Ligand-binding proteins show an increasing interest as drug carriers and de
livery systems [Wolf FA, Brett GM. Pharmacol Rev, 2000;52:207-36]. The wide
binding properties of plant non-specific lipid transfer proteins such as L
TP1 also offer many unexplored possibilities for such a task. In the presen
t paper, by using intrinsic tyrosine LTP1 fluorescence, we survey, for the
first time, the binding of wheat LTP1 with various ligands having cosmetic
or pharmaceutical applications. LTP1 was found to bind skin lipids such as
sphingosine, sphingomyelin, and cerebroside with an affinity of about one m
icromolar, low enough to allow a slow release of these molecules. Ether pho
spholipids and an azole derivative BD56 having antitumoral and/or antileish
mania properties were also shown to bind LTP1 with similar affinity. Finall
y, amphotericin B, which is widely used as an antifungal drug, was shown to
form a complex with LTP1, although no affinity could be determined. This b
inding study is a prerequisite for further work aimed at developing applica
tions in LTP-mediated transport and controlled release of low molecular wei
ght drugs. (C) 2001 Elsevier Science Inc. All rights reserved.