Interfacial tension measurements have been performed at the water/hexane interface on mixtures of the bovine milk protein β-lactoglobulin and positively charged cationic surfactants (alkytrimethylammonium bromides). The addition of surfactants with different chain lengths leads to the formation of protein-surfactant complexes with different adsorption properties as compared to those of the single protein. In this study, the formation of complexes has been observed clearly for protein-long chain surfactant (TTAB and CTAB) mixtures, which has shown in addition to specific electrostatic interactions the relevance of hydrophobic interactions between surfactant molecules and the protein. The modeling of interfacial tension data by using a mixed adsorption model provides a quantitative understanding of the mixture behavior. Indeed, the value of the adsorption constant of the protein obtained in the presence of surfactants has strongly varied as compared to the single protein. Actually, this parameter which represents the affinity of the molecule for the interface is representative of the hydrophobic character of the compound and so of its surface activity. Even if a more hydrophobic and more surface active protein-surfactant complex has been formed, the replacement of this complex from the interface by surfactants close to their cmc was observed.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1021/la1040757 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Polymerized whey protein-SDS interactions at their high concentrations.
Int J Biol Macromol
December 2024
Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC 27695, USA. Electronic address:
Protein-surfactant interactions have been an ongoing topic of interest for many decades. Applications involving complexes of proteins and surfactants are relevant in food, pharmaceuticals, hygiene, molecular characterization, and other fields. In this study, the interactions of polymerized whey proteins (PWP) and sodium dodecyl sulfate (SDS) at high concentrations are investigated.
View Article and Find Full Text PDFEffect of surface viscoelasticity on top jet drops produced by bursting bubbles.
Soft Matter
June 2024
Department of Mechanical Science and Engineering, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
Jet drops resulting from bubble bursting at a liquid surface play a key role in various mass transfer processes across the interface, including sea spray aerosol generation and pathogen transmission. However, the impact of structurally compound interfaces, characterized by complex surface rheology introduced by surface-active contaminants, on the jet drop ejection still remains unclear. Here, we experimentally investigate the influence of surface viscoelasticity on the size and velocity of the top jet drops from surface bubble bursting, examining both pure protein and mixed protein-surfactant solutions.
View Article and Find Full Text PDFCompetitive effects of salt and surfactant on the structure of nanoparticles in a binary system of nanoparticle and protein.
Phys Chem Chem Phys
August 2023
Solid State Physics Division, Bhabha Atomic Research Centre, Mumbai 400 085, India.
Article Synopsis
- SANS and DLS experiments investigate how NaCl and SDS surfactant affect silica nanoparticle and BSA protein interactions.
- Silica nanoparticles and BSA remain mostly separate in solution, but higher BSA concentrations can lead to nanoparticle aggregation due to protein-induced depletion attraction.
- Adding small amounts of salt triggers aggregation by reducing electrostatic repulsion, while SDS can suppress aggregation at lower salt levels through enhanced electrostatic repulsion with protein interactions.
Analysis and modeling of SDS and DPC micelle SAXS data for membrane protein solution structure characterization.
Data Brief
April 2023
Laboratoire de Biologie Physico-Chimique des Protéines Membranaires (IBPC), Université Paris Cité, CNRS, Paris F-75005, France.
Herein, we present analysis and analytical modeling of Small Angle X-ray Scattering (SAXS) data on two surfactants forming micelles (i.e., sodium dodecyl sulfate and dodecyl phosphocholine) and used for the study in solution of mTSPO, the translocator membrane protein from , as supporting data of the research article published in Biochimie (Combet et al.
View Article and Find Full Text PDFMolecular interaction of di-ester bonded cationic Gemini surfactants with pepsin: and perspectives.
J Biomol Struct Dyn
December 2023
Department of Chemistry, Aligarh Muslim University, Aligarh, India.
The implications of surfactant-enzyme/protein interactions in a variety of fields, including biotechnology, cosmetics, paints and pharmaceuticals, have attracted a lot of attention in contemporary studies. Herein, we have employed several and techniques such as excitation and absorption spectroscopies, circular dichroism and FT-IR spectroscopies, density functional and molecular dynamics simulations to understand the interaction behavior of oxy-diester-based green cationic Gemini surfactants, N,N,N,N-tetramethyl-2,13-dioxo-N,N-dialkyl-3,6,12-tetraoxateradecane-1,14-diaminiumdichloride (abbreviated as C-E2O2-C, where 'm' stands for alkyl chain length, = 12 and 14) with one of the main digestive proteins, pepsin. The spectroscopic techniques confirm the static quenching effect of surfactants on pepsin.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!