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  Physical gelation of α-helical copolypeptides

Vacogne, C. D., Schopferer, M., & Schlaad, H. (2016). Physical gelation of α-helical copolypeptides. Biomacromolecules, 17(7), 2384-2391. doi:10.1021/acs.biomac.6b00427.

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Vacogne, Charlotte Dominique1, Author              
Schopferer, Michael, Author
Schlaad, Helmut, Author
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1Kolloidchemie, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863288              

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 Abstract: Owing to its rod-like α-helical secondary structure, the synthetic polypeptide poly(γ-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(γ-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 which 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 1H NMR and rheological measurements. The study revealed that both copolypeptide composition and chain length affected secondary structure, gelation temperature, and gel stiffness.

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 Dates: 2016-05-272016
 Publication Status: Published in print
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 Identifiers: DOI: 10.1021/acs.biomac.6b00427
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Title: Biomacromolecules
  Other : Biomacromolecules
Source Genre: Journal
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Publ. Info: Washington, DC : American Chemical Society
Pages: - Volume / Issue: 17 (7) Sequence Number: - Start / End Page: 2384 - 2391 Identifier: ISSN: 1525-7797