mehan et al 2015 ). Surfactants of biological origin have an advantage over synthetic surfactants in terms of their ability to prevent denaturation of proteins and a reduction in their aggregation (Otzen 2011 , 2017 ).…”

Section: Surfactant–protein Interactionsmentioning

confidence: 99%

“…The effect on stabilization or destabilization mediated by a surfactant is dependent on the concentration of the surfactant (Mehan et al 2015 ). In that sense, many surfactants (biological and synthetic ones), usually promote protein stabilization at concentrations far below Critical Micelle Concentration (CMC), while at concentrations higher than the CMC there is an opposite effect, they promote denaturation, aggregation, as well as loss of biological function of proteins (Díaz et al 2003 ; Otzen 2011 ; Malik 2015 ).…”

Section: Surfactant–protein Interactionsmentioning

confidence: 99%

See 1 more Smart Citation

Surfactants: physicochemical interactions with biological macromolecules

et al. 2021

View full text Add to dashboard Cite

Macromolecules are essential cellular components in biological systems responsible for performing a large number of functions that are necessary for growth and perseverance of living organisms. Proteins, lipids and carbohydrates are three major classes of biological macromolecules. To predict the structure, function, and behaviour of any cluster of macromolecules, it is necessary to understand the interaction between them and other components through basic principles of chemistry and physics. An important number of macromolecules are present in mixtures with surfactants, where a combination of hydrophobic and electrostatic interactions is responsible for the specific properties of any solution. It has been demonstrated that surfactants can help the formation of helices in some proteins thereby promoting protein structure formation. On the other hand, there is extensive research towards the use of surfactants to solubilize drugs and pharmaceuticals; therefore, it is evident that the interaction between surfactants with macromolecules is important for many applications which includes environmental processes and the pharmaceutical industry. In this review, we describe the properties of different types of surfactants that are relevant for their physicochemical interactions with biological macromolecules, from macromolecules–surfactant complexes to hydrophobic and electrostatic interactions.

show abstract

Tuning of protein-surfactant interaction to modify the resultant structure

Cited by 21 publications

References 55 publications

KnowVolution of the Polymer-Binding Peptide LCI for Improved Polypropylene Binding

KnowVolution of the Polymer-Binding Peptide LCI for Improved Polypropylene Binding

Unfolding and Refolding of Protein by a Combination of Ionic and Nonionic Surfactants

Surfactants: physicochemical interactions with biological macromolecules

Contact Info

Product

Resources

About