Oligomerization of a Glucagon-like Peptide 1 Analog: Bridging Experiment and Simulations.

@article{Frederiksen2015OligomerizationOA,
  title={Oligomerization of a Glucagon-like Peptide 1 Analog: Bridging Experiment and Simulations.},
  author={Tine Maja Frederiksen and Pernille S{\o}nderby and Line A Ryberg and Pernille Harris and Jens T Bukrinski and Anne M Scharff-Poulsen and Maria Northved Elf-Lind and G{\"u}nther H J Peters},
  journal={Biophysical journal},
  year={2015},
  volume={109 6},
  pages={
          1202-13
        }
}
The glucagon-like peptide 1 (GLP-1) analog, liraglutide, is a GLP-1 agonist and is used in the treatment of type-2 diabetes mellitus and obesity. From a pharmaceutical perspective, it is important to know the oligomerization state of liraglutide with respect to stability. Compared to GLP-1, liraglutide has an added fatty acid (FA) moiety that causes oligomerization of liraglutide as suggested by small-angle x-ray scattering (SAXS) and multiangle static light scattering (MALS) results. SAXS data… CONTINUE READING
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