Correlation between the hydration of acyl chains and phosphate groups in lipid bilayers: Effect of phase state, head group, chain length, double bonds and carbonyl groups

Rosa, Antonio Sebastián; Cejas, Jimena P.; Disalvo, E.A.; Frías, María A.

doi:10.1016/j.bbamem.2019.03.018

Cited by 12 publications

(25 citation statements)

References 49 publications

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“…This shows that the degree of hydration increased very sharply with increasing CT concentration. The significant role of water in the acyl chain region of liposomes has been confirmed by others [ 44 , 47 ].…”

Section: Discussionsupporting

confidence: 55%

“…In the liquid crystalline phase, we observed that increasing presence of CT decreased membrane ordering and lowered packing density, leading to increased hydration. The observed increased packing density and bilayer ordering at higher CT concentration above T m was ascribed to water molecules entering the acyl chain region, which stabilized this region, potentially contributing to the observed increased bilayer stability [ 47 , 53 ].…”

Section: Discussionmentioning

confidence: 99%

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Phase Transitions and Structural Changes in DPPC Liposomes Induced by a 1-Carba-Alpha-Tocopherol Analogue

et al. 2021

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Steady-state emission spectroscopy of 1-anilino-8- naphthalene sulfonate (ANS) and 1,6-diphenyl-1,3,5-hexatriene (DPH), fluorescence anisotropy, and DSC methods were used to characterize the interactions of the newly synthesized 1-carba-alpha-tocopherol (CT) with a 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) membrane. The DSC results showed significant perturbations in the DPPC structure for CT concentrations as low as 2 mol%. The main phase transition peak was broadened and shifted to lower temperatures in a concentration-dependent manner, and pretransition was abolished. Increasing CT concentrations induced the formation of new phases in the DPPC structure, leading to melting at lower temperatures and, finally, disruption of the ordered DPPC structure. Hydration and structural changes of the DPPC liposomes using ANS and DPH fluorescent probes, which are selectively located at different places in the bilayer, were studied. With the increased concentration of CT molecules in the DPPC liposomes, structural changes with the simultaneous formation of different phases of such mixture were observed. Temperature studies of such mixtures revealed a decrease in the temperature of the main phase transition and fluidization at decreasing temperatures related to increasing hydration in the bilayer. Contour plots obtained from concentration–temperature data with fluorescent probes allowed for identification of different phases, such as gel, ordered liquid, disordered liquid, and liquid crystalline phases. The CT molecule with a modified chromanol ring embedded in the bilayer led to H-bonding interactions, expelling water molecules from the interphase, thus introducing disorder and structural changes to the highly ordered gel phase.

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Section: Discussionsupporting

confidence: 55%

Section: Discussionmentioning

confidence: 99%

Phase Transitions and Structural Changes in DPPC Liposomes Induced by a 1-Carba-Alpha-Tocopherol Analogue

et al. 2021

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“…In the case of desiccation, the volume change that occurs as water is lost causes membrane lipids to become closely packed into the gel phase (Fig. 2 d and e), even if the membrane composition is unchanged [ 47 ]. When a desiccated membrane is rehydrated, the transition from the gel phase back to the liquid crystal phase does not occur uniformly across the membrane; some regions remain packed in the gel phase while others spread out in the liquid crystal phase (Fig.…”

Section: Main Textmentioning

confidence: 99%

The biology of tardigrade disordered proteins in extreme stress tolerance

Hesgrove

Boothby

2020

Cell Commun Signal

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Disordered proteins have long been known to help mediate tolerance to different abiotic stresses including freezing, osmotic stress, high temperatures, and desiccation in a diverse set of organisms. Recently, three novel families of intrinsically disordered proteins were identified in tardigrades, microscopic animals capable of surviving a battery of environmental extremes. These three families include the Cytoplasmic-, Secreted-, and Mitochondrial- Abundant Heat Soluble (CAHS, SAHS, and MAHS) proteins, which are collectively termed Tardigrade Disordered Proteins (TDPs). At the level of sequence conservation TDPs are unique to tardigrades, and beyond their high degree of disorder the CAHS, SAHS, and MAHS families do not resemble one another. All three families are either highly expressed constitutively, or significantly enriched in response to desiccation. In vivo, ex vivo, and in vitro experiments indicate functional roles for members of each TDP family in mitigating cellular perturbations induced by various abiotic stresses. What is currently lacking is a comprehensive and holistic understanding of the fundamental mechanisms by which TDPs function, and the properties of TDPs that allow them to function via those mechanisms. A quantitative and systematic approach is needed to identify precisely what cellular damage TDPs work to prevent, what sequence features are important for these functions, and how those sequence features contribute to the underlying mechanisms of protection. Such an approach will inform us not only about these fascinating proteins, but will also provide insights into how the sequence of a disordered protein can dictate its functional, structural, and dynamic properties. Graphical abstract

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“…Moreover, hydration of each of these regions is correlated. The water-phosphate interaction is enhanced when carbonyl groups are absent [11,12]. It has been shown using a combination of fluorescent spectroscopy, FTIR-ATR analysis and monolayer surface pressure/area isotherms that the population of relaxable water molecules is increased in ether in comparison to ester PC [13].…”

Section: J O U R N a L P R E -P R O O Fmentioning

confidence: 99%

“…It is understood that in the absence of CO groups the hydrogen bonds with the phosphate groups are strengthen [12,16,17]. Thus, the water molecules form with the phosphate a tighter first hydration shell making, in consequence, a looser second hydration one.…”

Section: J O U R N a L P R E -P R O O Fmentioning

confidence: 99%

Effect of cholesterol on the hydration properties of ester and ether lipid membrane interphases

Pérez

Alarcón

Verde

et al. 2021

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Correlation between the hydration of acyl chains and phosphate groups in lipid bilayers: Effect of phase state, head group, chain length, double bonds and carbonyl groups

Cited by 12 publications

References 49 publications

Phase Transitions and Structural Changes in DPPC Liposomes Induced by a 1-Carba-Alpha-Tocopherol Analogue

Phase Transitions and Structural Changes in DPPC Liposomes Induced by a 1-Carba-Alpha-Tocopherol Analogue

The biology of tardigrade disordered proteins in extreme stress tolerance

Effect of cholesterol on the hydration properties of ester and ether lipid membrane interphases

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