Calorimetric studies of the interaction between the lecithin and copolymers of L-lysine and L-leucine.

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The interaction between the dimyristoyl phosphatidylcholine (DMPC) bilayers and aqueous copolymers of L-lysine and L-leucine was investigated by means of differential scanning calorimetry. None of the copolymers had any effects on the transition temperature of DMPC, irrespective of the lysine/leucine ratio, although the pretransition peak disappeared. The transition enthalpy did not appreciably change upon the addition of copolymers if the leucine fraction was small (<0.25), but it remarkably decreased upon the addition of a copolymer with a large leucine content (>0.3). The latter case suggests the penetration of copolymers into the hydrophobic region (hydrocarbon-chain region) of DMPC as a result of the hydrophobic effect of leucine residues. On the contrary, copolymers of a small leucine content can penetrate at most into the polar region of DMPC because of the electric charge derived from lysine residues, indicating the effect of the copolymer composition on the penetrability of a copolymer into lipid layers.
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