Integration of Adenylate Kinase 1 with Its Peptide Conformational Imprint
In the present study, molecularly imprinted polymers (MIPs) were used as a tool to grasp a targeted α-helix or β-sheet of protein. During the fabrication of the hinge-mediated MIPs, elegant cavities took shape in a special solvent on quartz crystal microbalance (QCM) chips. The cavities, which were...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-06-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/12/6521 |
| _version_ | 1797486539056349184 |
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| author | Cheng-Hsin Wu Chung-Yin Lin Tzu-Chieh Lin Dar-Fu Tai |
| author_facet | Cheng-Hsin Wu Chung-Yin Lin Tzu-Chieh Lin Dar-Fu Tai |
| author_sort | Cheng-Hsin Wu |
| collection | DOAJ |
| description | In the present study, molecularly imprinted polymers (MIPs) were used as a tool to grasp a targeted α-helix or β-sheet of protein. During the fabrication of the hinge-mediated MIPs, elegant cavities took shape in a special solvent on quartz crystal microbalance (QCM) chips. The cavities, which were complementary to the protein secondary structure, acted as a peptide conformational imprint (PCI) for adenylate kinase 1 (AK1). We established a promising strategy to examine the binding affinities of human AK1 in conformational dynamics using the peptide-imprinting method. Moreover, when bound to AK1, PCIs are able to gain stability and tend to maintain higher catalytic activities than free AK1. Such designed fixations not only act on hinges as accelerators; some are also inhibitors. One example of PCI inhibition of AK1 catalytic activity takes place when PCI integrates with an AK1<sub>9-23</sub> β-sheet. In addition, conformation ties, a general MIP method derived from random-coil AK1<sub>133-144</sub> in buffer/acetonitrile, are also inhibitors. The inhibition may be due to the need for this peptide to execute conformational transition during catalysis. |
| first_indexed | 2024-03-09T23:34:42Z |
| format | Article |
| id | doaj.art-06d9459859fa438388ccfe58127d5f3f |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T23:34:42Z |
| publishDate | 2022-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-06d9459859fa438388ccfe58127d5f3f2023-11-23T17:02:16ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-06-012312652110.3390/ijms23126521Integration of Adenylate Kinase 1 with Its Peptide Conformational ImprintCheng-Hsin Wu0Chung-Yin Lin1Tzu-Chieh Lin2Dar-Fu Tai3Department of Chemistry, National Dong Hwa University, Hualien 97403, TaiwanMedical Imaging Research Center, Institute for Radiological Research, Chang Gung University, Taoyuan 33302, TaiwanDepartment of Chemistry, National Dong Hwa University, Hualien 97403, TaiwanDepartment of Chemistry, National Dong Hwa University, Hualien 97403, TaiwanIn the present study, molecularly imprinted polymers (MIPs) were used as a tool to grasp a targeted α-helix or β-sheet of protein. During the fabrication of the hinge-mediated MIPs, elegant cavities took shape in a special solvent on quartz crystal microbalance (QCM) chips. The cavities, which were complementary to the protein secondary structure, acted as a peptide conformational imprint (PCI) for adenylate kinase 1 (AK1). We established a promising strategy to examine the binding affinities of human AK1 in conformational dynamics using the peptide-imprinting method. Moreover, when bound to AK1, PCIs are able to gain stability and tend to maintain higher catalytic activities than free AK1. Such designed fixations not only act on hinges as accelerators; some are also inhibitors. One example of PCI inhibition of AK1 catalytic activity takes place when PCI integrates with an AK1<sub>9-23</sub> β-sheet. In addition, conformation ties, a general MIP method derived from random-coil AK1<sub>133-144</sub> in buffer/acetonitrile, are also inhibitors. The inhibition may be due to the need for this peptide to execute conformational transition during catalysis.https://www.mdpi.com/1422-0067/23/12/6521adenylate kinase 1molecularly imprinted polymersconformationsecondary structureinhibition |
| spellingShingle | Cheng-Hsin Wu Chung-Yin Lin Tzu-Chieh Lin Dar-Fu Tai Integration of Adenylate Kinase 1 with Its Peptide Conformational Imprint International Journal of Molecular Sciences adenylate kinase 1 molecularly imprinted polymers conformation secondary structure inhibition |
| title | Integration of Adenylate Kinase 1 with Its Peptide Conformational Imprint |
| title_full | Integration of Adenylate Kinase 1 with Its Peptide Conformational Imprint |
| title_fullStr | Integration of Adenylate Kinase 1 with Its Peptide Conformational Imprint |
| title_full_unstemmed | Integration of Adenylate Kinase 1 with Its Peptide Conformational Imprint |
| title_short | Integration of Adenylate Kinase 1 with Its Peptide Conformational Imprint |
| title_sort | integration of adenylate kinase 1 with its peptide conformational imprint |
| topic | adenylate kinase 1 molecularly imprinted polymers conformation secondary structure inhibition |
| url | https://www.mdpi.com/1422-0067/23/12/6521 |
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