TY  - JOUR
A1  - Vacogne, Charlotte D.
A1  - Schopferer, Michael
A1  - Schlaad, Helmut
T1  - Physical Gelation of alpha-Helical Copolypeptides
JF  - Biomacromolecules : an interdisciplinary journal focused at the interface of polymer science and the biological sciences
N2  - 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.
Y1  - 2016
U6  - https://doi.org/10.1021/acs.biomac.6b00427
SN  - 1525-7797
SN  - 1526-4602
VL  - 17
SP  - 2384
EP  - 2391
PB  - American Chemical Society
CY  - Washington
ER  -