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VPDLLADLLK is a synthetic decapeptide, which shows a difference in conformation in various environments. Circular dichroism spectral studies show that it exists in an unordered conformation in the aqueous phase, and in dimyristoylphosphatidylcholine (DMPC) lipid bilayer, it exhibits an alpha-helical structure. The membrane property modification due to the peptide incorporation has been studied by using differential scanning calorimetry and fluorescence spectroscopy. With incorporation of the peptide the average steady-state anisotropy of DPH in the membrane decreases slightly in the gel state but remains more or less the same in the liquid crystalline state. The peptide incorporation causes a shift in the phase-transition temperature from 23 to 26 degrees C for 15 mol% and 29 degrees C for 30 mol% of the peptide, which is accompanied by a decrease in the sharpness and a broadening of the DSC thermogram. This preferential stabilization of the more ordered gel phase by the peptide could be due to the hydrophobic mismatch between the length of the peptide and the length of the hydrophobic segment of the DMPC bilayer. Copyright 2001 Academic Press.