Influence of Acylation on the Adsorption of Insulin to Hydrophobic Surfaces
ABSTRACT Purpose To study the effect of acylation on the adsorption of insulin to hydrophobic polystyrene beads. Methods Adsorption isotherms for adsorption of insulin and acylated insulin to hydrophobic polystyrene beads were established, and the adsorption of the two proteins was compared further...
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| Published in | Pharmaceutical research Vol. 28; no. 5; pp. 1031 - 1040 |
|---|---|
| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Boston
Springer US
01.05.2011
Springer Springer Nature B.V |
| Subjects | |
| Online Access | Get full text |
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| Abstract | ABSTRACT
Purpose
To study the effect of acylation on the adsorption of insulin to hydrophobic polystyrene beads.
Methods
Adsorption isotherms for adsorption of insulin and acylated insulin to hydrophobic polystyrene beads were established, and the adsorption of the two proteins was compared further with isothermal titration calorimetry. In addition, the secondary structure and the association behavior of the two proteins were studied with circular dichroism.
Results
Insulin and acylated insulin adsorbed with high affinity to the hydrophobic polystyrene beads. More acylated insulin molecules than insulin molecules adsorbed per unit surface area from solutions containing monomer-dimer mixtures of acylated insulin and insulin, respectively. In contrast, no difference was observed in the number of insulin and acylated insulin molecules adsorbing per unit surface area, when adsorption occurred from solutions containing monomer-dimer-hexamer mixtures.
Conclusion
The influence of acylation on the adsorption behavior of insulin depends on the association degree of insulin, possibly due to a greater difference in hydrophobicity between monomeric insulin and acylated insulin than between the hexameric forms of these two proteins. |
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| AbstractList | To study the effect of acylation on the adsorption of insulin to hydrophobic polystyrene beads. Adsorption isotherms for adsorption of insulin and acylated insulin to hydrophobic polystyrene beads were established, and the adsorption of the two proteins was compared further with isothermal titration calorimetry. In addition, the secondary structure and the association behavior of the two proteins were studied with circular dichroism. Insulin and acylated insulin adsorbed with high affinity to the hydrophobic polystyrene beads. More acylated insulin molecules than insulin molecules adsorbed per unit surface area from solutions containing monomer-dimer mixtures of acylated insulin and insulin, respectively. In contrast, no difference was observed in the number of insulin and acylated insulin molecules adsorbing per unit surface area, when adsorption occurred from solutions containing monomer-dimer-hexamer mixtures. The influence of acylation on the adsorption behavior of insulin depends on the association degree of insulin, possibly due to a greater difference in hydrophobicity between monomeric insulin and acylated insulin than between the hexameric forms of these two proteins.[PUBLICATION ABSTRACT] To study the effect of acylation on the adsorption of insulin to hydrophobic polystyrene beads. Adsorption isotherms for adsorption of insulin and acylated insulin to hydrophobic polystyrene beads were established, and the adsorption of the two proteins was compared further with isothermal titration calorimetry. In addition, the secondary structure and the association behavior of the two proteins were studied with circular dichroism. Insulin and acylated insulin adsorbed with high affinity to the hydrophobic polystyrene beads. More acylated insulin molecules than insulin molecules adsorbed per unit surface area from solutions containing monomer-dimer mixtures of acylated insulin and insulin, respectively. In contrast, no difference was observed in the number of insulin and acylated insulin molecules adsorbing per unit surface area, when adsorption occurred from solutions containing monomer-dimer-hexamer mixtures. The influence of acylation on the adsorption behavior of insulin depends on the association degree of insulin, possibly due to a greater difference in hydrophobicity between monomeric insulin and acylated insulin than between the hexameric forms of these two proteins. ABSTRACT Purpose To study the effect of acylation on the adsorption of insulin to hydrophobic polystyrene beads. Methods Adsorption isotherms for adsorption of insulin and acylated insulin to hydrophobic polystyrene beads were established, and the adsorption of the two proteins was compared further with isothermal titration calorimetry. In addition, the secondary structure and the association behavior of the two proteins were studied with circular dichroism. Results Insulin and acylated insulin adsorbed with high affinity to the hydrophobic polystyrene beads. More acylated insulin molecules than insulin molecules adsorbed per unit surface area from solutions containing monomer-dimer mixtures of acylated insulin and insulin, respectively. In contrast, no difference was observed in the number of insulin and acylated insulin molecules adsorbing per unit surface area, when adsorption occurred from solutions containing monomer-dimer-hexamer mixtures. Conclusion The influence of acylation on the adsorption behavior of insulin depends on the association degree of insulin, possibly due to a greater difference in hydrophobicity between monomeric insulin and acylated insulin than between the hexameric forms of these two proteins. PURPOSETo study the effect of acylation on the adsorption of insulin to hydrophobic polystyrene beads. METHODSAdsorption isotherms for adsorption of insulin and acylated insulin to hydrophobic polystyrene beads were established, and the adsorption of the two proteins was compared further with isothermal titration calorimetry. In addition, the secondary structure and the association behavior of the two proteins were studied with circular dichroism. RESULTSInsulin and acylated insulin adsorbed with high affinity to the hydrophobic polystyrene beads. More acylated insulin molecules than insulin molecules adsorbed per unit surface area from solutions containing monomer-dimer mixtures of acylated insulin and insulin, respectively. In contrast, no difference was observed in the number of insulin and acylated insulin molecules adsorbing per unit surface area, when adsorption occurred from solutions containing monomer-dimer-hexamer mixtures. CONCLUSIONThe influence of acylation on the adsorption behavior of insulin depends on the association degree of insulin, possibly due to a greater difference in hydrophobicity between monomeric insulin and acylated insulin than between the hexameric forms of these two proteins. |
| Author | Bukrinsky, Jens Thostrup Hostrup, Susanne Pinholt, Charlotte Frokjaer, Sven Jorgensen, Lene |
| Author_xml | – sequence: 1 givenname: Charlotte surname: Pinholt fullname: Pinholt, Charlotte email: cp@farma.ku.dk organization: Department of Pharmaceutics and Analytical Chemistry Faculty of Pharmaceutical Sciences, University of Copenhagen, Faculty of Pharmaceutical Sciences – sequence: 2 givenname: Susanne surname: Hostrup fullname: Hostrup, Susanne organization: CMC Diabetes Analysis and Formulation, Novo Nordisk A/S – sequence: 3 givenname: Jens Thostrup surname: Bukrinsky fullname: Bukrinsky, Jens Thostrup organization: Novozymes Biopharma DK A/S – sequence: 4 givenname: Sven surname: Frokjaer fullname: Frokjaer, Sven organization: Department of Pharmaceutics and Analytical Chemistry Faculty of Pharmaceutical Sciences, University of Copenhagen – sequence: 5 givenname: Lene surname: Jorgensen fullname: Jorgensen, Lene organization: Department of Pharmaceutics and Analytical Chemistry Faculty of Pharmaceutical Sciences, University of Copenhagen |
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| CitedBy_id | crossref_primary_10_1016_j_colsurfb_2013_01_075 crossref_primary_10_1002_psc_2423 crossref_primary_10_1016_j_ijpharm_2018_06_023 crossref_primary_10_1080_00986445_2012_655812 crossref_primary_10_1021_acs_langmuir_6b00522 crossref_primary_10_1016_j_ifacsc_2019_100042 crossref_primary_10_1016_j_ijpharm_2012_01_040 crossref_primary_10_1517_17425247_2011_577062 crossref_primary_10_1016_S1773_2247_13_50051_7 crossref_primary_10_1002_jmr_1167 crossref_primary_10_1021_jp4101202 crossref_primary_10_1002_jctb_5148 crossref_primary_10_1021_acs_langmuir_5b01477 |
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| Keywords | protein adsorption CD ITC insulin acylated insulin Pharmaceutical technology Adsorption Insulin Protein Acylation |
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| Snippet | ABSTRACT
Purpose
To study the effect of acylation on the adsorption of insulin to hydrophobic polystyrene beads.
Methods
Adsorption isotherms for adsorption of... To study the effect of acylation on the adsorption of insulin to hydrophobic polystyrene beads. Adsorption isotherms for adsorption of insulin and acylated... To study the effect of acylation on the adsorption of insulin to hydrophobic polystyrene beads. Adsorption isotherms for adsorption of insulin and acylated... PURPOSETo study the effect of acylation on the adsorption of insulin to hydrophobic polystyrene beads. METHODSAdsorption isotherms for adsorption of insulin... |
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| SubjectTerms | Adsorption Amino Acid Sequence Biochemistry Biological and medical sciences Biomedical and Life Sciences Biomedical Engineering and Bioengineering Biomedicine General pharmacology Humans Hydrophobic and Hydrophilic Interactions Insulin Insulin - chemistry Medical Law Medical sciences Molecular Sequence Data Pharmaceutical sciences Pharmaceutical technology. Pharmaceutical industry Pharmacology. Drug treatments Pharmacology/Toxicology Pharmacy Proteins Research Paper Surface Properties |
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| Title | Influence of Acylation on the Adsorption of Insulin to Hydrophobic Surfaces |
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