Gecko’s feet, lotus leaves, blue butterfly wings, spider’s silk, fireflies, mother-of-pearl…. All
these wonders of nature, which traditionally filled the pages of natural history magazines
have attracted the attention of materials scientists over the past decades. They have often
been presented as models to design and engineer optimal structures. And this renewed
interest in natural systems has undoubtedly brought about innovating strategies in
chemistry, materials science and nanotechnology....
Most of the biochemical and biophysical processes of proteins take place
at membranes, and are thus under the influence of strong local electric
fields, which are likely to affect the structure as well as the reaction mecha-nism and dynamics.
Depth of bilayer penetration and effects on lipid mobility
conferred by themembrane-active peptidesmagainin, melit-tin, and a hydrophobic helical sequence KKA(LA)7KK
(denoted KAL), were investigated by colorimetric and
time-resolved fluorescence techniques in biomimetic phos-pholipid/poly(diacetylene)vesicles. The experiments dem-onstrated that the extent of bilayer permeation and peptide
localization within the membrane was dependent upon the
bilayer composition, and that distinct dynamic modifica-tions were induced by each peptide within the head-group
environment of the phospholipids....
The phospholipase D (PLD) fromStreptomyces chromo-fuscusbelongs to the superfamily of PLDs. All the enzymes
included in this superfamily are able to catalyze both
hydrolysis and transphosphatidylation activities. However,
S. chromofuscusPLD is calcium dependent and is often
described as an enzyme with weak transphosphatidylation
activity. S. chromofuscus PLD-catalyzed hydrolysis of
phospholipids in aqueous medium leads to the formation of