Synthetic peptides corresponding to the calmodulin-binding domains of skeletal muscle myosin light chain kinase and human erythrocyte calcium pump interact with and permeabilize liposomes and cell membranes
- 1 July 1993
- journal article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 32 (26) , 6721-6728
- https://doi.org/10.1021/bi00077a027
Abstract
Synthetic calmodulin-binding (CaM-binding) peptides (CBPs) representing CaM-binding domains of Ca2+/CaM-dependent enzymes have been reported to interfere with the activity of the melanocyte-stimulating hormone (MSH) receptor function in melanoma cells [Gerst, J. E., & Salomon, Y. (1988) J. Biol. Chem. 263, 7073-7078]. We postulated that membrane lipids may play an important role in the mode of action of CBPs on cells. We therefore tested the ability of CBPs to interact with membrane bilayers. Using artificial phospholipid vesicles, or M2R melanoma cells and cell membranes derived therefrom, as models, we report here that synthetic peptides representing the CaM-binding domains of skeletal muscle myosin light chain kinase (M5) and the human erythrocyte calcium pump (C28W), as well as other CBPs, interact with lipid bilayers and cell membranes. Significant interactions of CBPs with the lipid bilayer were detected in both model systems. M5 and C28W were found to partition into the lipid bilayer of melanoma cell membranes and soybean lecithin vesicles, and surface partition constants obtained (for the liposome model) were in the range 10(3)-10(4) M-1. In addition, C28W and its N-modified NBD derivative were found to inhibit [125I]iodo-[Nle4,D-Phe7]alpha MSH binding to cultured M2R melanoma cells. These and other CBPs were also found to induce the release of cations and calcein from liposomes, suggesting that the interaction of CBPs with the lipid bilayer increases membrane permeability.(ABSTRACT TRUNCATED AT 250 WORDS)Keywords
This publication has 37 references indexed in Scilit:
- The actions of melittin on membranesPublished by Elsevier ,2003
- Identification of two domains which mediate the binding of activating phospholipids to the plasma‐membrane Ca2+ pumpEuropean Journal of Biochemistry, 1992
- The effect of a membrane potential on the interaction of mastoparan X, a mitochondrial presequence, and several regulatory peptides with phospholipid vesiclesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1991
- Peptide binding to lipid membranes. Spectroscopic studies on the insertion of a cyclic somatostatin analog into phospholipid bilayersBiochimica et Biophysica Acta (BBA) - Biomembranes, 1991
- Melittin binding to mixed phosphatidylglycerol/phosphatidylcholine membranesBiochemistry, 1990
- Synthetic peptides based on the calmodulin-binding domain of myosin light chain kinase inhibit activation of other calmodulin-dependent enzymesBiochemical and Biophysical Research Communications, 1988
- Preferred conformation, orientation, and accumulation of dynorphin A-(1-13)-tridecapeptide on the surface of neutral lipid membranesBiochemistry, 1985
- The amphipathic helix: its possible role in the interaction of glucagon and other peptide hormones with membrane receptor sitesTrends in Biochemical Sciences, 1983
- Ca2+-dependent high-affinity complex formation between calmodulin and melittinBiochemical Journal, 1983
- Serum-induced leakage of liposome contentsBiochimica et Biophysica Acta (BBA) - Biomembranes, 1980