Comparative Interactions of Dihydroquinazolin Derivatives with Human Serum Albumin Observed via Multiple Spectroscopy
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-dihydr...
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MDPI AG
2017-02-01
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| Online Access: | http://www.mdpi.com/2076-3417/7/2/200 |
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| author | Yi Wang Meiqing Zhu Jia Liu Risong Na Feng Liu Xiangwei Wu Shisuo Fan Zhen Wang Dandan Pan Jun Tang Qing X. Li Rimao Hua Shangzhong Liu |
| author_facet | Yi Wang Meiqing Zhu Jia Liu Risong Na Feng Liu Xiangwei Wu Shisuo Fan Zhen Wang Dandan Pan Jun Tang Qing X. Li Rimao Hua Shangzhong Liu |
| author_sort | Yi Wang |
| collection | DOAJ |
| description | 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 |
| first_indexed | 2024-12-13T01:48:48Z |
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| id | doaj.art-3fc15c3b9dda46a786ff64a9ff711f70 |
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| issn | 2076-3417 |
| language | English |
| last_indexed | 2024-12-13T01:48:48Z |
| publishDate | 2017-02-01 |
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| spelling | doaj.art-3fc15c3b9dda46a786ff64a9ff711f702022-12-22T00:03:34ZengMDPI AGApplied Sciences2076-34172017-02-017220010.3390/app7020200app7020200Comparative Interactions of Dihydroquinazolin Derivatives with Human Serum Albumin Observed via Multiple SpectroscopyYi Wang0Meiqing Zhu1Jia Liu2Risong Na3Feng Liu4Xiangwei Wu5Shisuo Fan6Zhen Wang7Dandan Pan8Jun Tang9Qing X. Li10Rimao Hua11Shangzhong Liu12Department of Science of Pesticides, School of Resources and Environment, Anhui Agricultural University, No. 130 Changjiang West Road, Hefei 230036, ChinaDepartment of Science of Pesticides, School of Resources and Environment, Anhui Agricultural University, No. 130 Changjiang West Road, Hefei 230036, ChinaDepartment of Science of Pesticides, School of Resources and Environment, Anhui Agricultural University, No. 130 Changjiang West Road, Hefei 230036, ChinaDepartment of Science of Pesticides, School of Resources and Environment, Anhui Agricultural University, No. 130 Changjiang West Road, Hefei 230036, ChinaDepartment of Applied Chemistry, China Agricultural University, No. 2 Yuanmingyuan West Road, Beijing 100193, ChinaDepartment of Science of Pesticides, School of Resources and Environment, Anhui Agricultural University, No. 130 Changjiang West Road, Hefei 230036, ChinaDepartment of Science of Pesticides, School of Resources and Environment, Anhui Agricultural University, No. 130 Changjiang West Road, Hefei 230036, ChinaDepartment of Science of Pesticides, School of Resources and Environment, Anhui Agricultural University, No. 130 Changjiang West Road, Hefei 230036, ChinaDepartment of Science of Pesticides, School of Resources and Environment, Anhui Agricultural University, No. 130 Changjiang West Road, Hefei 230036, ChinaDepartment of Science of Pesticides, School of Resources and Environment, Anhui Agricultural University, No. 130 Changjiang West Road, Hefei 230036, ChinaDepartment of Molecular Biosciences and Bioengineering, University of Hawaii at Manoa, Honolulu, HI 96822, USADepartment of Science of Pesticides, School of Resources and Environment, Anhui Agricultural University, No. 130 Changjiang West Road, Hefei 230036, ChinaDepartment of Applied Chemistry, China Agricultural University, No. 2 Yuanmingyuan West Road, Beijing 100193, ChinaThe 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 studieshttp://www.mdpi.com/2076-3417/7/2/200synthesisfluorescence quenchinghuman serum albuminPDQL |
| spellingShingle | Yi Wang Meiqing Zhu Jia Liu Risong Na Feng Liu Xiangwei Wu Shisuo Fan Zhen Wang Dandan Pan Jun Tang Qing X. Li Rimao Hua Shangzhong Liu Comparative Interactions of Dihydroquinazolin Derivatives with Human Serum Albumin Observed via Multiple Spectroscopy Applied Sciences synthesis fluorescence quenching human serum albumin PDQL |
| title | Comparative Interactions of Dihydroquinazolin Derivatives with Human Serum Albumin Observed via Multiple Spectroscopy |
| title_full | Comparative Interactions of Dihydroquinazolin Derivatives with Human Serum Albumin Observed via Multiple Spectroscopy |
| title_fullStr | Comparative Interactions of Dihydroquinazolin Derivatives with Human Serum Albumin Observed via Multiple Spectroscopy |
| title_full_unstemmed | Comparative Interactions of Dihydroquinazolin Derivatives with Human Serum Albumin Observed via Multiple Spectroscopy |
| title_short | Comparative Interactions of Dihydroquinazolin Derivatives with Human Serum Albumin Observed via Multiple Spectroscopy |
| title_sort | comparative interactions of dihydroquinazolin derivatives with human serum albumin observed via multiple spectroscopy |
| topic | synthesis fluorescence quenching human serum albumin PDQL |
| url | http://www.mdpi.com/2076-3417/7/2/200 |
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