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Appl. Sci. 2017, 7(2), 200; doi:10.3390/app7020200

Comparative Interactions of Dihydroquinazolin Derivatives with Human Serum Albumin Observed via Multiple Spectroscopy

1
Department of Science of Pesticides, School of Resources and Environment, Anhui Agricultural University, No. 130 Changjiang West Road, Hefei 230036, China
2
Department of Applied Chemistry, China Agricultural University, No. 2 Yuanmingyuan West Road, Beijing 100193, China
3
Collaborative Innovation Center of Henan Grain Crops, National Key Laboratory of Wheat and Maize Crop Science, College of Plant Protection, Henan Agricultural University, Wenhua Road No. 95, Zhengzhou 450002, China
4
Department of Molecular Biosciences and Bioengineering, University of Hawaii at Manoa, Honolulu, HI 96822, USA
*
Authors to whom correspondence should be addressed.
Received: 19 December 2016 / Accepted: 14 February 2017 / Published: 17 February 2017
(This article belongs to the Section Chemistry)
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Abstract

The interactions of dihydroquinazolines with human serum albumin (HSA) were studied in pH 7.4 aqueous solution via fluorescence, circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopic techniques. In this work, 6-chloro-1-(3,3-dimethyl-butanoyl)-2(un)substitutedphenyl-2,3-dihydroquinazolin-4(1H)-one (PDQL) derivatives were designed and synthesized to study the impact of five similar substituents (methyl, methoxy, cyano, trifluoromethyl and isopropyl) on the interactions between PDQL and HSA using a comparative methodology. The results revealed that PDQL quenched the intrinsic fluorescence of HSA through a static quenching process. Displacement experiments with site-specific markers revealed that PDQL binds to HSA at site II (subdomain IIIA) and that there may be only one binding site for PDQL on HSA. The thermodynamic parameters indicated that hydrophobic interactions mainly drove the interactions between PDQL and HSA. The substitution using five similar groups in the benzene ring could increase the interactions between PDQL and HSA to some extent through the van der Waals force or hydrogen bond effects in the proper temperature range. Isopropyl substitution could particularly enhance the binding affinity, as observed via comparative studies View Full-Text
Keywords: synthesis; fluorescence quenching; human serum albumin; PDQL synthesis; fluorescence quenching; human serum albumin; PDQL
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MDPI and ACS Style

Wang, Y.; Zhu, M.; Liu, J.; Na, R.; Liu, F.; Wu, X.; Fan, S.; Wang, Z.; Pan, D.; Tang, J.; Li, Q.X.; Hua, R.; Liu, S. Comparative Interactions of Dihydroquinazolin Derivatives with Human Serum Albumin Observed via Multiple Spectroscopy. Appl. Sci. 2017, 7, 200.

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