Novel 7-(dimethylamino)fluorene-based fluorescent probes and their binding to human serum albumin.
A novel solvatochromic fluorescent molecule, 9,9-dibutyl-7-(dimethylamino)-2-fluorenesulfonate 2 was synthesized from 2-nitrofluorene in moderate yield. The fluorescence spectra of 2 and 7-(dimethylamino)-2-fluorenesulfonate 1 shift to shorter wavelengths as the polarity of the medium decreases. Bot...
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| Format: | Journal article |
| Language: | English |
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2009
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| _version_ | 1797090618514604032 |
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| author | Park, K Park, J Hamilton, A |
| author_facet | Park, K Park, J Hamilton, A |
| author_sort | Park, K |
| collection | OXFORD |
| description | A novel solvatochromic fluorescent molecule, 9,9-dibutyl-7-(dimethylamino)-2-fluorenesulfonate 2 was synthesized from 2-nitrofluorene in moderate yield. The fluorescence spectra of 2 and 7-(dimethylamino)-2-fluorenesulfonate 1 shift to shorter wavelengths as the polarity of the medium decreases. Both 1 and 2 bind to hydrophobic sites of human serum albumin (HSA). The apparent binding constants were determined by fluorescence titration to be 0.37 x 10(6) M(-1) for 1 and 2.2 x 10(6) M(-1) for 2. The energy of the Trp-214 fluorescence of HSA is transferred to the HSA-bound fluorophores with near 100% efficiency. The covalent bonding of acrylodan (AC) to Cys-34 has little effect on the binding affinity of 2 to HSA or fluorescent behavior of HSA-bound 2. Bound 2 also has little effect on the fluorescence of AC, but 2-->AC and Trp-214-->2-->AC resonance energy transfers were observed. Competitive binding between the fluorene compounds and other ligands such as 1-anilino-8-naphthalenesulfonate, aspirin, S-(+)-ibuprofen and phenylbutazone were also studied fluorometrically. The results indicated that the primary binding site of 2 to HSA is site II in domain IIIA, whereas 1 binds to site I in domain IIA, but a different region from the phenylbutazone binding site. Because of its large molar absorptivity, strong fluorescence, sensitivity to its environment, and high binding constant to HSA, 2 can be used successfully in the study of proteins and their binding properties. |
| first_indexed | 2024-03-07T03:21:14Z |
| format | Journal article |
| id | oxford-uuid:b7822eaf-592b-4150-823c-8fd231623ce5 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T03:21:14Z |
| publishDate | 2009 |
| record_format | dspace |
| spelling | oxford-uuid:b7822eaf-592b-4150-823c-8fd231623ce52022-03-27T04:49:08ZNovel 7-(dimethylamino)fluorene-based fluorescent probes and their binding to human serum albumin.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:b7822eaf-592b-4150-823c-8fd231623ce5EnglishSymplectic Elements at Oxford2009Park, KPark, JHamilton, AA novel solvatochromic fluorescent molecule, 9,9-dibutyl-7-(dimethylamino)-2-fluorenesulfonate 2 was synthesized from 2-nitrofluorene in moderate yield. The fluorescence spectra of 2 and 7-(dimethylamino)-2-fluorenesulfonate 1 shift to shorter wavelengths as the polarity of the medium decreases. Both 1 and 2 bind to hydrophobic sites of human serum albumin (HSA). The apparent binding constants were determined by fluorescence titration to be 0.37 x 10(6) M(-1) for 1 and 2.2 x 10(6) M(-1) for 2. The energy of the Trp-214 fluorescence of HSA is transferred to the HSA-bound fluorophores with near 100% efficiency. The covalent bonding of acrylodan (AC) to Cys-34 has little effect on the binding affinity of 2 to HSA or fluorescent behavior of HSA-bound 2. Bound 2 also has little effect on the fluorescence of AC, but 2-->AC and Trp-214-->2-->AC resonance energy transfers were observed. Competitive binding between the fluorene compounds and other ligands such as 1-anilino-8-naphthalenesulfonate, aspirin, S-(+)-ibuprofen and phenylbutazone were also studied fluorometrically. The results indicated that the primary binding site of 2 to HSA is site II in domain IIIA, whereas 1 binds to site I in domain IIA, but a different region from the phenylbutazone binding site. Because of its large molar absorptivity, strong fluorescence, sensitivity to its environment, and high binding constant to HSA, 2 can be used successfully in the study of proteins and their binding properties. |
| spellingShingle | Park, K Park, J Hamilton, A Novel 7-(dimethylamino)fluorene-based fluorescent probes and their binding to human serum albumin. |
| title | Novel 7-(dimethylamino)fluorene-based fluorescent probes and their binding to human serum albumin. |
| title_full | Novel 7-(dimethylamino)fluorene-based fluorescent probes and their binding to human serum albumin. |
| title_fullStr | Novel 7-(dimethylamino)fluorene-based fluorescent probes and their binding to human serum albumin. |
| title_full_unstemmed | Novel 7-(dimethylamino)fluorene-based fluorescent probes and their binding to human serum albumin. |
| title_short | Novel 7-(dimethylamino)fluorene-based fluorescent probes and their binding to human serum albumin. |
| title_sort | novel 7 dimethylamino fluorene based fluorescent probes and their binding to human serum albumin |
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