Resumen:
e 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 α-helix perpendicular to the interface. The α-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/lip