Author(s):
Castro, Vânia I. B. ; Carvalho, Carina Martins ; Fernandes, Rui D. V. ; Pereira-Lima, Sílvia M. M. A. ; Castanheira, Elisabete M. S. ; Costa, Susana P. G.
Date: 2016
Persistent ID: https://hdl.handle.net/1822/39800
Origin: RepositóriUM - Universidade do Minho
Project/scholarship:
info:eu-repo/grantAgreement/FCT/5876-PPCDTI/118389/PT
;
info:eu-repo/grantAgreement/FCT/COMPETE/132953/PT;
info:eu-repo/grantAgreement/FCT/COMPETE/132974/PT;
info:eu-repo/grantAgreement/FCT/COMPETE/118389/PT;
Subject(s): alpha,alpha-Dialkylglycines; Peptaibolin; Membrane permeating peptides; Model membranes; Fluorescence spectroscopy; Science & Technology; Ciências Naturais::Ciências Físicas
Description
Analogues of Peptaibolin, a peptaibol with antibiotic activity, incorporating α,α-dialkylglycines (Deg, Dpg, and Ac6c) at selected positions were synthesised by MW-SPPS and fully characterized. A control analogue incorporating L-alanine was also prepared. The native peptide and the analogues were studied by fluorescence spectroscopy for their membrane permeating activity. Small unilamellar vesicles (SUVs) of egg phosphatidylcholine/ cholesterol (70:30) containing an encapsulated fluorescence probe (6-carboxyfluorescein) were used as membrane models. The assays of carboxyfluorescein release from SUVs upon peptide addition showed that Peptaibolin-Dpg and Peptaibolin-Ac6c are the most active peptides. These results indicate that the structure of the α,α-dialkylglycines is crucial for the membrane permeating ability of these Peptaibolin analogues.
Fundação para a Ciência e Tecnologia (Portugal)
The authors acknowledge Fundação para a Ciência e a Tecnologia (Portugal) and FEDERCOMPETE-QREN-EU for financial support through projects PTDC/QUI-BIQ/118389/2010 (FCOMP-01-0124-FEDER-020906), PEst-C/QUI/UI0686/2013 (F-COMP-01-0124-FEDER- 037302), PEst-C/FIS/UI0607/2013 (F-COMP-01-0124-FEDER-022711) and the portuguese NMR network (PTNMR, Bruker Avance III 400-Univ. Minho).
