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

Matsumori, Nobuaki; Yamaguchi, Toshiyuki; Maeta, Yoshiko; Murata, Michio

doi:10.1016/j.bpj.2015.05.011

Cited by 29 publications

(24 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Texas-Red 1,2-palmitoyl-sn-glycero-3-phosphoethanolamine and 1-palmitoyl-2-oleoyl-phospatidyl choline (POPC) were purchased from Avanti Polar Lipid (Alabaster, AL). SSM was purified from bovine brain sphingomyelin (Avanti Polar Lipids) by reverse-phase high-performance liquid chromatography (14). Synthesis of ent-SSM (compounds 3 and 4 in Fig.…”

Section: Generalmentioning

confidence: 99%

“…The hydroxybearing chiral center is introduced by subsequent enzymatic reductions to produce D-erythro-sphingomyelin (2S, 3R) (13). These chiral centers likely contribute to the formation of intermolecular hydrogen-bonding, which has long been considered important for lipid-raft formation (14). A previous study using chemically modified sphingomyelins such as 3-O-methylated and 2-N-methylated analogs demonstrated that O-or N-methylation disrupts the intermolecular hydrogen-bonding network, which results in decreased gel formation and reduces the ordering effects of Cho (15).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Sphingomyelin Stereoisomers Reveal That Homophilic Interactions Cause Nanodomain Formation

Yano

Hanashima

Yasuda

et al. 2018

Biophysical Journal

Self Cite

View full text Add to dashboard Cite

Sphingomyelin is an abundant lipid in some cellular membrane domains, such as lipid rafts. Hydrogen bonding and hydrophobic interactions of the lipid with surrounding components such as neighboring sphingomyelin and cholesterol (Cho) are widely considered to stabilize the raft-like liquid-ordered (Lo) domains in membrane bilayers. However, details of their interactions responsible for the formation of Lo domains remain largely unknown. In this study, the enantiomer of stearoyl sphingomyelin (ent-SSM) was prepared, and its physicochemical properties were compared with the natural SSM and the diastereomer of SSM to examine possible stereoselective lipid-lipid interactions. Interestingly, differential scanning calorimetry experiments demonstrated that palmitoyl sphingomyelin, with natural stereochemistry, exhibited higher miscibility with SSM bilayers than with ent-SSM bilayers, indicating that the homophilic sphingomyelin interactions occurred in a stereoselective manner. Solid-state 2 H NMR revealed that Cho elicited its ordering effect very similarly on SSM and ent-SSM (and even on the diastereomer of SSM), suggesting that SSM-Cho interactions are not significantly affected by stereospecific hydrogen bonding. SSM and ent-SSM formed gel-like domains with very similar lateral packing in SSM/Cho/palmitoyloleoyl phosphatidylcholine membranes, as shown by fluorescence lifetime experiments. This observation can be explained by a homophilic hydrogen-bond network, which was largely responsible for the formation of gel-like nanodomains of SSMs (or ent-SSM). Our previous study revealed that Cho-poor gel-like domains contributed significantly to the formation of an Lo phase in sphingomyelin/Cho membranes. The results of the study presented here further show that SSM-SSM interactions occur near the headgroup region, whereas hydrophobic SSM-Cho interactions appeared important in the bilayer interior for Lo domain formation. The homophilic interactions of sphingomyelins could be mainly responsible for the formation of the domains of nanometer size, which may correspond to the small sphingomyelin/Cho-based rafts that temporally occur in biological membranes.

show abstract

Section: Generalmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Sphingomyelin Stereoisomers Reveal That Homophilic Interactions Cause Nanodomain Formation

Yano

Hanashima

Yasuda

et al. 2018

Biophysical Journal

Self Cite

View full text Add to dashboard Cite

show abstract

“…Seventeen different site-selectively deuterated SMs were prepared and site-specific dynamics of SM was revealed in raft and non-raft membranes. In the third approach, the orientation of the SM amide plane in lipid bilayers was analyzed using dipolar couplings and CSAs [166] as described below.…”

Section: Dynamics Of Amphotericin B and Sphingomyelin In Membrane Bilmentioning

confidence: 99%

Dynamic membrane interactions of antibacterial and antifungal biomolecules, and amyloid peptides, revealed by solid-state NMR spectroscopy

Naito

Matsumori

Ramamoorthy

2018

Biochimica et Biophysica Acta (BBA) - General Subjects

Self Cite

View full text Add to dashboard Cite

A variety of biomolecules acting on the cell membrane folds into a biologically active structure in the membrane environment. It is, therefore, important to determine the structures and dynamics of such biomolecules in a membrane environment. While several biophysical techniques are used to obtain low-resolution information, solid-state NMR spectroscopy is one of the most powerful means for determining the structure and dynamics of membrane bound biomolecules such as antibacterial biomolecules and amyloidogenic proteins; unlike X-ray crystallography and solution NMR spectroscopy, applications of solid-state NMR spectroscopy are not limited by non-crystalline, non-soluble nature or molecular size of membrane-associated biomolecules. This review article focuses on the applications of solid-state NMR techniques to study a few selected antibacterial and amyloid peptides. Solid-state NMR studies revealing the membrane inserted bent α-helical structure associated with the hemolytic activity of bee venom melittin and the chemical shift oscillation analysis used to determine the transmembrane structure (with α-helix and 3-helix in the N- and C-termini, respectively) of antibiotic peptide alamethicin are discussed in detail. Oligomerization of an amyloidogenic islet amyloid polypeptide (IAPP, or also known as amylin) resulting from its aggregation in a membrane environment, molecular interactions of the antifungal natural product amphotericin B with ergosterol in lipid bilayers, and the mechanism of lipid raft formation by sphingomyelin studied using solid state NMR methods are also discussed in this review article. This article is part of a Special Issue entitled "Biophysical Exploration of Dynamical Ordering of Biomolecular Systems" edited by Dr. Koichi Kato.

show abstract

“…Total lipid concentration: 500 mM. (d) Conformation of the central region of SM in small isotropic bicelles (SSM/DHPC = 1:2) deduced from 1 H NMR spin–spin coupling constants (blue arrows) and NOEs (red arrows) …”

Section: Lipid‐raft‐related Molecules Conformation and Dynamicsmentioning

confidence: 99%

“…We also utilized small isotropic bicelles composed of SSM and DHPC ( q = 0.5) to determine the conformation of SM in isotropic bicelles on the basis of nuclear Overhauser effects and vicinal 1 H– 1 H coupling constants . The NOESY spectra provided conformationally relevant NOEs such as H‐3/H‐5, H‐2/H‐4, and NH/H‐3 (Figure d).…”

Section: Lipid‐raft‐related Molecules Conformation and Dynamicsmentioning

confidence: 99%

Bioactive Structure of Membrane Lipids and Natural Products Elucidated by a Chemistry‐Based Approach

Murata

Sugiyama

Matsuoka

et al. 2015

The Chemical Record

Self Cite

View full text Add to dashboard Cite

Determining the bioactive structure of membrane lipids is a new concept, which aims to examine the functions of lipids with respect to their three-dimensional structures. As lipids are dynamic by nature, their "structure" does not refer solely to a static picture but also to the local and global motions of the lipid molecules. We consider that interactions with lipids, which are completely defined by their structures, are controlled by the chemical, functional, and conformational matching between lipids and between lipid and protein. In this review, we describe recent advances in understanding the bioactive structures of membrane lipids bound to proteins and related molecules, including some of our recent results. By examining recent works on lipid-raft-related molecules, lipid-protein interactions, and membrane-active natural products, we discuss current perspectives on membrane structural biology.

show abstract

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

Cited by 29 publications

References 48 publications

Sphingomyelin Stereoisomers Reveal That Homophilic Interactions Cause Nanodomain Formation

Sphingomyelin Stereoisomers Reveal That Homophilic Interactions Cause Nanodomain Formation

Dynamic membrane interactions of antibacterial and antifungal biomolecules, and amyloid peptides, revealed by solid-state NMR spectroscopy

Bioactive Structure of Membrane Lipids and Natural Products Elucidated by a Chemistry‐Based Approach

Contact Info

Product

Resources

About