Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 425576
Title Influence of PEGylation with linear and branched PEG chains on the adsorption of glucagon to hydrophobic surfaces
Author(s) Pinholt, C.; Bukrinsky, J.T.; Hostrup, S.; Frokjaer, S.; Norde, W.; Jorgensen, L.
Source European Journal of Pharmaceutics and Biopharmaceutics 77 (2011)1. - ISSN 0939-6411 - p. 139 - 147.
DOI http://dx.doi.org/10.1016/j.ejpb.2010.11.001
Department(s) Physical Chemistry and Colloid Science
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) poly(ethylene glycol)-modified lysozyme - protein adsorption - polyethylene-glycols - silica - conformation - fluorescence - association - molecules - fragments - peptide
Abstract PEGylation has proven useful for prolonging the plasma half lives of proteins, and since approval of the first PEGylated protein drug product by the FDA in 1990, several PEGylated protein drug products have been marketed. However, the influence of PEGylation on the behavior of proteins at interfaces is only poorly understood. The aim of this work was to study the effect of PEGylation on the adsorption of glucagon from aqueous solution to a hydrophobic surface and to compare the effects of PEGylation with a linear and a branched PEG chain, respectively. The 3483 Da peptide glucagon was PEGylated with a 2.2 kDa linear and a branched PEG chain, respectively, and the adsorption behaviors of the three proteins were compared using isothermal titration calorimetry, fixed-angle optical reflectometry and total internal reflection fluorescence. PEGylation decreased the number of glucagon molecules adsorbing per unit surface area and increased the initial adsorption rate of glucagon. Furthermore, the results indicated that the orientation and/or structural changes of glucagon upon adsorption were affected by the PEGylation. Finally, from the isothermal titration calorimetry and the reflectometry data, it was observed that the architecture of the PEG chains had an influence on the observed heat flow upon adsorption as well as on the initial rate of adsorption, respectively.
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