Effect of protein lipidation on adsorption and surface-associated protein fibrillation
Lipidation of proteins is used in the pharmaceutical industry to improve the therapeutic efficacy of proteins. However, there is a limited knowledge on the physicochemical properties of these lipidated proteins. They may form irreversible multilayers upon adsorption onto solid surfaces, which in turn may catalyze the formation of surface-associated protein fibrillation. Fibrillation of proteins is considered to be a cause of multiple serious diseases. Insulin detemir, a human insulin analogue, with a fatty acid chain attached to the protein, was used as model compound, and compared to human insulin. Initial AFM and QCM-D results have shown that the lipid chain significant increases the initial adsorption and subsequent formation of fibrils onto hydrophobic surfaces. NR data can give a unique structural insight into the initial adsorbed (multi)-layers, density and thickness of these layers as well as for surface-associated fibrils. This structural insight will be of great significance in exploiting lipidation of proteins as a safe method to improve the therapeutic activity of proteins and understand the impact of the lipid chain in the adsorption process and subsequent fibrillation.
Please note that you will need to login with your ILL credentials to download the data.
Download DataThe recommended format for citing this dataset in a research publication is in the following format:
CARDENAS; Kathryn Browning; Richard A. Campbell; HEDEGAARD Sofie; Tania Kjellerup Lind; MARIC Selma and NORDSTROM Randi. (2016). Effect of protein lipidation on adsorption and surface-associated protein fibrillation. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-02-711
ILL has partnered with DataCite as the registration agency
for data persistent identifiers.