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Here, polymersomes are self\u2010assembled via film rehydration, solvent exchange, and polymerization\u2010induced self\u2010assembly using five different block copolymers. The hydrophilic blocks are composed of anti\u2010fouling polymers, poly(ethylene glycol) (PEG) or poly(2\u2010methyl\u20102\u2010oxazoline) (PMOXA), and all the data is benchmarked to PEGylated \u201cstealth\u201d liposomes. High colloidal stability in human plasma (HP) is confirmed for all but two tested nanovesicles. In situ fluorescence correlation spectroscopy measurements are then performed after incubating unlabeled nanovesicles with fluorescently labeled HP or the specific labeled plasma proteins, human serum albumin, and clusterin (apolipoprotein J). The binding of HP to PMOXA\u2010polymersomes could explain their relatively short circulation times found previously. In contrast, PEGylated liposomes also interact with HP but accumulate high levels of clusterin, providing them with their known prolonged circulation time. The absence of significant protein binding for most PEG\u2010polymersomes indicates mechanistic differences in protein interactions and associated downstream effects, such as cell uptake and circulation time, compared to PEGylated liposomes. These are key observations for bringing polymersomes closer to clinical translation and highlighting the importance of such comparative studies.<\/jats:p>","DOI":"10.1002\/mabi.202200424","type":"journal-article","created":{"date-parts":[[2022,11,30]],"date-time":"2022-11-30T06:09:31Z","timestamp":1669788571000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["Differences in Human Plasma Protein Interactions between Various Polymersomes and Stealth Liposomes as Observed by Fluorescence Correlation Spectroscopy"],"prefix":"10.1002","volume":"23","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4868-9364","authenticated-orcid":false,"given":"Adrian","family":"Najer","sequence":"first","affiliation":[{"name":"Department of Materials Department of Bioengineering and Institute of Biomedical Engineering Imperial College London  London SW7 2AZ 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