caa a22 4500 445803711 CHVBK 20180317145150.0 cr unu---uuuuu 170323e20110701xx s 000 0 eng 10.1007/s10337-011-2043-1 doi (NATIONALLICENCE)springer-10.1007/s10337-011-2043-1 Binding Interaction between Nicotine and Human Serum Albumin by High Performance Affinity Chromatography [Elektronische Daten] [Xunyu Xiong, Yefei Nan, Qunzheng Zhang] Several reports have confirmed that nicotine can bind to serum albumin, but the exact strength, location and number of the binding sites used during this process remain unclear. In this work, frontal analysis investigation showed that the binding isotherm of nicotine to human serum albumin (HSA) best fitted the Langmuir model, suggesting a single kind of binding site for nicotine on HSA. Competitive studies with probe compounds revealed that nicotine is in direct competition with l-tryptophan, indicated that nicotine binds to Sudlow site II (i.e., the indole-benzodiazepine site of HSA). No interactions were seen between nicotine and S-warfarin, tamoxifen or digitoxin. The association constant of nicotine binding to HSA was (8.60±2.26)×104M−1 at pH7.2 and 37°C. The value of ∆G for this reaction was −42.75kJmol−1 at 37°C, with an associated change in enthalpy (∆H) of 6.7kJmol−1 and a change in entropy (∆S) of 116.4Jmol-1 K−1, demonstrating that the interaction was driven mainly by entropy, and that hydrophobic interaction was the main power behind the binding process. These results will help provide a more detailed description of how nicotine is transported in the blood and how it may interact with other drugs in the body. Springer-Verlag, 2011 Affinity chromatography nationallicence Nicotine nationallicence Frontal analysis nationallicence Zonal elution nationallicence Human serum albumin nationallicence Xiong Xunyu College of Chemistry and Chemical Engineering, Xi'an Shiyou University, No.18, East of Dianzi Second Road, 710065, Shaanxi, Xi'an, China aut Nan Yefei College of Chemistry and Chemical Engineering, Xi'an Shiyou University, No.18, East of Dianzi Second Road, 710065, Shaanxi, Xi'an, China aut Zhang Qunzheng College of Chemistry and Chemical Engineering, Xi'an Shiyou University, No.18, East of Dianzi Second Road, 710065, Shaanxi, Xi'an, China aut Chromatographia Springer-Verlag 74/1-2(2011-07-01), 127-131 0009-5893 74:1-2<127 2011 74 10337 https://doi.org/10.1007/s10337-011-2043-1 text/html Onlinezugriff via DOI 1 brief-communication jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10337-011-2043-1 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Xiong Xunyu College of Chemistry and Chemical Engineering, Xi'an Shiyou University, No.18, East of Dianzi Second Road, 710065, Shaanxi, Xi'an, China aut NATIONALLICENCE 700 1- Nan Yefei College of Chemistry and Chemical Engineering, Xi'an Shiyou University, No.18, East of Dianzi Second Road, 710065, Shaanxi, Xi'an, China aut NATIONALLICENCE 700 1- Zhang Qunzheng College of Chemistry and Chemical Engineering, Xi'an Shiyou University, No.18, East of Dianzi Second Road, 710065, Shaanxi, Xi'an, China aut NATIONALLICENCE 773 0- Chromatographia Springer-Verlag 74/1-2(2011-07-01), 127-131 0009-5893 74:1-2<127 2011 74 10337 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer