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. 2012 Dec 5;103(11):2295–2303. doi: 10.1016/j.bpj.2012.08.053

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© 2012 by the Biophysical Society.

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Adsorption isotherms obtained from ellipsometry represent coiled-coil formation of E-peptides binding to K-LPs. Bilayers were formed from DOPC/MCCDOPE 97:3, and K-peptides were then coupled covalently to the surface. The isotherm was measured by subsequently increasing the added E-peptide concentration. (A) Parallel coiled-coil formation. Solid circles: LP-K3Cys + E3Cys; solid triangles: LP-i-K3Cys + i-E3Cys; data were fitted according to Eq. 2 (fits: gray line). (B) Antiparallel coiled-coil formation. Open circles: LP-K3Cys + i-E3Cys; open triangles: LP-i-K3Cys + E3Cys. Data were fitted according to Langmuir for LP-i-K3Cys + E3Cys, and a Bragg-Williams isotherm (Eq. 3) was used for LP-K3Cys + i-E3Cys (fits: gray line).