{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T13:01:01Z","timestamp":1791378061338,"version":"4.3.2"},"reference-count":126,"publisher":"MDPI AG","issue":"23","license":[{"start":{"date-parts":[[2025,11,24]],"date-time":"2025-11-24T00:00:00Z","timestamp":1763942400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Center for Biomedical Photonics","award":["D01-101\/2025"],"award-info":[{"award-number":["D01-101\/2025"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Abnormal accumulation of amyloid-beta (A\u03b2) peptides in the brain is a hallmark of Alzheimer\u2019s disease (AD). Importantly, the peripheral blood cells are also exposed to the effects of pathological peptides that accumulate in AD. Herein, the interaction of A\u03b242 oligomers (A\u03b242) with human red blood cells (RBCs) and erythrocyte ghosts as in vitro models for AD is studied combining fluorescence spectroscopy, fluorescence microscopy, and electrokinetics. The binding of A\u03b242 to RBCs was evidenced by the use of a fluorescent-labeled peptide. The membrane lipid order increased with the increase in both the A\u03b242 concentration and the incubation time, creating a lipid\u2013protein microenvironment characterized by higher molecular order and reduced heterogeneity in RBC membranes compared to control conditions. Notably, the increase in lipid order was less pronounced in erythrocyte ghosts than in intact RBCs. Furthermore, the \u03b6-potential measurements revealed A\u03b242 induced alteration of the surface potential of RBCs in a concentration- and time-dependent manner, with freshly isolated RBCs exhibiting a highly negative potential that became increasingly negative at higher A\u03b242 concentrations. These findings suggest that A\u03b242 not only impacts neuronal function but also significantly alters the physical properties of RBCs that might compromise their function, potentially contributing to the systemic effects observed in AD.<\/jats:p>","DOI":"10.3390\/ijms262311361","type":"journal-article","created":{"date-parts":[[2025,11,25]],"date-time":"2025-11-25T08:50:20Z","timestamp":1764060620000},"page":"11361","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Amyloid \u03b2 Peptide Modifies Membrane Architecture and Surface Electrostatic Properties of Human Red Blood Cells"],"prefix":"10.3390","volume":"26","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-2089-3603","authenticated-orcid":false,"given":"Galya","family":"Staneva","sequence":"first","affiliation":[{"name":"Institute of Biophysics and Biomedical Engineering, Bulgarian Academy of Sciences, \u201cAcad. G. Bonchev\u201d Str., Block 21, 1113 Sofia, Bulgaria"},{"name":"Department of Endocrinology, Faculty of Medicine, Medical University\u2014Sofia, \u201cAcad. Ivan Geshov\u201d Blvd. No. 15, 1000 Sofia, Bulgaria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0753-8084","authenticated-orcid":false,"given":"Vesela","family":"Yordanova","sequence":"additional","affiliation":[{"name":"Institute of Biophysics and Biomedical Engineering, Bulgarian Academy of Sciences, \u201cAcad. G. Bonchev\u201d Str., Block 21, 1113 Sofia, Bulgaria"},{"name":"Department of Endocrinology, Faculty of Medicine, Medical University\u2014Sofia, \u201cAcad. Ivan Geshov\u201d Blvd. No. 15, 1000 Sofia, Bulgaria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Avgustina","family":"Danailova","sequence":"additional","affiliation":[{"name":"Institute of Biophysics and Biomedical Engineering, Bulgarian Academy of Sciences, \u201cAcad. G. Bonchev\u201d Str., Block 21, 1113 Sofia, Bulgaria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana-Maria","family":"Marinovska","sequence":"additional","affiliation":[{"name":"Institute of Biophysics and Biomedical Engineering, Bulgarian Academy of Sciences, \u201cAcad. G. Bonchev\u201d Str., Block 21, 1113 Sofia, Bulgaria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6112-884X","authenticated-orcid":false,"given":"Andr\u00e1s","family":"D\u00e9r","sequence":"additional","affiliation":[{"name":"Institute of Biophysics, HUN-REN Biological Research Centre, H-6701 Szeged, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6851-4516","authenticated-orcid":false,"given":"Stefka G.","family":"Taneva","sequence":"additional","affiliation":[{"name":"Institute of Biophysics and Biomedical Engineering, Bulgarian Academy of Sciences, \u201cAcad. G. 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