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Physical Gelation of alpha-Helical Copolypeptides

  • 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,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.zeige mehrzeige weniger

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Metadaten
Verfasserangaben:Charlotte D. Vacogne, Michael Schopferer, Helmut SchlaadORCiDGND
DOI:https://doi.org/10.1021/acs.biomac.6b00427
ISSN:1525-7797
ISSN:1526-4602
Pubmed ID:https://pubmed.ncbi.nlm.nih.gov/27233111
Titel des übergeordneten Werks (Englisch):Biomacromolecules : an interdisciplinary journal focused at the interface of polymer science and the biological sciences
Verlag:American Chemical Society
Verlagsort:Washington
Publikationstyp:Wissenschaftlicher Artikel
Sprache:Englisch
Jahr der Erstveröffentlichung:2016
Erscheinungsjahr:2016
Datum der Freischaltung:22.03.2020
Band:17
Seitenanzahl:8
Erste Seite:2384
Letzte Seite:2391
Fördernde Institution:International Max Planck Research School (IMPRS) on "Multiscale Biosystems"
Organisationseinheiten:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Chemie
Peer Review:Referiert
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