{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,8]],"date-time":"2025-10-08T21:10:07Z","timestamp":1759957807503,"version":"build-2065373602"},"reference-count":36,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2008,5,16]],"date-time":"2008-05-16T00:00:00Z","timestamp":1210896000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Chemistry \u0097 An Asian Journal"],"published-print":{"date-parts":[[2008,7,7]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The interfacing of functional proteins with solid supports and the study of related protein\u2010adsorption behavior are promising and important for potential device applications. In this study, we describe the preparation of bacteriorhodopsin (bR) monolayers on Br\u2010terminated solid supports through covalent attachment. The bonding, by chemical reaction of the exposed free amine groups of bR with the pendant Br group of the chemically modified solid surface, was confirmed both by negative AFM results obtained when acetylated bR (instead of native bR) was used as a control and by weak bands observed at around 1610\u2005cm<jats:sup>\u22121<\/jats:sup> in the FTIR spectrum. The coverage of the resultant bR monolayer was significantly increased by changing the pH of the purple\u2010membrane suspension from 9.2 to 6.8. Although bR, which is an exceptionally stable protein, showed a pronounced loss of its photoactivity in these bR monolayers, it retained full photoactivity after covalent binding to Br\u2010terminated alkyls in solution. Several characterization methods, including atomic force microscopy (AFM), contact potential difference (CPD) measurements, and UV\/Vis and Fourier transform infrared (FTIR) spectroscopy, verified that these bR monolayers behaved significantly different from native bR. Current\u2013voltage (<jats:italic>I<\/jats:italic>\u2013<jats:italic>V<\/jats:italic>) measurements (and optical absorption spectroscopy) suggest that the retinal chromophore is probably still present in the protein, whereas the UV\/Vis spectrum suggests that it lacks the characteristic covalent protonated Schiff base linkage. This finding sheds light on the unique interactions of biomolecules with solid surfaces and may be significant for the design of protein\u2010containing device structures.<\/jats:p>","DOI":"10.1002\/asia.200700403","type":"journal-article","created":{"date-parts":[[2008,5,16]],"date-time":"2008-05-16T08:16:51Z","timestamp":1210925811000},"page":"1146-1155","source":"Crossref","is-referenced-by-count":2,"title":["Covalent Attachment of Bacteriorhodopsin Monolayer to Bromo\u2010terminated Solid Supports: Preparation, Characterization, and Protein Stability"],"prefix":"10.1002","volume":"3","author":[{"given":"Yongdong","family":"Jin","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Olga","family":"Girshevitz","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Noga","family":"Friedman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Izhar","family":"Ron","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David","family":"Cahen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mordechai","family":"Sheves","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2008,6,23]]},"reference":[{"key":"e_1_2_6_1_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.pc.41.100190.003343"},{"key":"e_1_2_6_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/newbio233149a0"},{"key":"e_1_2_6_3_2","doi-asserted-by":"publisher","DOI":"10.1021\/nl050157v"},{"key":"e_1_2_6_4_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0511234103"},{"key":"e_1_2_6_5_2","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/0040-6090(92)90193-F","volume":"210","author":"Miyasaka T.","year":"1992","journal-title":"Thin Solid Films"},{"key":"e_1_2_6_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2736(80)90023-1"},{"key":"e_1_2_6_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/0303-2647(94)01501-W"},{"key":"e_1_2_6_8_2","doi-asserted-by":"publisher","DOI":"10.1002\/adma.200401144"},{"key":"e_1_2_6_9_2","doi-asserted-by":"publisher","DOI":"10.1039\/b518268a"},{"key":"e_1_2_6_10_2","doi-asserted-by":"publisher","DOI":"10.1021\/la971336y"},{"key":"e_1_2_6_11_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.265.5173.762"},{"key":"e_1_2_6_12_2","doi-asserted-by":"publisher","DOI":"10.1021\/jp022400"},{"key":"e_1_2_6_13_2","doi-asserted-by":"publisher","DOI":"10.1116\/1.580706"},{"key":"e_1_2_6_14_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja056278e"},{"key":"e_1_2_6_15_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja042898o"},{"key":"e_1_2_6_16_2","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2728(94)00161-W"},{"key":"e_1_2_6_17_2","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1016\/S0005-2736(97)00016-3","volume":"1326","author":"Sugiyama Y.","year":"1997","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"e_1_2_6_18_2","doi-asserted-by":"publisher","DOI":"10.1021\/la9710886"},{"key":"e_1_2_6_19_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.76.10.5046"},{"key":"e_1_2_6_20_2","unstructured":"Even though the amine group of Tris may also react with the Br\u2010modified surface this process can be excluded as a major reason for the observed differences in the results. This conclusion is based on the finding that no pronounced difference in surface coverage was found when we prepared films at pH\u20056.8 (deionized H2O only) with or without pretreating the Br\u2010modified substrate with pH\u20059.2 Tris buffer."},{"key":"e_1_2_6_21_2","unstructured":"The contact potential difference CPD=WF(Au)\u2212WF(sample) with WF(Au) taken as 5.0\u2005eV (WF=work function). Therefore if the CPD decreases from \u22120.35 to \u22120.50\u2005V this means that WF(sample with PM) is 0.15\u2005V higher than WF(sample without PM)."},{"key":"e_1_2_6_22_2","doi-asserted-by":"publisher","DOI":"10.1021\/ac001207d"},{"key":"e_1_2_6_23_2","doi-asserted-by":"publisher","DOI":"10.1021\/jp013131a"},{"key":"e_1_2_6_24_2","doi-asserted-by":"publisher","DOI":"10.1093\/protein\/12.9.755"},{"key":"e_1_2_6_25_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi961845j"},{"key":"e_1_2_6_26_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-3495(96)79858-2"},{"key":"e_1_2_6_27_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00489a038"},{"key":"e_1_2_6_28_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0040-6090(95)08407-X"},{"key":"e_1_2_6_29_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi00243a025"},{"key":"e_1_2_6_30_2","doi-asserted-by":"publisher","DOI":"10.1038\/35004539"},{"key":"e_1_2_6_31_2","doi-asserted-by":"publisher","DOI":"10.1002\/smll.200500052"},{"key":"e_1_2_6_32_2","doi-asserted-by":"publisher","DOI":"10.1002\/adfm.200600545"},{"key":"e_1_2_6_33_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0006-3495(79)85172-3"},{"key":"e_1_2_6_34_2","doi-asserted-by":"crossref","first-page":"1259","DOI":"10.1016\/S0006-3495(89)82773-0","volume":"56","author":"Albeck A.","year":"1989","journal-title":"Biophys. 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