Interactions of β-lactoglobulin with sodium decylsulfonate, decyltriethylammonium bromide, and their mixtures

Lu, Run-Chao; Cao, Aoneng; Lai, Luhua; Xiao, Jin‐Xin

doi:10.1016/j.jcis.2006.02.038

Cited by 21 publications

(28 citation statements)

References 34 publications

(46 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In the scientific community, protein-surfactant interactions have received considerable attention owing to their potential applications in the various domains like cosmetics, pharmaceuticals, biotechnology and physiological systems [1][2][3][4][5][6][7]. Health care products and pharmaceuticals contain proteins in combination with binding agents as functional ingredients [8][9][10].…”

Section: Introductionmentioning

confidence: 99%

“…Therefore, it seems appropriate to study 16-E2-16 + xanthine oxidase interactions. Moreover, as most of the surfactants (both conventional and gemini surfactants) have the ability to alter/denature proteins [1][2][3][4][5][6][7][21][22][23][24][25][26][27][28][29][30][31][32], therefore, 16-E2-16 gemini surfactant too is expected to influence the conformation of xanthine oxidase.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Conformational alterations induced by novel green 16-E2-16 gemini surfactant in xanthine oxidase: Biophysical insights from tensiometry, spectroscopy, microscopy and molecular modeling

Akram

Bhat

et al. 2015

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

View full text Add to dashboard Cite

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Conformational alterations induced by novel green 16-E2-16 gemini surfactant in xanthine oxidase: Biophysical insights from tensiometry, spectroscopy, microscopy and molecular modeling

Akram

Bhat

et al. 2015

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

View full text Add to dashboard Cite

“…The enzymes fluorescence is mostly associated with the microenvironment of the Trp residues and cationic surfactants would tend to cluster around Glu and Asp side chains of protein (Lu et al 2006). Analysis of conserved domain database with PSI-BLAST program reveals ( Fig.…”

Section: Sequence Analysismentioning

confidence: 99%

Conformational changes and sequence analysis in cellulase from Aspergillus niger with cationic surfactant

Bordbar

Mehnati-Najafabadi

2010

Cellulose

View full text Add to dashboard Cite

The present study evaluates the binding of cetylpyridinium chloride (CPC) with cellulase in various experimental conditions using potentiometric, fluorescence spectroscopy and turbidimetric techniques. The analysis of binding curves revealed the existence of two sets of binding sets for CPC. The binding parameters were estimated and interpreted in terms of structural viewpoints of cellulase. The observation of turbidity suggests that CPC molecules individually nucleate around cellulase/CMC complex to form micelle-like structures. Fluorescence spectroscopy analysis of cellulase/CMC-surfactant system showed that these complexes could be compact to elucidate the mechanism of binding cellulase/CMC complex to CPC. The differential response of the enzyme/CMC to surfactant, indicates that the interaction on the complex surface is strongly ionic and hydrophobic(cooperative) in nature. A sequencing analysis was also conducted on b-1, 4-endoglucanase from A. niger (EglA) and others from family 12 in order to examine the nature of interaction involved in binding process and structure of carbohydrate-protein complexes. The results suggest that the conserved residues are located in a more hydrophobic microenvironment and apolar area energy is more than polar within enzyme structure.

show abstract

“…Studies on the interaction between surfactants and proteins have attracted considerable interest in the past decades due to the manifold applications of protein–surfactant systems, e.g. in the food industry, pharmaceutical industry, analytical biochemistry and physiological systems . It is reported that interactions of surfactants with proteins also change the conformations and biological functions of proteins .…”

Section: Introductionmentioning

confidence: 99%

Studies on the synthesis, characterization, human serum albumin binding and biological activity of single chain surfactant–cobalt(III) complexes

et al. 2015

View full text Add to dashboard Cite

The interaction of surfactant-cobalt(III) complexes [Co(bpy)(dien)TA](ClO4)3 · 3H2O (1) and [Co(dien)(phen)TA](ClO4)3 · 4H2O (2), where bpy = 2,2'-bipyridine, dien = diethylenetriamine, phen = 1,10-phenanthroline and TA = tetradecylamine with human serum albumin (HSA) under physiological conditions was analyzed using steady state, synchronous, 3D fluorescence, UV/visabsorption and circular dichroism spectroscopic techniques. The results show that these complexes cause the fluorescence quenching of HSA through a static mechanism. The binding constant (Kb ) and number of binding-sites (n) were obtained at different temperatures. The corresponding thermodynamic parameters (∆G°, ∆H° and ∆S°) and Ea were also obtained. According to Förster's non-radiation energy transfer theory, the binding distance (r) between the complexes and HSA were calculated. The results of synchronous and 3D fluorescence spectroscopy indicate that the binding process has changed considerably the polarity around the fluorophores, along with changes in the conformation of the protein. The antimicrobial and anticancer activities of the complexes were tested and the results show that the complexes have good activities against pathogenic microorganisms and cancer cells.

show abstract

Interactions of β-lactoglobulin with sodium decylsulfonate, decyltriethylammonium bromide, and their mixtures

Cited by 21 publications

References 34 publications

Conformational alterations induced by novel green 16-E2-16 gemini surfactant in xanthine oxidase: Biophysical insights from tensiometry, spectroscopy, microscopy and molecular modeling

Conformational alterations induced by novel green 16-E2-16 gemini surfactant in xanthine oxidase: Biophysical insights from tensiometry, spectroscopy, microscopy and molecular modeling

Conformational changes and sequence analysis in cellulase from Aspergillus niger with cationic surfactant

Studies on the synthesis, characterization, human serum albumin binding and biological activity of single chain surfactant–cobalt(III) complexes

Contact Info

Product

Resources

About