دورية أكاديمية
Design of eco-friendly antifreeze peptides as novel inhibitors of gas-hydration kinetics.
| العنوان: | Design of eco-friendly antifreeze peptides as novel inhibitors of gas-hydration kinetics. |
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| المؤلفون: | Zhang N; Laboratory of Theoretical Biophysics, School of Physical Science and Technology, Inner Mongolia University, Hohhot 010021, China., Zhu Y; Laboratory of Theoretical Biophysics, School of Physical Science and Technology, Inner Mongolia University, Hohhot 010021, China., Li YN; Laboratory of Theoretical Biophysics, School of Physical Science and Technology, Inner Mongolia University, Hohhot 010021, China., Zhang LR; Laboratory of Theoretical Biophysics, School of Physical Science and Technology, Inner Mongolia University, Hohhot 010021, China., Zhang FS; The Key Laboratory of Beam Technology and Material Modification of Ministry of Education, College of Nuclear Science and Technology, Beijing Normal University, Beijing 100875, China., Liu JJ; Laboratory of Theoretical Biophysics, School of Physical Science and Technology, Inner Mongolia University, Hohhot 010021, China. |
| المصدر: | The Journal of chemical physics [J Chem Phys] 2024 Aug 07; Vol. 161 (5). |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Institute of Physics Country of Publication: United States NLM ID: 0375360 Publication Model: Print Cited Medium: Internet ISSN: 1089-7690 (Electronic) Linking ISSN: 00219606 NLM ISO Abbreviation: J Chem Phys Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: New York, NY : American Institute of Physics Original Publication: Lancaster, Pa., American Institute of Physics. |
| مواضيع طبية MeSH: | Antifreeze Proteins*/chemistry , Methane*/chemistry , Methane*/analogs & derivatives , Water*/chemistry , Tenebrio*/chemistry, Kinetics ; Animals ; Gases/chemistry ; Peptides/chemistry ; Peptides/pharmacology |
| مستخلص: | In this study, peptides designed using fragments of an antifreeze protein (AFP) from the freeze-tolerant insect Tenebrio molitor, TmAFP, were evaluated as inhibitors of clathrate hydrate formation. It was found that these peptides exhibit inhibitory effects by both direct and indirect mechanisms. The direct mechanism involves the displacement of methane molecules by hydrophobic methyl groups from threonine residues, preventing their diffusion to the hydrate surface. The indirect mechanism is characterized by the formation of cylindrical gas bubbles, the morphology of which reduces the pressure difference at the bubble interface, thereby slowing methane transport. The transfer of methane to the hydrate interface is primarily dominated by gas bubbles in the presence of antifreeze peptides. Spherical bubbles facilitate methane migration and potentially accelerate hydrate formation; conversely, the promotion of a cylindrical bubble morphology by two of the designed systems was found to mitigate this effect, leading to slower methane transport and reduced hydrate growth. These findings provide valuable guidance for the design of effective peptide-based inhibitors of natural-gas hydrate formation with potential applications in the energy and environmental sectors. (© 2024 Author(s). Published under an exclusive license by AIP Publishing.) |
| المشرفين على المادة: | 0 (Antifreeze Proteins) OP0UW79H66 (Methane) 059QF0KO0R (Water) 0 (Gases) 0 (Peptides) |
| تواريخ الأحداث: | Date Created: 20240801 Date Completed: 20240801 Latest Revision: 20240801 |
| رمز التحديث: | 20240801 |
| DOI: | 10.1063/5.0211732 |
| PMID: | 39087548 |
| قاعدة البيانات: | MEDLINE |
Find this article in full text from Scitation. | تدمد: | 1089-7690 |
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| DOI: | 10.1063/5.0211732 |