Self-Reproduction of Nanoparticles through Synergistic Self-Assembly

Ikeda, Keisuke; Nakano, Minoru

doi:10.1021/la503491p

Cited by 11 publications

(10 citation statements)

References 32 publications

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“…Mimetic or fragment peptides of apoA‐I that have amphipathic helical motif with a specific distribution of nonpolar and charged/polar amino acid residues (called ‘class A’) are known to form discoidal complexes with phospholipids similar to apoA‐I . A model peptide with 18 amino acids Ac‐DWLKAFYDKVAEKLKEAF‐NH 2 (2F) was designed to mimic apoA‐I relating to the class A amphipathic α ‐helix .…”

Section: Introductionmentioning

confidence: 99%

“…A 23 amino acid monomeric peptide corresponding to the helix 10 of human apoA‐I had an ability to modulate diameters of nanodiscs from 9 to 15 nm by varying DMPC/peptide ratios . In addition, apoA‐I mimetic peptides are able to spontaneously solubilize vesicles composed of physiological phospholipid, 1‐palmitoyl‐2‐oleoyl phosphatidylcholine (POPC), into nanodiscs without using detergent . This property is advantageous for apoA‐I mimetic peptides as scaffolding nanodiscs because apoA‐I cannot solubilize POPC at physiological pH .…”

Section: Introductionmentioning

confidence: 99%

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Formation of stable nanodiscs by bihelical apolipoprotein A‐I mimetic peptide

Kariyazono

Nadai

Miyajima

et al. 2016

Journal of Peptide Science

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Nanodiscs are composed of scaffold protein or peptide such as apolipoprotein A-I (apoA-I) and phospholipids. Although peptide-based nanodiscs have an advantage to modulate the size of nanodiscs by changing phospholipid/peptide ratios, they are usually less stable than apoA-I-based nanodiscs. In this study, we designed a novel nanodisc scaffold peptide (NSP) that has proline-punctuated bihelical amphipathic structure based on apoA-I mimetic peptides. NSP formed α-helical structure on 1-palmitoyl-2-oleoyl phosphatidylcholine (POPC) nanodiscs prepared by cholate dialysis method. Dynamic light scattering measurements demonstrated that diameters of NSP nanodiscs vary depending upon POPC/NSP ratios. Comparison of thermal unfolding of nanodiscs monitored by circular dichroism measurements demonstrated that NSP forms much more stable nanodiscs with POPC than monohelical peptide, 4F, exhibiting comparable stability to apoA-I-POPC nanodiscs. Intrinsic Trp fluorescence measurements showed that Trp residues of NSP exhibit more hydrophobic environment than that of 4 F on nanodiscs, suggesting the stronger interaction of NSP with phospholipids. Thus, the bihelical structure of NSP appears to increase the stability of nanodiscs because of the enhanced interaction of peptides with phospholipids. In addition, NSP as well as 4F spontaneously solubilized POPC vesicles into nanodiscs without using detergent. These results indicate that bihelical NSP forms nanodiscs with comparable stability to apoA-I and has an ability to control the size of nanodiscs simply by changing phospholipid/peptide ratios.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Formation of stable nanodiscs by bihelical apolipoprotein A‐I mimetic peptide

Kariyazono

Nadai

Miyajima

et al. 2016

Journal of Peptide Science

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“…A large range of mimetic peptides can modulate the diameter of the discs. The main advantage of mimetic peptides is their ability to solubilise vesicles into nanodiscs at physiological conditions without detergent [55,56]. Due to the lack of stability of some peptide discs, a range of different mimetic peptides with various features is being developed with promising results [57].…”

Section: Artificial Discs a Nanodiscsmentioning

confidence: 99%

Artificial membranes for membrane protein purification, functionality and structure studies

Parmar

Lousa

Muench

et al. 2016

Biochemical Society Transactions

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Membrane proteins represent one of the most important targets for pharmaceutical companies. Unfortunately, technical limitations have long been a major hindrance in our understanding of the function and structure of such proteins. Recent years have seen the refinement of classical approaches and the emergence of new technologies that have resulted in a significant step forward in the field of membrane protein research. This review summarises some of the current techniques used for studying membrane proteins, with overall advantages and drawbacks for each method. Micelles and classical detergent techniquesMembrane proteins account for~30% of both prokaryotic and eukaryotic proteins [1]. Integral proteins such as transporters or ion channels, as well as peripheral membrane proteins such as G-proteins, all perform essential tasks in signal transduction, cell metabolism and transport of small molecules [2][3][4]. Integral and peripheral membrane proteins are respectively embedded in or closely associated with the phospholipid bilayer of cell membranes. Therefore, their function often relies on their precise lipid environment [5,6]. For instance, cardiolipin, which constitutes about 20% of the inner mitochondrial membrane, is essential to the function of many mitochondrial transporters such as the ADP/ATP carriers, the enzymes of the respiratory chain, and bacterial proteins [7][8][9]. This is because cardiolipin offers polar and electrostatic interactions that increase protein stability[10]; similar interactions have been observed for other lipids [11,12]. Unfortunately, classical techniques to study membrane proteins involve the use of detergents that solubilise the protein but also destabilise its interaction with membrane lipids. In many cases, membrane proteins may be stable in only a few detergents, limiting the range of conditions that can be used for crystallization trials [13]. Consequently, much time is spent testing various detergents in different ratios and concentrations in the hope of finding conditions that will mimic the essential interactions of the protein with its natural lipidic environment -and this way stabilise the protein and preserve its functional state. These problems have hindered membrane protein research for many years: both biophysical characterisation and structure solution have suffered due to difficulties of extracting proteins from membranes and keeping them stable away from their native environment. The past few years have seen the emergence of new techniques aimed at providing a membrane-like natural environment. These novel techniques include liposomes, bicelles, discs, polymer and lipids based strategies.

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“…Though a spontaneous exchange of lipids in vesicles has been well studied before, 14,15 a dynamic equilibrium between peptide and lipids enables constant exchange of lipids in peptide derived nanodiscs. 5,6 The rate of lipid exchange is faster in peptide nanodiscs as compared to that observed in vesicles, whereas the MSP based nanodiscs exhibit extremely slow lipid exchange. 16−18 This dynamic nature was attributed to the presence of breaks in the belt (or the spacing between peptides) surrounding the lipid bilayer nanodisc.…”

mentioning

confidence: 99%

“…Controlled self-assembly of lipids and proteins/peptides, inspired from high density lipoprotein (HDL) particles (called as nanodiscs), is increasingly utilized to provide a native-like environment to study the structure and function of membrane proteins. Nanodiscs are disc shaped lipid bilayers surrounded by a rim of amphipathic belt protein. , The rim of a nanodisc is made up of a protein called membrane scaffold protein (MSP). , Amphipathic peptides − derived from MSP have also been shown to form nanodiscs; and polymers − have also been shown to from nanodiscs. Peptide based nanodiscs can be prepared by simply mixing lipid and peptide, and do not require a detergent unlike the production of MSP based nanodiscs. , The size of nanodiscs can be controlled by changing the lipid-to-peptide ratio.…”

mentioning

confidence: 99%