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In this work, we focus on the membrane\u2010binding properties of P2 and its Charcot\u2013Marie\u2013Tooth disease variants. Experiments were carried out on lipid monolayers at the air\u2013water interface as a membrane model system, with the lipid composition of the cytoplasmic leaflet of myelin. Our study provides quantitative data on the membrane affinity of P2 and its disease\u2010linked or structure\u2010based missense variants toward the native lipid membrane and shows affinity differences due to single P2 point mutations. Phospholipid monolayer surface pressure measurements are supported by epifluorescence microscopy, which not only shows the adhesive property of all P2 variants but also the complex cross\u2010linking property of the wild\u2010type P2. An analysis of transcriptomics databases confirms expression of P2 in human, but not mouse, central nervous system nonneuronal cells. Taken together, our work further confirms the role of P2 in binding myelin\u2010like lipid membranes as well as its direct effects on lipid membrane properties.<\/jats:p>","DOI":"10.1002\/cbic.202500947","type":"journal-article","created":{"date-parts":[[2026,4,21]],"date-time":"2026-04-21T07:21:36Z","timestamp":1776756096000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Human Peripheral Myelin Protein 2 and Charcot\u2013Marie\u2013Tooth Disease or Structural Missense Variants Show Different Binding to Myelin\u2010Like Lipid Monolayers"],"prefix":"10.1002","volume":"27","author":[{"given":"Florian Arndt","family":"Sch\u00f6ffmann","sequence":"first","affiliation":[{"name":"Institute of Chemistry Physical Chemistry \u2013 Complex Self-Organizing Systems Martin Luther University Halle-Wittenberg  Halle (Saale) Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Md Abdus 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