Sphingomyelin analogs with branched N-acyl chains: The position of branching dramatically affects acyl chain order and sterol interactions in bilayer membranes

Jaikishan, Shishir; Björkbom, Anders; Slotte, J. Peter

doi:10.1016/j.bbamem.2010.07.006

Cited by 42 publications

(44 citation statements)

References 56 publications

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“…Cholesterol is known to affect membrane fluidity via its effects on phospholipid acyl chain order [20]. With our bilayer model (POPC: PSM 4:1) cholesterol will increase mostly PSM acyl chain order (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Palmitoyl SM (PSM) was purified from egg SM using preparative HPLC on a reverse phase (C18) column, as described previously [20]. Cholesterol, calcein and Sephacryl S200HR were obtained from Sigma/Aldrich (St. Louis, MO, USA).…”

Section: Methodsmentioning

confidence: 99%

“…With cholesterol, PSM becomes more liquid-ordered [20], and with PCer a gel phase is likely to arise [18,29]. To test for these possibilities, the steady-state anisotropy of tPa-SM was measured.…”

Section: How Does Cholesterol or Pcer Addition To Popc:psm Bilayers Amentioning

confidence: 99%

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Cholesterol stimulates and ceramide inhibits Sticholysin II-induced pore formation in complex bilayer membranes

Alm

García‐Linares

Gavilanes

et al. 2015

Biochimica et Biophysica Acta (BBA) - Biomembranes

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The pore forming capacity of Sticholysin II (StnII; isolated from Stichodactyla helianthus) in bilayer membranes containing 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC), palmitoylsphingomyelin (PSM) and either cholesterol or palmitoyl ceramide (PCer) has been examined. The aim of the study was to elucidate how the presence of differently ordered PSM domains affected StnII oligomerization and pore formation. Cholesterol is known to enhance pore formation by StnII, and our results confirmed this and provide kinetic information for the process. The effect of cholesterol on bilayer permeabilization kinetics was concentration-dependent. In the concentration regime used (2.5-10nmol cholesterol in POPC:PSM 80:20 by nmol), cholesterol also increased the acyl chain order in the fluid PSM domain and thus decreased bilayer fluidity, suggesting that fluidity per se was not responsible for cholesterol's effect. Addition of PCer (2.5-10nmol) to the POPC:PSM (80:20 by nmol) bilayers attenuated StnII-induced pore formation, again in a concentration-dependent fashion. This addition also led to the formation of a PCer-rich gel phase. Addition of cholesterol to PCer-containing membranes could partially reduce the inhibitory effect of PCer on StnII pore formation. We conclude that the physical state of PSM (as influenced by either cholesterol or PCer) affected StnII binding and pore formation under the conditions examined.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Cholesterol stimulates and ceramide inhibits Sticholysin II-induced pore formation in complex bilayer membranes

Alm

García‐Linares

Gavilanes

et al. 2015

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…D- erythro-N -palmitoyl sphingomyelin (PSM) was isolated from egg sphingomyelin as described (38). Cholesterol and Triton X-100 were from Sigma/Aldrich (St. Louis, MO, USA).…”

Section: Methodsmentioning

confidence: 99%

Interaction of 3β-Amino-5-cholestene with Phospholipids in Binary and Ternary Bilayer Membranes

et al. 2011

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3β-Amino-5-cholestene (aminocholesterol) is a synthetic sterol whose properties in bilayer membranes have been examined. In fluid palmitoyl sphingomyelin (PSM) bilayers, aminocholesterol and cholesterol were equally effective in increasing acyl chain order, based on changes in diphenylhexatriene (DPH) anisotropy. In fluid 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) bilayers, aminocholesterol ordered acyl chains, but slightly less efficiently than cholesterol. Aminocholesterol eliminated the PSM and DPPC gel-to-liquid crystalline phase transition enthalpy linearly with concentration, and the enthalpy approached zero at 30 mol% sterol. Whereas cholesterol was able to increase the thermostability of ordered PSM domains in a fluid bilayer, aminocholesterol under equal conditions failed to do this, suggesting that its interaction with PSM was not as favorable as cholesterol’s. In ternary mixed bilayers, containing 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC), PSM or DPPC, and cholesterol at proportions to contain a liquid-ordered phase (60:40 by mol of POPC and PSM or DPPC, and 30 mol% cholesterol), the average life-time of trans parinaric acid (tPA) was close to 20 ns. When cholesterol was replaced with aminocholesterol in such mixed bilayers, the average life-time of tPA was only marginally shorter (about 18 ns). This observation, together with acyl chain ordering data, clearly shows that aminocholesterol was able to form a liquid-ordered phase with saturated PSM or DPPC. We conclude that aminocholesterol should be a good sterol replacement in model membrane systems for which a partial positive charge is deemed beneficial.

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“…Since pure stearoyl SM membrane forms gel phase below the phase transition temperature (44 C) (29), which provides broadened solid-state NMR spectra, it is necessary to measure the spectra above 44 C. In addition, in our previous report (17), we found that there is no critical difference in the 2 H NMR spectra of deuterated SM bilayers between 45 C and 50 C in either the presence or absence of Chol; thus, the NMR spectra were recorded at 45 C for SM and SM-Chol membranes. In membrane environments, lipid molecules undergo fast axial rotation, giving rise to an axially symmetric signal pattern that is defined by the two tensor values d ┴ and d // .…”

Section: And 15 N Csa Of Sm Amidesmentioning

confidence: 99%

Orientation and Order of the Amide Group of Sphingomyelin in Bilayers Determined by Solid-State NMR

Matsumori

Yamaguchi

Maeta

et al. 2015

Biophysical Journal

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Sphingomyelin (SM) and cholesterol (Chol) are considered essential for the formation of lipid rafts; however, the types of molecular interactions involved in this process, such as intermolecular hydrogen bonding, are not well understood. Since, unlike other phospholipids, SM is characterized by the presence of an amide group, it is essential to determine the orientation of the amide and its order in the lipid bilayers to understand the nature of the hydrogen bonds in lipid rafts. For this study, 1'-(13)C-2-(15)N-labeled and 2'-(13)C-2-(15)N-labeled SMs were prepared, and the rotational-axis direction and order parameters of the SM amide in bilayers were determined based on (13)C and (15)N chemical-shift anisotropies and intramolecular (13)C-(15)N dipole coupling constants. Results revealed that the amide orientation was minimally affected by Chol, whereas the order was enhanced significantly in its presence. Thus, Chol likely promotes the formation of an intermolecular hydrogen-bond network involving the SM amide without significantly changing its orientation, providing a higher order to the SM amide. To our knowledge, this study offers new insight into the significance of the SM amide orientation with regard to molecular recognition in lipid rafts, and therefore provides a deeper understanding of the mechanism of their formation.

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Sphingomyelin analogs with branched N-acyl chains: The position of branching dramatically affects acyl chain order and sterol interactions in bilayer membranes

Cited by 42 publications

References 56 publications

Cholesterol stimulates and ceramide inhibits Sticholysin II-induced pore formation in complex bilayer membranes

Cholesterol stimulates and ceramide inhibits Sticholysin II-induced pore formation in complex bilayer membranes

Interaction of 3β-Amino-5-cholestene with Phospholipids in Binary and Ternary Bilayer Membranes

Orientation and Order of the Amide Group of Sphingomyelin in Bilayers Determined by Solid-State NMR

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