Insulin analog with additional disulfide bond has increased stability and preserved activity.

@article{Vinther2013InsulinAW,
  title={Insulin analog with additional disulfide bond has increased stability and preserved activity.},
  author={Tine N. Vinther and Mathias Norrman and Ulla Ribel and Kasper Huus and Morten Schlein and Dorte Bjerre Steensgaard and Thomas {\AA}skov Pedersen and Ingrid Pettersson and S. Ludvigsen and Thomas L. Kjeldsen and Knud J Jensen and Franti{\vs}ek Hub{\'a}lek},
  journal={Protein science : a publication of the Protein Society},
  year={2013},
  volume={22 3},
  pages={296-305}
}
Insulin is a key hormone controlling glucose homeostasis. All known vertebrate insulin analogs have a classical structure with three 100% conserved disulfide bonds that are essential for structural stability and thus the function of insulin. It might be hypothesized that an additional disulfide bond may enhance insulin structural stability which would be highly desirable in a pharmaceutical use. To address this hypothesis, we designed insulin with an additional interchain disulfide bond in… CONTINUE READING

From This Paper

Topics from this paper.
10 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 10 extracted citations

Similar Papers

Loading similar papers…