Displacement of Adsorbed Insulin by Tween 80 Monitored Using Total Internal Reflection Fluorescence and Ellipsometry

Mollmann, Susanne H.; Elofsson, Ulla; Bukrinsky, Jens T.; Frøkjær, Sven

doi:10.1007/s11095-005-7249-1

Cited by 49 publications

(17 citation statements)

References 44 publications

(44 reference statements)

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“…A similar effect of Tween 80 on the adsorption of insulin onto the hydrophobic surface of silane-modified quartz slides has been reported (61), as it was hypothesized that Tween 80 displaced adsorbed insulin from the silane-modified quartz (61). In this study, the adsorption of cellulase onto CEL-SELP was reduced by 60% with the addition of 0.1-0.2% Tween 80.…”

Section: Resultssupporting

confidence: 85%

Adsorption of Cellulase on Cellulolytic Enzyme Lignin from Lodgepole Pine

Tu¹,

Pan²,

Saddler³

2009

J. Agric. Food Chem.

181

122

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Enzymatic hydrolysis of lignocellulosic materials is significantly affected by cellulase adsorption onto the lignocellulosic substrates and lignin. The presence of lignin plays an important role in lignocellulosic hydrolysis and enzyme recycling. Three cellulase preparations (Celluclast, Spezyme CP, and MSUBC) were evaluated to determine their adsorption onto cellulolytic enzyme lignin (CEL) from steam-exploded Lodgepole pine (SELP) and ethanol (organosolv)-pretreated Lodgepole pine (EPLP). The adsorption affinity of cellulase (Celluclast) onto isolated lignin (CEL-EPLP and CEL-SELP) was slightly higher than that from corresponding EPLP and SELP substrates on the basis of the Langmuir constants. Effects of temperature, ionic strength, and surfactant on cellulase adsorption onto isolated lignin were also explored in this study. Thermodynamic analysis of enzyme adsorption onto isolated lignin (Gibbs free energy change DeltaG(0) approximately -30 kJ/mol) indicated this adsorption was a spontaneous process. The addition of surfactant (0.2% w/v) could reduce the adsorption of cellulase onto CEL-SELP by 60%. Two types of adsorption isotherm were compared for cellulase adsorption onto isolated lignin. A Langmuir adsorption isotherm showed better fit for the experimental data than a Freundlich adsorption isotherm.

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Section: Resultssupporting

confidence: 85%

Adsorption of Cellulase on Cellulolytic Enzyme Lignin from Lodgepole Pine

Tu¹,

Pan²,

Saddler³

2009

J. Agric. Food Chem.

181

122

View full text Add to dashboard Cite

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“…On the other hand, the Trp side chain peak did not disappear in response to Tween 80, indicating that there was no hydrophobic interaction between the peptide and Tween 80. This is further supported by a previous study that did not find any general structural changes in insulin in the presence of Tween 80, which suggests that only limited interactions, if any, occur between the two species in solution [50]. Clearly, this result shows that Tween 80 had no harmful effects on the peptides, which could be useful for the cosmetic application of these peptides using Tween 80 as a co-surfactant.…”

Section: Resultssupporting

confidence: 84%

Applications of Circular Dichroism for Structural Analysis of Gelatin and Antimicrobial Peptides

Gopal

Park

Seo

et al. 2012

IJMS

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Circular dichroism (CD) is a useful technique for monitoring changes in the conformation of antimicrobial peptides or gelatin. In this study, interactions between cationic peptides and gelatin were observed without affecting the triple helical content of the gelatin, which was more strongly affected by anionic surfactant. The peptides did not adopt a secondary structure in the presence of aqueous solution or Tween 80, but a peptide secondary structure formed upon the addition of sodium dodecyl sulfate (SDS). The peptides bound to the phosphate group of lipopolysaccharide (LPS) and displayed an alpha-helical conformation while (KW) 4 adopted a folded conformation. Further, the peptides did not specifically interact with the fungal cell wall components of mannan or laminarin. Tryptophan blue shift assay indicated that these peptides interacted with SDS, LPS, and gelatin but not with Tween 80, mannan, or laminarin. The peptides also displayed antibacterial activity against P. aeruginosa without cytotoxicity against HaCaT cells at MIC, except for HPA3NT3-analog peptide. In this study, we used a CD spectroscopic method to demonstrate the feasibility of peptide characterization in numerous environments. The CD method can thus be used as a screening method of gelatin-peptide interactions for use in wound healing applications. OPEN ACCESSInt. J. Mol. Sci. 2012, 13 3230

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“…4 As the same stabilizing effect is expected to be present for IGlu, an opposite effect or effects leading to a net reduction in IGlu physical stability must have been present in order to explain the significant reduced stability of the pumped IGlu samples. It can be speculated if the stabilizer used in IGlu (polysorbate 20) tends to be adsorbed to the polymeric surface material of the reservoir inner wall and/or infusion set as published for other detergents, 15 thus leading to a reduced amount of free detergent in the aqueous phase to stabilize the insulin. If this is the case, the negative effect of reduced detergent concentration on physical stability of IGlu must dominate the positive effect of insulin-related impurities on the physical stability against fibrillation.…”

Section: Results and Conclusionmentioning

confidence: 99%