Abstract
We investigated the effects of a de novo designed peptide, WLFLLKKK (peptide-1) andLa3+, which can bind with the electrically neutral lipid membrane interface,on the stability of the phosphatidylcholine (PC) membrane in theLα phase and that of the liquid-ordered (lo) phase membranes. The results of spacing of themultilamellar vesicle and shape changes of the giant unilamellar vesicle (GUV)indicate that the peptide-1 can be partitioned into the membrane interface in theLα phase but not intothat in the lo phase. La3+ induced shape changes of GUVs of the lo phase membrane, which are the same as those of GUVs in theLα phase. This indicatesthat the binding of La3+ induced an increase in the lateral compression pressure of the membrane, which decreased thesurface area of the membrane in the lo phase. The difference of the membrane interface between theLα phase and the lo phase is discussed.
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