Study of the Aggregation of Insulin Glargine by Light Scattering
| Autor: | V. Villari, S. Coppolino, R. Coppolino |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Absorption (pharmacology)
medicine.medical_specialty Light Chemistry Pharmaceutical medicine.medical_treatment Molecular Sequence Data Insulin Glargine Pharmaceutical Science Protein aggregation light scattering Light scattering protein aggregation particle sizing Internal medicine medicine Human insulin Insulin Scattering Radiation Amino Acid Sequence Particle Size colloid Nanotubes Insulin glargine Chemistry Temperature Controlled release Low ionic strength Insulin Long-Acting Pharmaceutical Solutions Endocrinology Solubility Biophysics Algorithms medicine.drug |
| Zdroj: | Journal of pharmaceutical sciences 95 (2006): 1029–1034. doi:10.1002/jps.20609 info:cnr-pdr/source/autori:R. Coppolino, S. Coppolino, V. Villari/titolo:Study of the aggregation of insulin glargine by light scattering/doi:10.1002%2Fjps.20609/rivista:Journal of pharmaceutical sciences/anno:2006/pagina_da:1029/pagina_a:1034/intervallo_pagine:1029–1034/volume:95 |
| ISSN: | 0022-3549 |
| DOI: | 10.1002/jps.20609 |
| Popis: | Insulin glargine (Lantus®, Aventis Pharma, Deutschland, GmbH) is a new long-acting human insulin analog. Structural modification of the insulin molecule at two sites alters its pH, causing insulin glargine to precipitate in the neutral environment of subcutaneous tissue and to form a depot that is slowly absorbed into the bloodstream. In this paper insulin glargine aggregation is investigated by light scattering. This study shows that, in a physiologic-like pH (even at low ionic strength) conditions, aggregation phenomena occur, giving rise to compact structures with radius of hundreds of nanometers. The aggregation of insulin glargine can be responsible for its slow in situ absorption allowing for a more controlled release. |
| Databáze: | OpenAIRE |
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