| Title |
Study of insulin aggregation and fibril structure under different environmental conditions / |
| Authors |
Žiaunys, Mantas ; Mikalauskaitė, Kamilė ; Sakalauskas, Andrius ; Smirnovas, Vytautas |
| DOI |
10.3390/ijms25179406 |
| Full Text |
|
| Is Part of |
International journal of molecular sciences: special issue: The role of environment in amyloid aggregation: 3rd edition.. Basel : MDPI. 2024, vol. 25, iss. 17, art. no. 9406, p. [1-17].. eISSN 1422-0067 |
| Keywords [eng] |
amyloids ; environmental conditions ; fibril structure ; insulin ; protein aggregation |
| Abstract [eng] |
Protein amyloid aggregation is linked with widespread and fatal neurodegenerative disorders as well as several amyloidoses. Insulin, a small polypeptide hormone, is associated with injection-site amyloidosis and is a popular model protein for in vitro studies of amyloid aggregation processes as well as in the search for potential anti-amyloid compounds. Despite hundreds of studies conducted with this specific protein, the procedures used have employed a vast array of different means of achieving fibril formation. These conditions include the use of different solution components, pH values, ionic strengths, and other additives. In turn, this variety of conditions results in the generation of fibrils with different structures, morphologies and stabilities, which severely limits the possibility of cross-study comparisons as well as result interpretations. In this work, we examine the condition-structure relationship of insulin amyloid aggregation under a range of commonly used pH and ionic strength conditions as well as solution components. We demonstrate the correlation between the reaction solution properties and the resulting aggregation kinetic parameters, aggregate secondary structures, morphologies, stabilities and dye-binding modes. |
| Published |
Basel : MDPI |
| Type |
Journal article |
| Language |
English |
| Publication date |
2024 |
| CC license |
|
