Surface Plasmon Resonance Based Biosensors for Exploring the Influence of Alkaloids on Aggregation of Amyloid-β Peptide 英文参考文献.docVIP

Sensors 2011, 11, 4030-4042; doi:10.3390/s110404030 OPEN ACCESS sensors ISSN 1424-8220 /journal/sensors Article Surface Plasmon Resonance Based Biosensors for Exploring the Influence of Alkaloids on Aggregation of Amyloid-β Peptide Bart?omiej Emil Kraziński, Jerzy Radecki and Hanna Radecka * Institute of Animal Reproduction and Food Research of Polish Academy of Sciences, Tuwima 10 Street, 10-747 Olsztyn, Poland; E-Mails: b.krazinski@pan.olsztyn.pl (B.E.K.); j.radecki@pan.olsztyn.pl (J.R.) * Author to whom correspondence should be addressed; E-Mail: hanna.radecka@pan.olsztyn.pl; Tel.: +4889-523-4636; Fax: +4889-524-0124. Received: 16 February 2011; in revised form: 16 March 2011 / Accepted: 28 March 2011 / Published: 6 April 2011 Abstract: 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-β peptide (Aβ40) 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 Aβ40 probe by creation of amide bonds in the presence of EDC/NHS. The modified SPR gold discs were used for exploring the Aβ40 aggregation process in the presence of selected alkaloids: arecoline hydrobromide, pseudopelletierine hydrochloride, trigonelline hydrochloride and α-lobeline hydrochloride. The obtained results were discussed with other parameters which govern the phenomenon studied such as lipophilicity/ hydrophilicy and Aβ40-alkaloid association constants. Keywords: amyloid-β peptide; surface plasmon resonance; alkaloids; thioaliphatic acid monolayer 1. Introduction Abnormal folding and aggregation of proteins characterizes many, if not all, neurodegenerative disorders such as Alz