دورية أكاديمية
Effects of a N-Maleimide-derivatized Phosphatidylethanolamine on the Architecture and Properties of Lipid Bilayers
العنوان: | Effects of a N-Maleimide-derivatized Phosphatidylethanolamine on the Architecture and Properties of Lipid Bilayers |
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المؤلفون: | Uxue Ballesteros, Emilio J. González-Ramirez, Igor de la Arada, Jesús Sot, Asier Etxaniz, Félix M. Goñi, Alicia Alonso, Lidia Ruth Montes |
المصدر: | International Journal of Molecular Sciences, Vol 24, Iss 23, p 16570 (2023) |
بيانات النشر: | MDPI AG, 2023. |
سنة النشر: | 2023 |
المجموعة: | LCC:Biology (General) LCC:Chemistry |
مصطلحات موضوعية: | maleimide, membrane fluidity, differential scanning calorimetry, fluorescence, infrared spectroscopy, autophagy proteins, Biology (General), QH301-705.5, Chemistry, QD1-999 |
الوصف: | N-maleimide-derivatized phospholipids are often used to facilitate protein anchoring to membranes. In autophagy studies, this is applied to the covalent binding of Atg8, an autophagy protein, to a phosphatidylethanolamine (PE) in the nascent autophagosome. However, the question remains on how closely the N-maleimide PE derivative (PE-mal) mimicks the native PE in the bilayer. In the present paper, spectroscopic and calorimetric techniques have been applied to vesicles containing either PE or PE-mal (together with other phospholipids) to compare the properties of the native and derivatized forms of PE. According to differential scanning calorimetry, and to infrared spectroscopy, the presence of PE-mal did not perturb the fatty acyl chains in the bilayer. Fluorescence spectroscopy and microscopy showed that PE-mal did not alter the bilayer permeability either. However, fluorescence emission polarization of the Laurdan and DPH probes indicated an increased order, or decreased fluidity, in the bilayers containing PE-mal. In addition, the infrared spectral data from the phospholipid phosphate region revealed a PE-mal-induced conformational change in the polar heads, accompanied by increased hydration. Globally considered, the results suggest that PE-mal would be a reasonable substitute for PE in model membranes containing reconstituted proteins. |
نوع الوثيقة: | article |
وصف الملف: | electronic resource |
اللغة: | English |
تدمد: | 24231657 1422-0067 1661-6596 |
Relation: | https://www.mdpi.com/1422-0067/24/23/16570; https://doaj.org/toc/1661-6596; https://doaj.org/toc/1422-0067 |
DOI: | 10.3390/ijms242316570 |
URL الوصول: | https://doaj.org/article/a03b7f2cf3584837a554b1b24fb21f60 |
رقم الأكسشن: | edsdoj.03b7f2cf3584837a554b1b24fb21f60 |
قاعدة البيانات: | Directory of Open Access Journals |
تدمد: | 24231657 14220067 16616596 |
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DOI: | 10.3390/ijms242316570 |