Probing Changes in Ca<sup>2+</sup>-Induced Interaction Forces between Calmodulin and Melittin by Atomic Force Microscopy
Mechanobiology studies the means by which physical forces and mechanical properties change intra- or inter- biological macromolecules. Calmodulin (CaM) is involved in physiological activities and various metabolic processes in eukaryotic cells. Although the configuration changes in the interaction b...
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doaj-c100216b53da4108bda52bd6dcf921a82020-11-25T03:55:37ZengMDPI AGMicromachines2072-666X2020-09-011190690610.3390/mi11100906Probing Changes in Ca<sup>2+</sup>-Induced Interaction Forces between Calmodulin and Melittin by Atomic Force MicroscopySheng Huang0Jianhua Wang1Heng Sun2Yuna Fu3Yan Wang4Key Laboratory of Biorheological Science and Technology, Ministry of Education College of Bioengineering, Chongqing University, Chongqing 400044, ChinaKey Laboratory of Biorheological Science and Technology, Ministry of Education College of Bioengineering, Chongqing University, Chongqing 400044, ChinaKey Laboratory of Biorheological Science and Technology, Ministry of Education College of Bioengineering, Chongqing University, Chongqing 400044, ChinaKey Laboratory of Biorheological Science and Technology, Ministry of Education College of Bioengineering, Chongqing University, Chongqing 400044, ChinaKey Laboratory of Biorheological Science and Technology, Ministry of Education College of Bioengineering, Chongqing University, Chongqing 400044, ChinaMechanobiology studies the means by which physical forces and mechanical properties change intra- or inter- biological macromolecules. Calmodulin (CaM) is involved in physiological activities and various metabolic processes in eukaryotic cells. Although the configuration changes in the interaction between calmodulin and melittin have been studied, the biomechanical relationship of their interaction has rarely been explored. Here, we measured the adhesion forces between calmodulin and melittin in solutions of gradient concentration of calcium ions using atomic force microscopy (AFM). We found that the specific (<i>F<sub>i</sub></i>) and nonspecific (<i>F<sub>0</sub></i>) adhesion forces between single melittin and calmodulin in a PBS solution were 69.4 ± 5.0 and 29.3 ± 8.9 pN, respectively. In the presence of 10<sup>−7</sup> to 10<sup>−3</sup> M Ca<sup>2+</sup> PBS solution, the <i>F<sub>i</sub></i> increased significantly to 93.8 ± 5.0, 139.9 ± 9.0, 140.4 ± 9.7, 171.5 ± 9.0, and 213.3 ± 17.8 pN, indicating that the unbinding force between melittin and calmodulin increased in the presence of Ca<sup>2+</sup> in a concentration-dependent manner. These findings demonstrated that biomechanical studies based on AFM could help us better understand the melittin/calmodulin-binding processes in the presence of calcium and help us design and screen peptide drugs based on calmodulin.https://www.mdpi.com/2072-666X/11/10/906mechanobiologycalmodulinmelittinatomic force microscopyself-assembled monolayer |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Sheng Huang Jianhua Wang Heng Sun Yuna Fu Yan Wang |
spellingShingle |
Sheng Huang Jianhua Wang Heng Sun Yuna Fu Yan Wang Probing Changes in Ca<sup>2+</sup>-Induced Interaction Forces between Calmodulin and Melittin by Atomic Force Microscopy Micromachines mechanobiology calmodulin melittin atomic force microscopy self-assembled monolayer |
author_facet |
Sheng Huang Jianhua Wang Heng Sun Yuna Fu Yan Wang |
author_sort |
Sheng Huang |
title |
Probing Changes in Ca<sup>2+</sup>-Induced Interaction Forces between Calmodulin and Melittin by Atomic Force Microscopy |
title_short |
Probing Changes in Ca<sup>2+</sup>-Induced Interaction Forces between Calmodulin and Melittin by Atomic Force Microscopy |
title_full |
Probing Changes in Ca<sup>2+</sup>-Induced Interaction Forces between Calmodulin and Melittin by Atomic Force Microscopy |
title_fullStr |
Probing Changes in Ca<sup>2+</sup>-Induced Interaction Forces between Calmodulin and Melittin by Atomic Force Microscopy |
title_full_unstemmed |
Probing Changes in Ca<sup>2+</sup>-Induced Interaction Forces between Calmodulin and Melittin by Atomic Force Microscopy |
title_sort |
probing changes in ca<sup>2+</sup>-induced interaction forces between calmodulin and melittin by atomic force microscopy |
publisher |
MDPI AG |
series |
Micromachines |
issn |
2072-666X |
publishDate |
2020-09-01 |
description |
Mechanobiology studies the means by which physical forces and mechanical properties change intra- or inter- biological macromolecules. Calmodulin (CaM) is involved in physiological activities and various metabolic processes in eukaryotic cells. Although the configuration changes in the interaction between calmodulin and melittin have been studied, the biomechanical relationship of their interaction has rarely been explored. Here, we measured the adhesion forces between calmodulin and melittin in solutions of gradient concentration of calcium ions using atomic force microscopy (AFM). We found that the specific (<i>F<sub>i</sub></i>) and nonspecific (<i>F<sub>0</sub></i>) adhesion forces between single melittin and calmodulin in a PBS solution were 69.4 ± 5.0 and 29.3 ± 8.9 pN, respectively. In the presence of 10<sup>−7</sup> to 10<sup>−3</sup> M Ca<sup>2+</sup> PBS solution, the <i>F<sub>i</sub></i> increased significantly to 93.8 ± 5.0, 139.9 ± 9.0, 140.4 ± 9.7, 171.5 ± 9.0, and 213.3 ± 17.8 pN, indicating that the unbinding force between melittin and calmodulin increased in the presence of Ca<sup>2+</sup> in a concentration-dependent manner. These findings demonstrated that biomechanical studies based on AFM could help us better understand the melittin/calmodulin-binding processes in the presence of calcium and help us design and screen peptide drugs based on calmodulin. |
topic |
mechanobiology calmodulin melittin atomic force microscopy self-assembled monolayer |
url |
https://www.mdpi.com/2072-666X/11/10/906 |
work_keys_str_mv |
AT shenghuang probingchangesincasup2supinducedinteractionforcesbetweencalmodulinandmelittinbyatomicforcemicroscopy AT jianhuawang probingchangesincasup2supinducedinteractionforcesbetweencalmodulinandmelittinbyatomicforcemicroscopy AT hengsun probingchangesincasup2supinducedinteractionforcesbetweencalmodulinandmelittinbyatomicforcemicroscopy AT yunafu probingchangesincasup2supinducedinteractionforcesbetweencalmodulinandmelittinbyatomicforcemicroscopy AT yanwang probingchangesincasup2supinducedinteractionforcesbetweencalmodulinandmelittinbyatomicforcemicroscopy |
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1724469152650887168 |