The Atomistic Understanding of the Ice Recrystallization Inhibition Activity of Antifreeze Glycoproteins
As the most potent ice recrystallization inhibitors, antifreeze glycoproteins (AFGPs) have been extensively studied since their discovery. However, the molecular mechanism of how they inhibit ice growth remains controversial—notably, which group directly contributes to the binding of AFGPs to ice is...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2023-02-01
|
| Series: | Crystals |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2073-4352/13/3/405 |
| _version_ | 1827750425928925184 |
|---|---|
| author | Wentao Yang Yucong Liao Qi Shi Zhaoru Sun |
| author_facet | Wentao Yang Yucong Liao Qi Shi Zhaoru Sun |
| author_sort | Wentao Yang |
| collection | DOAJ |
| description | As the most potent ice recrystallization inhibitors, antifreeze glycoproteins (AFGPs) have been extensively studied since their discovery. However, the molecular mechanism of how they inhibit ice growth remains controversial—notably, which group directly contributes to the binding of AFGPs to ice is hotly debated. Here, we use molecular dynamics simulations to investigate the atomistic details of the binding of AFGP8 to ice. We show that the binding of AFGP8 to ice can be divided into three cases: backbone dominant binding (BDB), disaccharide dominant binding (DDB) and weak binding (WB). Hydrogen-bonding and hydrophobic groups contribute equally to the binding of AFGP8 to ice and synergistically promote the binding. The –CH<sub>3</sub> groups promote the contacting of AFGP8 to ice via hydrophobic effect, and the hydrogen-bonding groups anchor AFGP8 to ice surfaces through direct hydrogen bonding with ice. Specially, we verify that the -CONH- groups anchor the backbone of AFGP8 to ice by forming hydrogen bonds with ice surfaces while the –OH groups not only anchor the disaccharide to ice but also slow down the dynamics of the surrounding water. In addition, we reveal that both the backbone and the disaccharide can bind to ice surfaces while the latter is more flexible, which also perturbs the hydrogen bond network of potential ice-like water molecules by swaying in the solution to further enhance its antifreeze activity. This work provides the atomistic details of the ice growth inhibition mechanism of AFGP8, which is helpful for the design of high-efficacy cryoprotectants. |
| first_indexed | 2024-03-11T06:43:12Z |
| format | Article |
| id | doaj.art-d7878eaad6484b0288dfe8533d0f00b3 |
| institution | Directory Open Access Journal |
| issn | 2073-4352 |
| language | English |
| last_indexed | 2024-03-11T06:43:12Z |
| publishDate | 2023-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Crystals |
| spelling | doaj.art-d7878eaad6484b0288dfe8533d0f00b32023-11-17T10:28:18ZengMDPI AGCrystals2073-43522023-02-0113340510.3390/cryst13030405The Atomistic Understanding of the Ice Recrystallization Inhibition Activity of Antifreeze GlycoproteinsWentao Yang0Yucong Liao1Qi Shi2Zhaoru Sun3School of Physical Science and Technology, ShanghaiTech University, Shanghai 201210, ChinaSchool of Physical Science and Technology, ShanghaiTech University, Shanghai 201210, ChinaSchool of Physical Science and Technology, ShanghaiTech University, Shanghai 201210, ChinaSchool of Physical Science and Technology, ShanghaiTech University, Shanghai 201210, ChinaAs the most potent ice recrystallization inhibitors, antifreeze glycoproteins (AFGPs) have been extensively studied since their discovery. However, the molecular mechanism of how they inhibit ice growth remains controversial—notably, which group directly contributes to the binding of AFGPs to ice is hotly debated. Here, we use molecular dynamics simulations to investigate the atomistic details of the binding of AFGP8 to ice. We show that the binding of AFGP8 to ice can be divided into three cases: backbone dominant binding (BDB), disaccharide dominant binding (DDB) and weak binding (WB). Hydrogen-bonding and hydrophobic groups contribute equally to the binding of AFGP8 to ice and synergistically promote the binding. The –CH<sub>3</sub> groups promote the contacting of AFGP8 to ice via hydrophobic effect, and the hydrogen-bonding groups anchor AFGP8 to ice surfaces through direct hydrogen bonding with ice. Specially, we verify that the -CONH- groups anchor the backbone of AFGP8 to ice by forming hydrogen bonds with ice surfaces while the –OH groups not only anchor the disaccharide to ice but also slow down the dynamics of the surrounding water. In addition, we reveal that both the backbone and the disaccharide can bind to ice surfaces while the latter is more flexible, which also perturbs the hydrogen bond network of potential ice-like water molecules by swaying in the solution to further enhance its antifreeze activity. This work provides the atomistic details of the ice growth inhibition mechanism of AFGP8, which is helpful for the design of high-efficacy cryoprotectants.https://www.mdpi.com/2073-4352/13/3/405antifreezeice growthantifreeze glycoproteinsice recrystallization inhibition |
| spellingShingle | Wentao Yang Yucong Liao Qi Shi Zhaoru Sun The Atomistic Understanding of the Ice Recrystallization Inhibition Activity of Antifreeze Glycoproteins Crystals antifreeze ice growth antifreeze glycoproteins ice recrystallization inhibition |
| title | The Atomistic Understanding of the Ice Recrystallization Inhibition Activity of Antifreeze Glycoproteins |
| title_full | The Atomistic Understanding of the Ice Recrystallization Inhibition Activity of Antifreeze Glycoproteins |
| title_fullStr | The Atomistic Understanding of the Ice Recrystallization Inhibition Activity of Antifreeze Glycoproteins |
| title_full_unstemmed | The Atomistic Understanding of the Ice Recrystallization Inhibition Activity of Antifreeze Glycoproteins |
| title_short | The Atomistic Understanding of the Ice Recrystallization Inhibition Activity of Antifreeze Glycoproteins |
| title_sort | atomistic understanding of the ice recrystallization inhibition activity of antifreeze glycoproteins |
| topic | antifreeze ice growth antifreeze glycoproteins ice recrystallization inhibition |
| url | https://www.mdpi.com/2073-4352/13/3/405 |
| work_keys_str_mv | AT wentaoyang theatomisticunderstandingoftheicerecrystallizationinhibitionactivityofantifreezeglycoproteins AT yucongliao theatomisticunderstandingoftheicerecrystallizationinhibitionactivityofantifreezeglycoproteins AT qishi theatomisticunderstandingoftheicerecrystallizationinhibitionactivityofantifreezeglycoproteins AT zhaorusun theatomisticunderstandingoftheicerecrystallizationinhibitionactivityofantifreezeglycoproteins AT wentaoyang atomisticunderstandingoftheicerecrystallizationinhibitionactivityofantifreezeglycoproteins AT yucongliao atomisticunderstandingoftheicerecrystallizationinhibitionactivityofantifreezeglycoproteins AT qishi atomisticunderstandingoftheicerecrystallizationinhibitionactivityofantifreezeglycoproteins AT zhaorusun atomisticunderstandingoftheicerecrystallizationinhibitionactivityofantifreezeglycoproteins |