Structural characterization of the model amphipathic peptide Ac-LKKLLKLLKKLLKL-NH2 in aqueous solution and with 2,2,2-trifluoroethanol and 1,1,1,3,3,3-hexafluoroisopropanol

Autor:	Avijita Jain, Garry W. Buchko, Matthew L. Reback, Wendy J. Shaw
Rok vydání:	2013
Předmět:	chemistry.chemical_classification Circular dichroism Aqueous solution Stereochemistry Organic Chemistry Size-exclusion chromatography Peptide General Chemistry Nuclear magnetic resonance spectroscopy Catalysis chemistry.chemical_compound 2 2 2-Trifluoroethanol chemistry Tetramer Amphiphile
Zdroj:	Canadian Journal of Chemistry. 91:406-413
ISSN:	1480-3291 0008-4042
DOI:	10.1139/cjc-2012-0429
Popis:	Short-chain amphipathic peptides are promising components in the new generation of engineered biomaterials. The model 14-residue leucine–lysine peptide Ac-LKKLLKLLKKLLKL-NH2 (LKα) is one such amphipathic peptide. In dilute aqueous solution (c) showed that the self-assembled LKα complexes contained three to five peptides. Removing the N-terminal acetyl group prevents LKα from forming helices and self-associating at high NaCl and peptide concentrations. This more detailed characterization of the structural and physical properties of LKα over a greater range of peptide concentrations and in the presence of fluorinated alcohols will assist the design of biomaterials containing amphipathic peptides and guide the ability to control self-assembly.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::8613ea53b018d4a96ee967128a02148b https://doi.org/10.1139/cjc-2012-0429 Zobrazit plný text záznamu Plný text ve formátu PDF