Polymer stabilized lipid-protein nanoparticles have become invaluable tools in membrane biology since they can isolate individual proteins with their surrounding lipids. These nanoparticles, termed nanodiscs, have historically relied on membrane scaffolding proteins, but can now be formed using amphipathic copolymers that directly intercalate into membranes. Since copolymeric nanodiscs are formed directly from membranes without requiring detergent solubilization, they have been presumed to retain the native membrane environment, but this assumption has not been thoroughly tested. To test if native membrane lipid packing is retained in styrene-maleic acid (SMA) and diisobutylene-maleic acid (DIBMA) stabilized nanodiscs, lipid packing was analyzed using solvatochromic dyes Laurdan, C-Laurdan, and Pro12A. SMA and DIBMA copolymeric nanodiscs were formed from membranes increasing in complexity from single and binary lipid mixture, to biomimetic ternary mixtures composed of palmitoyl-sphingomyelin (PSM), 1-palmitoyl-2-oleoylphosphatidylcholine (POPC), and cholesterol, and ultimately to mammalian cellular membranes. For all synthetic model membranes, lipid packing of fluid-disordered membranes was significantly increased in both SMA and DIBMA nanodiscs compared to intact membranes, with DIBMA being the least perturbing. In contrast, lipid packing in ordered membranes was unaffected. For cellular membranes, lipid packing was also higher inside nanodiscs than in native membranes. Our data challenges the assumption that native membrane properties are retained inside nanodiscs. While not maintaining native membrane properties, nanodiscs can be useful models for studying protein-lipid interactions, as they are composed of membrane lipids. Interestingly, nanodiscs can exchange lipids through collisions, allowing tuning of their lipid compositions. We used this capability to analyze the preferred surrounding lipidome of multi-pass transmembrane proteins. Altogether, our studies demonstrate that copolymeric nanodiscs have different properties to those of intact membranes, but they are useful models in studying the paralipidomes of membrane proteins.