Insulin &amp; Related Proteins - Structure to Function and Pharmacology

Dieken, Markus Leyck; Federwisch, Matthias; Meyts, Pierre De

doi:10.1007/0-306-47582-0

2002

DOI: 10.1007/0-306-47582-0

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Insulin & Related Proteins - Structure to Function and Pharmacology

Markus Leyck Dieken¹,

Matthias Federwisch²,

Pierre De Meyts³

Abstract: Activation Mechanism of fibroblast growth factor receptor tyrosine kinase revealed by crystal structure of fibroblast growth factor receptor ectodomain bound to fibroblast growth factor and heparin. 189 J. Grötzinger IL-6 type cytokine receptor complexes 201

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Cited by 3 publications

References 272 publications

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Hepatoselectivity and the evolution of insulin

Herring

Jones

Russell‐Jones

2013

Diabetes Obes Metab

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In spite of major developments in insulin production, purification, pharmaceutical formulation and methods of delivery, problems remain both in the day to day management of insulin-treated diabetes and with regard to its long-term complications. The risks of hypoglycaemia and weight gain are major concerns particularly for the patient, and the persistence of microvascular and premature macrovascular complications as the main causes of morbidity and mortality in both type 1 and type 2 diabetes is a constant reminder that our therapeutic and management strategies are inadequate. One clear and striking difference between currently available insulin treatments and normal physiology is the relative difference in exposure to insulin of the liver versus peripheral tissues. Hepatoselective insulin analogues have the potential to restore the normal hepatic to peripheral gradient in insulin action. Here, we discuss the possible therapeutic potential that such analogues may have over currently available insulin preparations. These benefits could include a lower risk of hypoglycaemia, less weight gain and a potential reduction in microvascular and macrovascular complications. We explore the evolution of insulin with hepatoselectivity in mind and possible strategies to create hepatoselective insulins.

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Hepatoselectivity and the evolution of insulin

Herring

Jones

Russell‐Jones

2013

Diabetes Obes Metab

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A Validated RP‐HPLC Method for the Determination of Recombinant Human Insulin in Bulk and Pharmaceutical Dosage Form

Moussa¹,

Farouk

Azzazy³

2010

Journal of Chemistry

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A modified RP-HPLC method was developed for the quantitative determination of recombinant human insulin in bulk and pharmaceutical dosage form with reduced retention time. Study of the effects of the column temperature, pH of the mobile phase and presence of vial additives (phenol andm-cresol), or impurities (A-21 Disamido) on the accuracy of the assay were assessed. Separation was achieved using a Hypersil BDS C-18 column and the mobile phase was composed of solution A (aqueous solution of 28.3 anhydrous Na2SO4g/L, pH 2.3) and solution B (28.5 g anhydrous Na2SO4g/L in 50:50 mixture of water and acetonitrile, pH 2.3) in a ratio 48:52 (v/v) at 45–50°C. The column temperature was 40°C, the flow rate was 1 mL/min and detection was performed at 216 nm. The procedures were validated according to international conference on harmonization (ICH) guidelines. Recovery study was done applying standard addition technique for further validation of the procedure. The retention time of recombinant human insulin was 19.7 min as compared to 29 min obtained by the reference method. Analytical conditions fluctuations or presence of vial additives or impurities did not show any significant effect on the accuracy of the method. The prepared standard insulin solution in 0.01 N HCl was found to be stable for 5 days. Statistical comparison showed no significant difference between the described method and reference method regarding the accuracy and precision. The modified method can be applied for routine quality control applications for determination of recombinant human insulin.

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How Nanoparticles Modify Adsorbed Proteins: Impact of Silica Nanoparticles on the Hemoglobin Active Site

Giraudon--Colas

Devineau

Marichal

et al. 2023

IJMS

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The adsorption of proteins on surfaces has been studied for a long time, but the relationship between the structural and functional properties of the adsorbed protein and the adsorption mechanism remains unclear. Using hemoglobin adsorbed on silica nanoparticles, we have previously shown that hemoglobin’s affinity towards oxygen increases with adsorption. Nevertheless, it was also shown that there were no significant changes in the quaternary and secondary structures. In order to understand the change in activity, we decided in this work to focus on the active sites of hemoglobin, the heme and its iron. After measuring adsorption isotherms of porcine hemoglobin on Ludox silica nanoparticles, we analyzed the structural modifications of adsorbed hemoglobin by X-ray absorption spectroscopy and circular dichroism spectra in the Soret region. It was found that upon adsorption, there were modifications in the heme pocket environment due to changes in the angles of the heme vinyl functions. These alterations can explain the greater affinity observed.

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Insulin & Related Proteins - Structure to Function and Pharmacology

Abstract: Activation Mechanism of fibroblast growth factor receptor tyrosine kinase revealed by crystal structure of fibroblast growth factor receptor ectodomain bound to fibroblast growth factor and heparin. 189 J. Grötzinger IL-6 type cytokine receptor complexes 201

Cited by 3 publications

References 272 publications

Hepatoselectivity and the evolution of insulin

Hepatoselectivity and the evolution of insulin

A Validated RP‐HPLC Method for the Determination of Recombinant Human Insulin in Bulk and Pharmaceutical Dosage Form

How Nanoparticles Modify Adsorbed Proteins: Impact of Silica Nanoparticles on the Hemoglobin Active Site

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