{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,13]],"date-time":"2026-09-13T05:05:12Z","timestamp":1789275912221,"version":"build-2803163510"},"reference-count":39,"publisher":"Wiley","issue":"17","license":[{"start":{"date-parts":[[2026,8,31]],"date-time":"2026-08-31T00:00:00Z","timestamp":1788134400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,8,31]],"date-time":"2026-08-31T00:00:00Z","timestamp":1788134400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100001659","name":"German Research Foundation","doi-asserted-by":"publisher","award":["564132680"],"award-info":[{"award-number":["564132680"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"German Research Foundation","doi-asserted-by":"publisher","award":["SFB 1756 \u2013 550938463"],"award-info":[{"award-number":["SFB 1756 \u2013 550938463"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["chemistry-europe.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["ChemPhysChem"],"published-print":{"date-parts":[[2026,9,14]]},"abstract":"<jats:p>\n                    Photoswitchable biomimetic membranes can be controlled by light and offer the possibility to study the role of membrane dynamics for the interaction with antimicrobial peptides. The \u03b1\u2010helical peptide LAH4, a well\u2010studied model system, interacts with membranes in a pH\u2010dependent manner. It binds to the membrane surface at acidic pH and inserts into the membrane at basic pH conditions. Polarized attenuated total reflection (ATR) Fourier\u2010transform infrared (FTIR) spectroscopy was employed to probe peptide orientation and structural changes, with particular emphasis on the pH\u2010dependent response of LAH4 to light\u2010induced membrane perturbations. Photoswitchable azoPC lipids were incorporated in large unilamellar vesicles (LUVs) as well as in DIBMA\u2010stabilized nanodiscs, and the light\u2010induced\n                    <jats:italic>cis<\/jats:italic>\n                    \u2010to\u2010\n                    <jats:italic>trans<\/jats:italic>\n                    isomerization of the azobenzene was monitored by characteristic vibrational modes showing a reversible transition between two membrane states for both membrane systems. The measurements reveal that photoswitching between the membrane states induces the reorientation of the surface\u2010bound peptide toward a membrane\u2010inserted state. The findings underline the potential of photoswitchable membranes for the study of lipid\u2010peptide interactions as well as the importance of membrane dynamics for antimicrobial activity.\n                  <\/jats:p>","DOI":"10.1002\/cphc.70554","type":"journal-article","created":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T04:20:35Z","timestamp":1788236435000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Polarized ATR\u2010FTIR Spectroscopy Reveals Light\u2010Induced Peptide Insertion of LAH4 Into Photoswitchable Membranes"],"prefix":"10.1002","volume":"27","author":[{"given":"Celine","family":"Eckert","sequence":"first","affiliation":[{"name":"Department of Chemistry University of Konstanz  Konstanz Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Selina","family":"Mertens","sequence":"additional","affiliation":[{"name":"Department of Chemistry University of Konstanz  Konstanz 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