Generation, selection and modification of anti-cardiac troponin I antibodies with high specificity and affinity
Copyright © 2021 Elsevier B.V. All rights reserved..
Current diagnosis of acute myocardial infarction involves quantification of circulating cTn levels. This work endeavoured to generate and enhance recombinant antibody fragments targeting various epitopes on the N- and C-terminals of the cTnI molecule, thereby facilitating highly sensitive detection of the troponin molecule. From this approach, two anti-cTnI scFv antibodies were successfully selected using either phage display or structural reformatting of full length anti-cTnI IgG. Their antibody binding affinity was further optimised via chain shuffling and/or site directed mutagenesis, resulting in scFv with heightened sensitivity when compared to the wild-type scFv. If used in conjunction with existing anti-mid fragment cTnI antibodies, these N- and C- terminal-targeting scFvs show high potential for the enhancement of current cTnI detection assays by limiting the effects from cTnI degradation or troponin complex formation.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2022 |
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| Erschienen: |
2022 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:500 |
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| Enthalten in: |
Journal of immunological methods - 500(2022) vom: 01. Jan., Seite 113183 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Ma, Hui [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 06.01.2022 Date Revised 06.01.2022 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.jim.2021.113183 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 500 | |a Date Revised 06.01.2022 | ||
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| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2021 Elsevier B.V. All rights reserved. | ||
| 520 | |a Current diagnosis of acute myocardial infarction involves quantification of circulating cTn levels. This work endeavoured to generate and enhance recombinant antibody fragments targeting various epitopes on the N- and C-terminals of the cTnI molecule, thereby facilitating highly sensitive detection of the troponin molecule. From this approach, two anti-cTnI scFv antibodies were successfully selected using either phage display or structural reformatting of full length anti-cTnI IgG. Their antibody binding affinity was further optimised via chain shuffling and/or site directed mutagenesis, resulting in scFv with heightened sensitivity when compared to the wild-type scFv. If used in conjunction with existing anti-mid fragment cTnI antibodies, these N- and C- terminal-targeting scFvs show high potential for the enhancement of current cTnI detection assays by limiting the effects from cTnI degradation or troponin complex formation | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Research Support, U.S. Gov't, Non-P.H.S. | |
| 650 | 4 | |a CTnI | |
| 650 | 4 | |a Chain shuffling | |
| 650 | 4 | |a Phage display | |
| 650 | 4 | |a Site directed mutagenesis | |
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| 650 | 7 | |a Troponin T |2 NLM | |
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| 700 | 1 | |a Ó'Fágáin, Ciarán |e verfasserin |4 aut | |
| 700 | 1 | |a O'Kennedy, Richard |e verfasserin |4 aut | |
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