Influence of acylation on the adsorption of GLP-2 to hydrophobic surfaces

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Standard

Influence of acylation on the adsorption of GLP-2 to hydrophobic surfaces. / Pinholt, Charlotte; Kapp, Sebastian J; Bukrinsky, Jens T; Hostrup, Susanne; Frokjaer, Sven; Norde, Willem; Jorgensen, Lene.

I: International Journal of Pharmaceutics, Bind 440, Nr. 1, 2013, s. 63-71.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Pinholt, C, Kapp, SJ, Bukrinsky, JT, Hostrup, S, Frokjaer, S, Norde, W & Jorgensen, L 2013, 'Influence of acylation on the adsorption of GLP-2 to hydrophobic surfaces', International Journal of Pharmaceutics, bind 440, nr. 1, s. 63-71. https://doi.org/10.1016/j.ijpharm.2012.01.040

APA

Pinholt, C., Kapp, S. J., Bukrinsky, J. T., Hostrup, S., Frokjaer, S., Norde, W., & Jorgensen, L. (2013). Influence of acylation on the adsorption of GLP-2 to hydrophobic surfaces. International Journal of Pharmaceutics, 440(1), 63-71. https://doi.org/10.1016/j.ijpharm.2012.01.040

Vancouver

Pinholt C, Kapp SJ, Bukrinsky JT, Hostrup S, Frokjaer S, Norde W o.a. Influence of acylation on the adsorption of GLP-2 to hydrophobic surfaces. International Journal of Pharmaceutics. 2013;440(1):63-71. https://doi.org/10.1016/j.ijpharm.2012.01.040

Author

Pinholt, Charlotte ; Kapp, Sebastian J ; Bukrinsky, Jens T ; Hostrup, Susanne ; Frokjaer, Sven ; Norde, Willem ; Jorgensen, Lene. / Influence of acylation on the adsorption of GLP-2 to hydrophobic surfaces. I: International Journal of Pharmaceutics. 2013 ; Bind 440, Nr. 1. s. 63-71.

Bibtex

@article{9f0feb4a20bd4620a673b3523342ecc2,

title = "Influence of acylation on the adsorption of GLP-2 to hydrophobic surfaces",

abstract = "Acylation of proteins with a fatty acid chain has proven useful for prolonging the plasma half-lives of proteins. In formulation of acylated protein drugs, knowledge about the effect of acylation with fatty acids on the adsorption behaviour of proteins at interfaces will be valuable. The aim of this work was to study the effect of acylation on the adsorption of GLP-2 from aqueous solution to a hydrophobic surface by comparing the adsorption of the 3766 Da GLP-2 with that of a GLP-2 variant acylated with a 16-carbon fatty acid chain through a {\ss}-alanine linker. Adsorption of GLP-2 and acylated GLP-2 were studied with isothermal titration calorimetry, fixed-angle optical reflectometry and total internal reflection fluorescence. Furthermore, the effect of acylation of GLP-2 on the secondary structure was studied with Far-UV CD. Acylation was observed to have several effects on the adsorption of GLP-2. Acylation increased the amount of GLP-2 adsorbing per unit surface area and decreased the initial adsorption rate of GLP-2. Finally, acylation increased the strength of the adsorption, as judged by the lower fraction desorbing upon rinsing with buffer.",

author = "Charlotte Pinholt and Kapp, {Sebastian J} and Bukrinsky, {Jens T} and Susanne Hostrup and Sven Frokjaer and Willem Norde and Lene Jorgensen",

year = "2013",

doi = "10.1016/j.ijpharm.2012.01.040",

language = "English",

volume = "440",

pages = "63--71",

journal = "International Journal of Pharmaceutics",

issn = "0378-5173",

publisher = "Elsevier",

number = "1",

}

RIS

TY - JOUR

T1 - Influence of acylation on the adsorption of GLP-2 to hydrophobic surfaces

AU - Pinholt, Charlotte

AU - Kapp, Sebastian J

AU - Bukrinsky, Jens T

AU - Hostrup, Susanne

AU - Frokjaer, Sven

AU - Norde, Willem

AU - Jorgensen, Lene

PY - 2013

Y1 - 2013

N2 - Acylation of proteins with a fatty acid chain has proven useful for prolonging the plasma half-lives of proteins. In formulation of acylated protein drugs, knowledge about the effect of acylation with fatty acids on the adsorption behaviour of proteins at interfaces will be valuable. The aim of this work was to study the effect of acylation on the adsorption of GLP-2 from aqueous solution to a hydrophobic surface by comparing the adsorption of the 3766 Da GLP-2 with that of a GLP-2 variant acylated with a 16-carbon fatty acid chain through a ß-alanine linker. Adsorption of GLP-2 and acylated GLP-2 were studied with isothermal titration calorimetry, fixed-angle optical reflectometry and total internal reflection fluorescence. Furthermore, the effect of acylation of GLP-2 on the secondary structure was studied with Far-UV CD. Acylation was observed to have several effects on the adsorption of GLP-2. Acylation increased the amount of GLP-2 adsorbing per unit surface area and decreased the initial adsorption rate of GLP-2. Finally, acylation increased the strength of the adsorption, as judged by the lower fraction desorbing upon rinsing with buffer.

AB - Acylation of proteins with a fatty acid chain has proven useful for prolonging the plasma half-lives of proteins. In formulation of acylated protein drugs, knowledge about the effect of acylation with fatty acids on the adsorption behaviour of proteins at interfaces will be valuable. The aim of this work was to study the effect of acylation on the adsorption of GLP-2 from aqueous solution to a hydrophobic surface by comparing the adsorption of the 3766 Da GLP-2 with that of a GLP-2 variant acylated with a 16-carbon fatty acid chain through a ß-alanine linker. Adsorption of GLP-2 and acylated GLP-2 were studied with isothermal titration calorimetry, fixed-angle optical reflectometry and total internal reflection fluorescence. Furthermore, the effect of acylation of GLP-2 on the secondary structure was studied with Far-UV CD. Acylation was observed to have several effects on the adsorption of GLP-2. Acylation increased the amount of GLP-2 adsorbing per unit surface area and decreased the initial adsorption rate of GLP-2. Finally, acylation increased the strength of the adsorption, as judged by the lower fraction desorbing upon rinsing with buffer.

U2 - 10.1016/j.ijpharm.2012.01.040

DO - 10.1016/j.ijpharm.2012.01.040

M3 - Journal article

C2 - 22310460

VL - 440

SP - 63

EP - 71

JO - International Journal of Pharmaceutics

JF - International Journal of Pharmaceutics

SN - 0378-5173

IS - 1

ER -

ID: 44287731