Stabilisation of dissolved proteins against denaturation at hydrophobic interfaces

Studies with insulin delivery devices have shown that denaturation of dissolved proteins at hydrophobic interfaces is a basic obstacle to long-term insulin stability in pumps. This study shows that polypropylene glycol/polyethylene glycol block polymers prevent both the adsorption of dissolved prote...

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Bibliographic Details
Published inDiabetologia Vol. 27; no. 2; p. 212
Main Authors Thurow, H, Geisen, K
Format Journal Article
LanguageEnglish
Published Germany 01.08.1984
Subjects
Adsorption
Animals
Cattle
Drug Stability
Insulin
Insulin Infusion Systems
Polyethylene Glycols - pharmacology
Polymers - pharmacology
Propylene Glycols - pharmacology
Protein Denaturation
Solubility
Surface Properties
Swine
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Summary:Studies with insulin delivery devices have shown that denaturation of dissolved proteins at hydrophobic interfaces is a basic obstacle to long-term insulin stability in pumps. This study shows that polypropylene glycol/polyethylene glycol block polymers prevent both the adsorption of dissolved proteins to hydrophobic interfaces and the resultant aggregation. At a concentration of 0.001% (w/v), the block polymer Genapol PF-10 stabilises insulin solutions over a wide range of concentrations. Insulin solutions thus stabilised are at present being clinically tested. The effectiveness of molecular variants of Genapol PF-10 to stabilise other proteins (human gamma-globulin, myoglobin and serum albumin) is presented also.
ISSN:0012-186X