Analytical methods for protein kinase and inhibitor screening including kinetic evaluation.
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| Title: | Analytical methods for protein kinase and inhibitor screening including kinetic evaluation. |
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| Authors: | Wurster, Viola1 (AUTHOR) viola.wurster@uni-tuebingen.de, Fechner, Peter1 (AUTHOR) peter.fechner@uni-tuebingen.de, Proll, Günther2 (AUTHOR) guenther.proll@reutlingen-university.de, Huhn, Carolin1 (AUTHOR) carolin.huhn@uni-tuebingen.de |
| Source: | Trends in Analytical Chemistry: TRAC. Dec2024:Part B, Vol. 181, pN.PAG-N.PAG. 1p. |
| Subjects: | Protein kinases, Surface plasmon resonance, Protein kinase inhibitors, Small molecules, Surface chemistry |
| Abstract: | Protein kinases promote cell processes such as cell growth and proliferation similarly in tumor cells and healthy cells. Pharmaceutical research aims at developing small molecules that inhibit tumor growth binding in the ATP-binding pocket of specific protein kinases. To understand the specificity of the inhibitor, thermodynamic and kinetic data of the kinase-inhibitor binding process are important. A broad range of analytical methods may investigate the interactions between protein kinases and inhibitors. Today, however, there is no comprehensive strategy to provide information on both specificity screening and binding kinetics. The purpose of this review is to summarize analytical methods used not only to monitor the protein kinase inhibition, but also to provide kinetic and thermodynamic data on the basis of screening applications. A focus is set on optical biosensing as the most promising techniques. We discuss, that intelligent combinations of methods can provide comprehensive information on protein kinases interacting with inhibitors. • Mainly biosensors provide binding affinity and kinetics at low costs and sample amounts. • Comprehensive analysis is reached with identification by mass spectrometry. • The biosensor's surface chemistry to beads allows kinase capturing. • The selectivity of the beads can be tuned via the choice of (selective) inhibitors. [ABSTRACT FROM AUTHOR] |
| Copyright of Trends in Analytical Chemistry: TRAC is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 181443252 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Analytical methods for protein kinase and inhibitor screening including kinetic evaluation. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Wurster%2C+Viola%22">Wurster, Viola</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> viola.wurster@uni-tuebingen.de</i><br /><searchLink fieldCode="AR" term="%22Fechner%2C+Peter%22">Fechner, Peter</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> peter.fechner@uni-tuebingen.de</i><br /><searchLink fieldCode="AR" term="%22Proll%2C+Günther%22">Proll, Günther</searchLink><relatesTo>2</relatesTo> (AUTHOR)<i> guenther.proll@reutlingen-university.de</i><br /><searchLink fieldCode="AR" term="%22Huhn%2C+Carolin%22">Huhn, Carolin</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> carolin.huhn@uni-tuebingen.de</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Trends+in+Analytical+Chemistry%3A+TRAC%22">Trends in Analytical Chemistry: TRAC</searchLink>. Dec2024:Part B, Vol. 181, pN.PAG-N.PAG. 1p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Protein+kinases%22">Protein kinases</searchLink><br /><searchLink fieldCode="DE" term="%22Surface+plasmon+resonance%22">Surface plasmon resonance</searchLink><br /><searchLink fieldCode="DE" term="%22Protein+kinase+inhibitors%22">Protein kinase inhibitors</searchLink><br /><searchLink fieldCode="DE" term="%22Small+molecules%22">Small molecules</searchLink><br /><searchLink fieldCode="DE" term="%22Surface+chemistry%22">Surface chemistry</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Protein kinases promote cell processes such as cell growth and proliferation similarly in tumor cells and healthy cells. Pharmaceutical research aims at developing small molecules that inhibit tumor growth binding in the ATP-binding pocket of specific protein kinases. To understand the specificity of the inhibitor, thermodynamic and kinetic data of the kinase-inhibitor binding process are important. A broad range of analytical methods may investigate the interactions between protein kinases and inhibitors. Today, however, there is no comprehensive strategy to provide information on both specificity screening and binding kinetics. The purpose of this review is to summarize analytical methods used not only to monitor the protein kinase inhibition, but also to provide kinetic and thermodynamic data on the basis of screening applications. A focus is set on optical biosensing as the most promising techniques. We discuss, that intelligent combinations of methods can provide comprehensive information on protein kinases interacting with inhibitors. • Mainly biosensors provide binding affinity and kinetics at low costs and sample amounts. • Comprehensive analysis is reached with identification by mass spectrometry. • The biosensor's surface chemistry to beads allows kinase capturing. • The selectivity of the beads can be tuned via the choice of (selective) inhibitors. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Trends in Analytical Chemistry: TRAC is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1016/j.trac.2024.118025 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 1 StartPage: N.PAG Subjects: – SubjectFull: Protein kinases Type: general – SubjectFull: Surface plasmon resonance Type: general – SubjectFull: Protein kinase inhibitors Type: general – SubjectFull: Small molecules Type: general – SubjectFull: Surface chemistry Type: general Titles: – TitleFull: Analytical methods for protein kinase and inhibitor screening including kinetic evaluation. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Wurster, Viola – PersonEntity: Name: NameFull: Fechner, Peter – PersonEntity: Name: NameFull: Proll, Günther – PersonEntity: Name: NameFull: Huhn, Carolin IsPartOfRelationships: – BibEntity: Dates: – D: 05 M: 12 Text: Dec2024:Part B Type: published Y: 2024 Identifiers: – Type: issn-print Value: 01659936 Numbering: – Type: volume Value: 181 Titles: – TitleFull: Trends in Analytical Chemistry: TRAC Type: main |
| ResultId | 1 |