Peptide surfactants for cell-free production of functional G protein-coupled receptors

Wu, Xiaoqiang; Corin, Karolina; Philipp, B.; Wienken, Christoph J.; Jerabek‐Willemsen, Moran; Duhr, Stefan; Braun, Dieter; Zhang, Shuguang

doi:10.1073/pnas.1018185108

Cited by 102 publications

(102 citation statements)

References 29 publications

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“…Not only do peptides structurally resemble lipid molecules, but they also exhibit similar surfactant-like properties. Several earlier studies focused on their application as surfactants in membrane protein stabilization [18][19][20][21][22][23]. Their use as antimicrobial agents has also been considered [24,25].…”

Section: Introductionmentioning

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: Introductionmentioning

confidence: 99%

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

et al. 2017

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“…S3A). D and S T were both quantified by microscale thermophoresis (18,26,(28)(29)(30), using an unreactive control monomer lacking sticky ends. To obtain the diffusion and Soret coefficients for multimers, we combined the monomer properties with the scaling laws established in ref.…”

Section: Theorymentioning

confidence: 99%

Escalation of polymerization in a thermal gradient

Mast

Schink

Gerland

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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155

159

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For the emergence of early life, the formation of biopolymers such as RNA is essential. However, the addition of nucleotide monomers to existing oligonucleotides requires millimolar concentrations. Even in such optimistic settings, no polymerization of RNA longer than about 20 bases could be demonstrated. How then could self-replicating ribozymes appear, for which recent experiments suggest a minimal length of 200 nt? Here, we demonstrate a mechanism to bridge this gap: the escalated polymerization of nucleotides by a spatially confined thermal gradient. The gradient accumulates monomers by thermophoresis and convection while retaining longer polymers exponentially better. Polymerization and accumulation become mutually self-enhancing and result in a hyperexponential escalation of polymer length. We describe this escalation theoretically under the conservative assumption of reversible polymerization. Taking into account the separately measured thermophoretic properties of RNA, we extrapolate the results for primordial RNA polymerization inside a temperature gradient in pores or fissures of rocks. With a dilute, nanomolar concentration of monomers the model predicts that a pore length of 5 cm and a temperature difference of 10 K suffice to polymerize 200-mers of RNA in micromolar concentrations. The probability to generate these long RNAs is raised by a factor of >10 600 compared with polymerization in a physical equilibrium. We experimentally validate the theory with the reversible polymerization of DNA blocks in a laser-driven thermal trap. The results confirm that a thermal gradient can significantly enlarge the available sequence space for the emergence of catalytically active polymers. molecular evolution | nonequilibrium | RNA world | (nonenzymatic) emergence of RNA | hydrothermal vents P olymers are the vital building blocks of all known life forms. According to the central dogma of molecular biology (1), DNA stores the information for how and when to build proteins, which for their part carry out catalytic tasks like the polymerization of DNA. How this self-perpetuating cycle has started is unknown. The RNA-world hypothesis posits that RNA molecules were the central players in prebiotic evolution, because they exhibit both a catalytic function similar to that of proteins and the information storage capabilities of DNA (2). However, how could such an RNA world have emerged from the prebiotic soup?A key element of the RNA world is a ribozyme that catalyzes RNA replication. Directed in vitro evolution and engineering have shown that such ribozymes exist, but require a length of 200 bases or more, even in favorable high-salt conditions (3). Starting from chemical nonequilibrium conditions with millimolar concentrations of energy-rich nucleotides (4-6) and with the help of catalytic surfaces (7), only the formation of much shorter polynucleotides on the order of 20 bases was demonstrated in the laboratory. Slow kinetics and cleavage due to hydrolysis limit the formation of long polynucleotides and finally lead...

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“…In addition, microscale thermophoresis measurements showed that one of ORs expressed using peptide surfactants can bind its known ligand heptanal. It indicates that these short and simple peptide surfactants will be able to facilitate the rapid production of ORs, or even other membrane proteins, for the structure and function studies [38]. That provides a convenient solution for the efficient production and natural structure maintenance of ORs in the development of biosensors.…”

Section: Natural Structure Maintenance Of Olfactory Receptorsmentioning

confidence: 98%

Smell Sensors Based on Olfactory Receptor

Zou

2015

Bioinspired Smell and Taste Sensors

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Peptide surfactants for cell-free production of functional G protein-coupled receptors

Cited by 102 publications

References 29 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

Escalation of polymerization in a thermal gradient

Smell Sensors Based on Olfactory Receptor

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