Imidazole Headgroup Phospholipid Shows Asymmetric Distribution in Vesicles and Zinc-Dependent Esterase Activity
Artificial lipids have become increasingly important in generating novel nanoenzymes and nanoparticles. Imidazole has been well established as a versatile catalyst in synthetic chemistry and through its related amino acid histidine in enzymes. By exploiting the transphosphatidylation reaction of pho...
Saved in:
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2024-10-01
|
| Series: | Biomolecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2218-273X/14/11/1363 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1850216793415614464 |
|---|---|
| author | Gabriela Sachet-Fernandez James W. Hindley Oscar Ces Rüdiger Woscholski |
| author_facet | Gabriela Sachet-Fernandez James W. Hindley Oscar Ces Rüdiger Woscholski |
| author_sort | Gabriela Sachet-Fernandez |
| collection | DOAJ |
| description | Artificial lipids have become increasingly important in generating novel nanoenzymes and nanoparticles. Imidazole has been well established as a versatile catalyst in synthetic chemistry and through its related amino acid histidine in enzymes. By exploiting the transphosphatidylation reaction of phospholipase D, the choline headgroup of phosphatidyl choline was exchanged for the imidazole moiety containing histidinol. Here, we introduce a novel phosphatidylhistidinol (PtdHisOH) lipid and characterise it with respect to its catalytic abilities and its ability to modulate vesicle size. Our data reveal a zinc-dependent esterase activity that was strongest in vesicles and micelles, with slower catalytic rates being observed in flat lipid presentation systems and two-phase systems, indicating the importance of surface presentation and curvature effects on the catalytic activity of PtdHisOH. Such lipids offer the opportunity to impart de novo catalytic functionality to self-assembled lipid systems such as synthetic cells, leading to the development of new technologies for biocatalysis applications. |
| format | Article |
| id | doaj-art-7d4028168ac24733bd0aea63fc363f2b |
| institution | OA Journals |
| issn | 2218-273X |
| language | English |
| publishDate | 2024-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj-art-7d4028168ac24733bd0aea63fc363f2b2025-08-20T02:08:12ZengMDPI AGBiomolecules2218-273X2024-10-011411136310.3390/biom14111363Imidazole Headgroup Phospholipid Shows Asymmetric Distribution in Vesicles and Zinc-Dependent Esterase ActivityGabriela Sachet-Fernandez0James W. Hindley1Oscar Ces2Rüdiger Woscholski3Department of Chemistry, Molecular Sciences Research Hub, Imperial College London, London W12 0BZ, UKDepartment of Chemistry, Molecular Sciences Research Hub, Imperial College London, London W12 0BZ, UKDepartment of Chemistry, Molecular Sciences Research Hub, Imperial College London, London W12 0BZ, UKDepartment of Chemistry, Molecular Sciences Research Hub, Imperial College London, London W12 0BZ, UKArtificial lipids have become increasingly important in generating novel nanoenzymes and nanoparticles. Imidazole has been well established as a versatile catalyst in synthetic chemistry and through its related amino acid histidine in enzymes. By exploiting the transphosphatidylation reaction of phospholipase D, the choline headgroup of phosphatidyl choline was exchanged for the imidazole moiety containing histidinol. Here, we introduce a novel phosphatidylhistidinol (PtdHisOH) lipid and characterise it with respect to its catalytic abilities and its ability to modulate vesicle size. Our data reveal a zinc-dependent esterase activity that was strongest in vesicles and micelles, with slower catalytic rates being observed in flat lipid presentation systems and two-phase systems, indicating the importance of surface presentation and curvature effects on the catalytic activity of PtdHisOH. Such lipids offer the opportunity to impart de novo catalytic functionality to self-assembled lipid systems such as synthetic cells, leading to the development of new technologies for biocatalysis applications.https://www.mdpi.com/2218-273X/14/11/1363phospholipase Denzyme-assisted synthesisallosterictemperaturealcohollipid |
| spellingShingle | Gabriela Sachet-Fernandez James W. Hindley Oscar Ces Rüdiger Woscholski Imidazole Headgroup Phospholipid Shows Asymmetric Distribution in Vesicles and Zinc-Dependent Esterase Activity Biomolecules phospholipase D enzyme-assisted synthesis allosteric temperature alcohol lipid |
| title | Imidazole Headgroup Phospholipid Shows Asymmetric Distribution in Vesicles and Zinc-Dependent Esterase Activity |
| title_full | Imidazole Headgroup Phospholipid Shows Asymmetric Distribution in Vesicles and Zinc-Dependent Esterase Activity |
| title_fullStr | Imidazole Headgroup Phospholipid Shows Asymmetric Distribution in Vesicles and Zinc-Dependent Esterase Activity |
| title_full_unstemmed | Imidazole Headgroup Phospholipid Shows Asymmetric Distribution in Vesicles and Zinc-Dependent Esterase Activity |
| title_short | Imidazole Headgroup Phospholipid Shows Asymmetric Distribution in Vesicles and Zinc-Dependent Esterase Activity |
| title_sort | imidazole headgroup phospholipid shows asymmetric distribution in vesicles and zinc dependent esterase activity |
| topic | phospholipase D enzyme-assisted synthesis allosteric temperature alcohol lipid |
| url | https://www.mdpi.com/2218-273X/14/11/1363 |
| work_keys_str_mv | AT gabrielasachetfernandez imidazoleheadgroupphospholipidshowsasymmetricdistributioninvesiclesandzincdependentesteraseactivity AT jameswhindley imidazoleheadgroupphospholipidshowsasymmetricdistributioninvesiclesandzincdependentesteraseactivity AT oscarces imidazoleheadgroupphospholipidshowsasymmetricdistributioninvesiclesandzincdependentesteraseactivity AT rudigerwoscholski imidazoleheadgroupphospholipidshowsasymmetricdistributioninvesiclesandzincdependentesteraseactivity |