FIDELIO GERARDO DANIEL
Artículos
Título:
Biophysical properties of a synthetic transit peptide from wheat chroloplast ribulose 1,5-bisphosphate carboxylase.
Autor/es:
AMBROGGIO E.E,; AUSTEN B.,; FIDELIO G.D
Editorial:
JOHN WILEY & SONS LTD
Referencias:
Año: 2007 vol. 13 p. 245 - 245
Resumen:
p class="abstract">The surface properties of pure RuBisCo transit peptide (RTP) and its interaction with zwitterionic, anionic phospholipids and chloroplast lipids were studied by using the Langmuir monolayer technique. Pure RTP is able to form insoluble films and the observed surface parameters are compatible with an alpha-helix perpendicular to the interface. The alpha-helix structure tendency was also observed by using transmission FT-IR spectroscopy in bulk system of a membrane mimicking environment (SDS). On the other hand, RTP adopts an unordered structure in either aqueous free interface or in the presence of vesicles composed of a zwitterionic phospholipid (POPC). Monolayer studies show that in peptide/lipid mixed monolayers, RTP shows no interaction with zwitterionic phospholipids, regardless of their physical state. Also, with the anionic POPG at high peptide ratios RTP retains its individual surface properties and behaves as an immiscible component of the peptide/lipid mixe