Optical Fingerprints of Proteases and Their Inhibited Complexes Provided by Differential Cross-Reactivity of Fluorophore-Labeled Single-Stranded DNA
Autor: | Shunsuke Tomita, Sayaka Ishihara, Masahiro Mimura, Kentaro Shiraki, Hiroka Sugai, Ryoji Kurita |
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Rok vydání: | 2019 |
Předmět: |
Proteases
Fluorophore Materials science Antithrombin III DNA Single-Stranded Biosensing Techniques 02 engineering and technology medicine.disease_cause 01 natural sciences Cross-reactivity chemistry.chemical_compound 0202 electrical engineering electronic engineering information engineering medicine Humans Trypsin General Materials Science Fluorescent Dyes Rhodamines 010401 analytical chemistry Fingerprint (computing) Thrombin 020206 networking & telecommunications Aptamers Nucleotide 0104 chemical sciences Biochemistry chemistry Multiprotein Complexes alpha 1-Antitrypsin Biosensor DNA Differential (mathematics) Peptide Hydrolases Protein Binding |
Zdroj: | ACS Applied Materials & Interfaces. 11:47428-47436 |
ISSN: | 1944-8252 1944-8244 |
DOI: | 10.1021/acsami.9b17829 |
Popis: | The detection of proteases and their complexes with inhibitor proteins is of great importance for diagnosis and medical-treatment applications. In this study, we report a fingerprint-based sensor using an array of single-stranded DNAs (ssDNAs) labeled with environment-responsive 3'-carboxytetramethylrhodamine (TAMRA) for the identification of proteases. Four TAMRA-modified ssDNAs with different sequences solubilized in two different buffer solutions were incorporated in an array that was capable of generating fluorescent fingerprints unique to the proteases through diverse cross-reactive interactions, allowing the discrimination of (i) 8 proteases and (ii) 12 different mixtures of trypsin and its inhibitor protein (α |
Databáze: | OpenAIRE |
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