Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1863, Issue 8, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.bbamem.2021.183628
Keywords
Biomimetic model membranes; Lyotropic phases; 1-deoxy-sphingolipids; Fluorescence spectroscopy
Categories
Funding
- Fundacao para a Ciencia e Tecnologia (FCT), Portugal [PTDC/BBB-BQB/3710/2014, PTDC/BIA-BFS/29448/2017, UIDB/04565/2020, UIDP/04138/2020, SAICTAC/0019/2015, SFRH/BD/102933/2014, IST -ID/105/2018]
- Investigador FCT [IF/00437/2014]
- Fundação para a Ciência e a Tecnologia [PTDC/BBB-BQB/3710/2014, SFRH/BD/102933/2014, PTDC/BIA-BFS/29448/2017] Funding Source: FCT
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1-deoxy(methyl)-sphingolipids induce unique changes in the biophysical properties of membranes, suggesting that these alterations might trigger the patho-biological actions of these lipids.
1-deoxy-sphingolipids, also known as atypical sphingolipids, are directly implicated in the development and progression of hereditary sensory and autonomic neuropathy type 1 and diabetes type 2. The mechanisms underlying their patho-physiological actions are yet to be elucidated. Accumulating evidence suggests that the biological actions of canonical sphingolipids are triggered by changes promoted on membrane organization and biophysical properties. However, little is known regarding the biophysical implications of atypical sphingolipids. In this study, we performed a comprehensive characterization of the effects of the naturally occurring 1-deoxy-dihydroceramide, 1-deoxy-ceramide(Delta 14Z) and 1-deoxymethyl-ceramide(Delta 3E) in the properties of a fluid membrane. In addition, to better define which structural features determine sphingolipid ability to form ordered domains, the synthetic 1-O-methyl-ceramide(Delta 4E) and 1-deoxy-ceramide(Delta 4E) were also studied. Our results show that natural and synthetic 1-deoxy(methyl)-sphingolipids fail to laterally segregate into ordered domains as efficiently as the canonical C16-ceramide. The impaired ability of atypical sphingolipids to form ordered domains was more dependent on the presence, position, and configuration of the sphingoid base double bond than on the structure of its C1 functional group, due to packing constraints introduced by an unsaturated backbone. Nonetheless, absence of a hydrogen bond donor and acceptor group at the C1 position strongly reduced the capacity of atypical sphingolipids to form gel domains. Altogether, the results showed that 1-deoxy(methyl)-sphingolipids induce unique changes on the biophysical properties of the membranes, suggesting that these alterations might, in part, trigger the patho-biological actions of these lipids.
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