It has been shown that changes in physical properties of the membrane, such as surface charge or fluidity, affect the activity of embedded proteins. This is likely related to the presence of polar and/or aromatic residues that are often observed in the interfacial regions of those proteins. There mutation often results in modification of their activity. This raises the question: how do those polar and/or aromatic residues affect the orientation and dynamic behavior of transmembrane segments of proteins, thus affecting protein activity? Here we try to understand how electrostatic interactions affect transmembrane segments by use of simplified model systems consisting of KALP and WALP peptides. These peptides are composed of alternating alanine and leucine stretches flanked with lysines or tryptophans residues respectively. The peptides are embedded in vesicles containing Zwitterionic (DMPC), negatively charged (DMPG, DMPS, DMPA), or positively charged (DMTAP) lipids. The samples are then analyzed with 2H or 14N and 31P wide line solid state NMR methods. The results show that lipid composition affects transmembrane peptides in different ways depending on whether they are flanked with lysines or tryptophans. The results highlight the different properties of salt-bridge interactions and cation-pi interactions, and their possible implications in membrane protein activity.