Influence of acylation on the adsorption of insulin to hydrophobic surfaces

Charlotte Pinholt; Susanne Hostrup; Jens Thostrup Bukrinsky; Sven Frøkjær; Lene Jørgensen

doi:10.1007/s11095-010-0349-6

Influence of acylation on the adsorption of insulin to hydrophobic surfaces

Charlotte Pinholt, Susanne Hostrup, Jens Thostrup Bukrinsky, Sven Frøkjær, Lene Jørgensen

13 Citations (Scopus)

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.

Original language	English
Journal	Pharmaceutical Research
Volume	28
Pages (from-to)	1031-1040
ISSN	0724-8741
DOIs	https://doi.org/10.1007/s11095-010-0349-6
Publication status	Published - May 2011

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Former Faculty of Pharmaceutical Sciences

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10.1007/s11095-010-0349-6

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title = "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 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.",

keywords = "Former Faculty of Pharmaceutical Sciences",

author = "Charlotte Pinholt and Susanne Hostrup and Bukrinsky, {Jens Thostrup} and Sven Fr{\o}kj{\ae}r and Lene J{\o}rgensen",

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doi = "10.1007/s11095-010-0349-6",

language = "English",

volume = "28",

pages = "1031--1040",

journal = "Pharmaceutical Research",

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T1 - Influence of acylation on the adsorption of insulin to hydrophobic surfaces

AU - Pinholt, Charlotte

AU - Hostrup, Susanne

AU - Bukrinsky, Jens Thostrup

AU - Frøkjær, Sven

AU - Jørgensen, Lene

PY - 2011/5

Y1 - 2011/5

N2 - 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.

AB - 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.

KW - Former Faculty of Pharmaceutical Sciences

U2 - 10.1007/s11095-010-0349-6

DO - 10.1007/s11095-010-0349-6

M3 - Journal article

C2 - 21190067

SN - 0724-8741

VL - 28

SP - 1031

EP - 1040

JO - Pharmaceutical Research

JF - Pharmaceutical Research

ER -

Influence of acylation on the adsorption of insulin to hydrophobic surfaces

Abstract

Keywords

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