Enhanced amyloid fibril formation of insulin in contact with catalytic hydrophobic surfaces
Independent thesis Basic level (degree of Bachelor), 10 points / 15 hpStudent thesis
The important protein hormone insulin, responsible for different kind of functions in our body but mainly storage of nutrients, has for a long time been used for treatment of diabetic patients. This important protein is both physically and chemically unstable. Especially during production where the insulin protein is exposed to unnatural environmental conditions such as acidic pH has this been causing problems since huge volumes of the product go to waste.
In the human body the environment for the protein is tolerable with normal body temperature and the right pH, but when the protein is commercially synthesised the environmental conditions are not ultimate. What happens during these unfavourable conditions is that the insulin starts to fibrillate. Meaning that linear, biologically inactive aggregates are formed. If then under these kinds of conditions such as high temperature and acidic pH, the insulin comes in contact with hydrophobic surfaces then the fibrillation of the protein goes even faster.
In the following experiment I am going to investigate if the experiments and conclusions done before, where different kinds of additives to insulin solutions have been used to enhance the amyloid fibrillation of insulin, are as effective as it has been proposed and I am going to prove that the presence of hydrophobic surfaces, such as coated silicon surfaces or glass and addition of preformed fibrils, so called seeds, increase amyloid fibrillation of the insulin protein under certain conditions, in comparison with the normal fibrillation under the same conditions.
Place, publisher, year, edition, pages
Institutionen för fysik, kemi och biologi , 2007. , 49 p.
amyloid fibril formation of insulin, enhanced fibril formation of insulin
IdentifiersURN: urn:nbn:se:liu:diva-10304ISRN: LITH-IFM-EX--07/1789--SEOAI: oai:DiVA.org:liu-10304DiVA: diva2:17043