{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,25]],"date-time":"2026-07-25T03:53:12Z","timestamp":1784951592578,"version":"3.55.0"},"reference-count":40,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2011,4,6]],"date-time":"2011-04-06T00:00:00Z","timestamp":1302048000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Sensors"],"abstract":"<jats:p>The main objective of the presented study was the development of a simple analytical tool for exploring the influence of naturally occurring compounds on the aggregation of amyloid-\u03b2 peptide (A\u03b240) in order to find potential anti-neurodegenerative drugs. The gold discs used for surface plasmon resonance (SPR) measurements were modified with thioaliphatic acid. The surface functionalized with carboxylic groups was used for covalent attaching of A\u03b240 probe by creation of amide bonds in the presence of EDC\/NHS. The modified SPR gold discs were used for exploring the A\u03b240 aggregation process in the presence of selected alkaloids: arecoline hydrobromide, pseudopelletierine hydrochloride, trigonelline hydrochloride and \u03b1-lobeline hydrochloride. The obtained results were discussed with other parameters which govern the phenomenon studied such as lipophilicity\/ hydrophilicy and A\u03b240-alkaloid association constants.<\/jats:p>","DOI":"10.3390\/s110404030","type":"journal-article","created":{"date-parts":[[2011,9,27]],"date-time":"2011-09-27T20:09:10Z","timestamp":1317154150000},"page":"4030-4042","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":22,"title":["Surface Plasmon Resonance Based Biosensors for Exploring the Influence of Alkaloids on Aggregation of Amyloid-\u03b2 Peptide"],"prefix":"10.3390","volume":"11","author":[{"given":"Bart\u0142omiej Emil","family":"Krazi\u0144ski","sequence":"first","affiliation":[{"name":"Institute of Animal Reproduction and Food Research of Polish Academy of Sciences, Tuwima 10 Street, 10-747 Olsztyn, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jerzy","family":"Radecki","sequence":"additional","affiliation":[{"name":"Institute of Animal Reproduction and Food Research of Polish Academy of Sciences, Tuwima 10 Street, 10-747 Olsztyn, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hanna","family":"Radecka","sequence":"additional","affiliation":[{"name":"Institute of Animal Reproduction and Food Research of Polish Academy of Sciences, Tuwima 10 Street, 10-747 Olsztyn, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2011,4,6]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"9989","DOI":"10.1073\/pnas.96.18.9989","article-title":"Amyloid diseases: Abnormal protein aggregation in neurodegeneration","volume":"96","author":"Koo","year":"1999","journal-title":"Proc. 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