Packing DNA with disc-shaped bicelles

Yang, Ping-Feng; Lin, Tsang–Lang; Lin, Tsung-Yi; Yang, Ching-Hsun; Hu, Yuan; Jeng, U‐Ser

doi:10.1039/c3sm51703a

Cited by 26 publications

(21 citation statements)

References 45 publications

(62 reference statements)

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“…Conventionally, bicelles are discoidal particles composed of long-chain lipids (e.g., 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC)) and short-chain lipids (e.g., 1,2-diheptanoyl-sn-glycero-3-phosphocholine (DHPC)). DMPC forms the bilayer region, whereas DHPC forms a surrounding belt [43,48]. Instead of DHPC, detergents and bile-salt derivatives have also been used [49,50].…”

Section: Peptide-induced Bicelle Formationmentioning

confidence: 99%

Peptide self-assembly into lamellar phases and the formation of lipid-peptide nanostructures

et al. 2017

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Lipids exhibit an extraordinary polymorphism in self-assembled mesophases, with lamellar phases as the most relevant biological representative. To mimic lipid lamellar phases with amphiphilic designer peptides, seven systematically varied short peptides were engineered. Indeed, four peptide candidates (V 4 D, V 4 WD, V 4 WD 2 , I 4 WD 2 ) readily self-assembled into lamellae in aqueous solution. Small-angle X-ray scattering (SAXS) patterns revealed ordered lamellar structures with a repeat distance of ~ 4-5 nm. Transmission electron microscopy (TEM) images confirmed the presence of stacked sheets. Two derivatives (V 3 D and V 4 D 2 ) remained as loose aggregates dispersed in solution; one peptide (L 4 WD 2 ) formed twisted tapes with internal lamellae and an antiparallel β-type monomer alignment. To understand the interaction of peptides with lipids, they were mixed with phosphatidylcholines. Low peptide concentrations (1.1 mM) induced the formation of a heterogeneous mixture of vesicular structures. Large multilamellar vesicles (MLV, d-spacing ~ 6.3 nm) coexisted with oligo-or unilamellar vesicles (~ 50 nm in diameter) and bicelle-like structures (~ 45 nm length, ~ 18 nm width). High peptide concentrations (11 mM) led to unilamellar vesicles (ULV, diameter ~ 260-280 nm) with a homogeneous mixing of lipids and peptides. SAXS revealed the temperature-dependent fine structure of these ULVs. At 25 °C the bilayer is in a fully interdigitated state (headgroup-to-headgroup distance d HH ~ 2.9 nm), whereas at 50 °C this interdigitation opens up (d HH ~ 3.6 nm). Our results highlight the versatility of self-assembled peptide superstructures. Subtle changes in the amino acid composition are key design elements in creating peptide-or lipidpeptide nanostructures with richness in morphology similar to that of naturally occurring lipids.

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Section: Peptide-induced Bicelle Formationmentioning

confidence: 99%

Peptide self-assembly into lamellar phases and the formation of lipid-peptide nanostructures

et al. 2017

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“…6,7 Lipids and polymers have been a preferred choice for designing non-viral carriers, which are often referred to as lipoplexes and polyplexes, respectively. 1 Conjugates formed between NAs and amphiphilic moieties can self-assemble into a wide variety of liquid crystalline polymorphs, 5,8 including multilamellar ("onion-like") arrays, 7 disc-shaped bicelles, 9 hexagonal structures, 10 and cubic phases. 11 Since cell transfection efficiency has been found to be dependent on a number of factors, including charge density and structural features, 12 an accurate understanding of the spatial organization within such transfection complexes is of key importance in order to optimize intracellular cargo delivery.…”

Section: Introductionmentioning

confidence: 99%

Structural behaviour and gene delivery in complexes formed between DNA and arginine-containing peptide amphiphiles

et al. 2016

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We describe in depth the structure of complexes formed between DNA and two classes of arginine-containing peptide amphiphiles, namely, the lipopeptide PRW-C (P = proline, R = arginine, W = tryptophan, C = C16 : 0 alkyl chain) and the bolaamphiphile RFLFR (R = arginine, F = phenylalanine, L = leucine). A combination of X-ray and neutron scattering provided unprecedented insights into the local structure of these complexes. Lipopeptide-based complexes self-assembled into layered structures with large-scale fractal features, hosting DNA in the interstices. Bola-amphiphile scaffolds were characterized by planar structures with DNA strands presumably sandwiched in-between peptide nanotapes. Importantly, complexation did not affect the structural integrity of DNA in either of the two complexes. The bolaamphiphile conjugates displayed high levels of molecular ordering in contrast to the liquid-crystalline features observed in lipopeptide assemblies. Peptide-DNA complexes were assessed for their potential as a means to deliver the reporter vector pEGFP-N1 into SW480 human colon carcinoma cells. Successfully transfected cells expressed green fluorescent protein. The potentiating effect of PRW-C on the cellular uptake of ectopic DNA was found to be much greater than that observed with RFLFR. In contrast to the bolaamphiphile-based conjugate, the liquid-crystalline nature of the lipopeptide complex is likely to play a key role in DNA release and transfection efficiency since these weakly bound structures require lower energy expenditure during disassembly and load release.

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“…Recently, nanodiscs, including protein‐based nanodiscs, peptide‐based nanodiscs, and polymer‐based nanodiscs were increasingly investigated as they provided a near native lipid membrane environment for membrane proteins to be studied in their active forms. Except for single bilayer bicelles and nanodiscs, stacked bicelles or nanodiscs were also developed to provide complexed cell membrane mimetics . However, the formation of cisternae stacks similar to the widely existed multilamellar organelles in cells, such as grana in chloroplast, endoplasmic reticulum, and Golgi apparatus, was rarely reported.…”

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confidence: 99%

Self‐Assembled “Breathing” Grana‐Like Cisternae Stacks

Han

2018

Advanced Materials

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Membranes in cells display elaborate, dynamic morphologies intimately tied to defined cellular functions. Cisternae stacks are a common membrane morphology in cells widely found in organelles. However, compared with the well-studied spherical cell membrane mimics, cisternae stacks as organelle membrane mimics are greatly neglected because of the difficulty of fabricating this unique structure. Herein, the grana-like cisternae stacks are assembled via the reorganization of stacked microsized bicelles to mimic grana functions. The cisternae stacks are connected by fusion regions between adjacent cisternae. The number of cisternae can be controlled from ≈4 to 15 by the variation of ethanol volume percentage. Under the stimulation of solvent or negatively charged nanoparticles, the cisternae stacks can reversibly compress and expand, similar to the "breathing" property of natural grana. During the "breathing" process, nanoparticles are reversibly captured and released. Frequency resonance energy transfer is realized on the cisternae stacks trapped with two kinds of quantum dots. The cisternae stacks provide advanced membrane model for cell biotechnology, and clues for the shaping of organelles composed of cisternae. The ability of the cisternae stacks to capture materials enables them to possibly be applied in biomimetics and the design of advanced functional materials.

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Packing DNA with disc-shaped bicelles

Cited by 26 publications

References 45 publications

Peptide self-assembly into lamellar phases and the formation of lipid-peptide nanostructures

Peptide self-assembly into lamellar phases and the formation of lipid-peptide nanostructures

Structural behaviour and gene delivery in complexes formed between DNA and arginine-containing peptide amphiphiles

Self‐Assembled “Breathing” Grana‐Like Cisternae Stacks

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