Binding of two mono-acylated lipid monomers by the barley lipid transfer protein, LTP1, as viewed by fluorescence, isothermal titration calorimetry and molecular modelling

Molecular properties of food allergens

“…36,37 It can actually accommodate 2 lipid molecules, which, on the basis of molecular modeling, appear to lay side by side in the tunnel. 18 These properties seem to be a general feature of nsLTPs and might be related to their putative role in plants in transporting lipids involved in the synthesis of waxy cutin and suberin layers in outer plant tissues in seeds and pollen. The 3-dimensional scaffold found in nsLTPs is characteristic of the prolamin superfamily, and it is becoming evident that in some forms of the protein (eg, AceAMP1 from onion roots), the tunnel has been lost, along with the ability to bind lipids, the cavity being filled up with tryptophan and phenylalanine side chains.…”

“…Thus the thermostability of blactoglobulin (bLg) increases on lipid binding, 17 as does that of the nsLTP of wheat. 18 These properties are described in more detail below for several notable allergens, including the major fish allergen parvalbumin, the cow's milk allergens casein and bLg, and the nsLTPs and Bet v 1 homologues found in a variety of plant foods.…”

“…Wheat nsLTP binds a range of fatty acids and phospholipids varying in chain length with high affinity, with dissociation constants in the order of 0.2 to 0.3 mM, depending on the lipid. 18,35 The cavity is highly plastic and can bind a wide range of lipophilic molecules, including sphingolipids, prostaglandins, amphoteracin B, and other hydrophobic drugs. 36,37 It can actually accommodate 2 lipid molecules, which, on the basis of molecular modeling, appear to lay side by side in the tunnel.…”

Computational study of ligand binding in lipid transfer proteins: Structures, interfaces, and free energies of protein‐lipid complexes

“…[4,[9][10][11][12][13][14][15][16][17][18] Crystal structures of maize nsLTP complexed with palmitate [10] and with an array of fatty acids ranging from C10 to C18, [11] wheat nsLTP in complex with lyso-myristoyl-phosphatidyl-choline (LMPC), [12] rice nsLTP complexed with stearate, [13] and peach nsLTP with bound laurate [14] have been determined by X-ray crystallography. Solution NMR structures of wheat nsLTP complexed with 1,2-dimyristoyl-phosphatidyl-glycerol [15] and with prostaglandin B 2 , [16] and barley nsLTP in complex with palmitoyl coenzyme A [17] and palmitate [18] have also been reported.…”

Electrochemical Study of the Lipid‐Transfer Protein

“…The compact structure of LTP comprises four ahelices stabilized by four disulfide bonds and a well defined C-terminal arm with no regular secondary structure [8]. A hydrophobic cavity within the protein can adapt its volume to bind a variety of lipids and hydrophobic molecules such as fatty acids, acyl-CoA, a lyso derivative and phospholipids [9].…”