@article{VacogneSchopfererSchlaad2016,
  author    = {Vacogne, Charlotte D. and Schopferer, Michael and Schlaad, Helmut},
  title     = {Physical Gelation of alpha-Helical Copolypeptides},
  series = {Biomacromolecules : an interdisciplinary journal focused at the interface of polymer science and the biological sciences},
  volume    = {17},
  journal   = {Biomacromolecules : an interdisciplinary journal focused at the interface of polymer science and the biological sciences},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {1525-7797},
  doi       = {10.1021/acs.biomac.6b00427},
  pages     = {2384 -- 2391},
  year      = {2016},
  abstract  = {Owing to its rod-like alpha-helical secondary structure, the synthetic polypeptide poly(gamma-benzyl-L-glutamate) (PBLG) can form physical and thermoreversible gels in helicogenic solvents such as toluene. The versatility of PBLG can be increased by introducing functionalizable comonomers, such as allylglycine (AG). In this work we examined the secondary structure of PBLG and a series of statistical poly(gamma-benzyl-L-glutamate-co-allylglycine) copolypeptides, varying in composition and chain length, by circular dichroism (CD), Fourier-transform infrared (FTIR) and Raman spectroscopy, and wide-angle X-ray scattering (WAXS). The secondary structure of PBLG and the copolypeptides presented dissimilarities that increased with increasing AG molar fraction, especially when racemic AG units were incorporated. The physical gelation behavior of these copolypeptides was analyzed by temperature-sweep H-1 NMR and rheological measurements. The study revealed that both copolypeptide composition and chain length affected secondary structure, gelation temperature, and gel stiffness.},
  language  = {en}
}