Advances in Biophysics最新文献_第8页

Two-dimensional crystals of apoferritin 载铁蛋白的二维晶体

Advances in Biophysics Pub Date : 1997-01-01 DOI: 10.1016/S0065-227X(97)89634-7

Hideyuki Yoshimura

{"title":"Two-dimensional crystals of apoferritin","authors":"Hideyuki Yoshimura","doi":"10.1016/S0065-227X(97)89634-7","DOIUrl":"10.1016/S0065-227X(97)89634-7","url":null,"abstract":"<div>A simple 2D crystallization method using unfolded protein film as a supporting film of crystals was described, which allows modification of protein surfaces by injecting chemical reagents into the subphase after the crystal formation. As an example, glutaraldehyde was used to cross-link adjacent proteins and then stabilize protein crystals. The second layer of other proteins can also be formed on the apoferritin array using cross-linkers.The array of apoferritin is not only beneficial for electron crystallography but also for practical applications. For example, apoferritin produces a mineral core with a size which can be adjusted by the size to the cavity (i.e. 6 nm). Fabrication of such a small size of well defined fine particles is currently not easy using physical or chemical procedures. Using apoferritin, however, it is easy to produce uniform fine particles. If the core is designed to add interesting properties such as magnetism it is possible to make the highest class of magnetic film with ferritin 2D crystals.Basic researches toward practical applications of 2D protein crystal is now under way in various fields. The well defined size and function of protein molecules will benefit to many applications. The function and crystalline order can be designed by site-directed mutagenesis with the development of protein engineering.</div>","PeriodicalId":50880,"journal":{"name":"Advances in Biophysics","volume":"34 ","pages":"Pages 93-107"},"PeriodicalIF":0.0,"publicationDate":"1997-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0065-227X(97)89634-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20149982","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 19

Supramolecular architectures for the functionalization of solid surfaces 固体表面功能化的超分子结构

Advances in Biophysics Pub Date : 1997-01-01 DOI: 10.1016/S0065-227X(97)89642-6

Wolfgang Knoll , Martha Liley , Darko Piscevic , Jürgen Spinke , Michael J. Tarlov

引用次数: 44

Molecular handling of photosynthetic proteins for molecular assembly construction 光合蛋白在分子组装构建中的分子处理

Advances in Biophysics Pub Date : 1997-01-01 DOI: 10.1016/S0065-227X(97)89635-9

Jun Miyake , Masayuki Hara

引用次数: 5

Criticality found in a model for orientational ordering of protein arrays 在蛋白质阵列定向排序模型中发现了临界性

Advances in Biophysics Pub Date : 1997-01-01 DOI: 10.1016/S0065-227X(97)89631-1

Michiru Hogyoku

引用次数: 5

Lateral forces acting between particles in liquid films or lipid membranes 作用于液体膜或脂质膜中的颗粒之间的侧向力

Advances in Biophysics Pub Date : 1997-01-01 DOI: 10.1016/S0065-227X(97)89629-3

Peter A. Kralchevsky

引用次数: 12

Assembly process of 2D protein arrays in wetting films 二维蛋白质阵列在湿膜中的组装过程

Advances in Biophysics Pub Date : 1997-01-01 DOI: 10.1016/S0065-227X(97)89633-5

Eiki Adachi , Kuniaki Nagayama

引用次数: 8

Assembly of protein structures on liposomes by non-specific and specific interactions 通过非特异性和特异性相互作用在脂质体上组装蛋白质结构

Advances in Biophysics Pub Date : 1997-01-01 DOI: 10.1016/S0065-227X(97)89637-2

Orlin D. Velev

{"title":"Assembly of protein structures on liposomes by non-specific and specific interactions","authors":"Orlin D. Velev","doi":"10.1016/S0065-227X(97)89637-2","DOIUrl":"10.1016/S0065-227X(97)89637-2","url":null,"abstract":"<div>We investigate different schemes for fabrication of nanometer sized assemblies that consist of a liposome core over which a shell of ferritin is attached. Three distinct interactions were used for this assembly: <ul><li>1.(i) Electrostatic attraction. The liposomes are charged by the presence of cationic surfactant (HTAB) and at an appropriate pH collect the ferritin molecules into a 2D-ordered ferritin shell. The protein shells can be fixed by glutaraldehyde. Next, the liposomes can be removed by solubilisation, leaving behind ordered ferritin clusters.</li><li>2.(ii) Specific avidin-biotin or streptavidin-biotin binding. The ferritin molecules are conjugated to avidin or streptavidin and the liposomes incorporate biotinylated lipid. We found that the specific binding can be completely blocked by unfavourable electrostatic repulsion. To adjust the appropriate liposome charge we include cationic surfactant in the lipid layer. Thus, to accomplish the assembly process, we need to design and modify both the specific and non-specific colloid interactions in the system. The result is liposomes heavily coated with a strongly and specifically attached ferritin layer.</li><li>3.(iii) Specific polysaccharide/lectin binding. The liposomes are first coated with a cholesterol-anchored mannan layer. The ferritin molecules are conjugated with Con A that binds to the polysaccharide. A smooth and dense coating with ferritin is obtained (Fig. 3b).</li></ul>The acquired data can find application in the future fabrication of microstructured, multicomponent, or functionalised protein and liposome/protein assemblies.</div>","PeriodicalId":50880,"journal":{"name":"Advances in Biophysics","volume":"34 ","pages":"Pages 139-157"},"PeriodicalIF":0.0,"publicationDate":"1997-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0065-227X(97)89637-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20149985","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 17

Advances in S-layer nanotechnology and biomimetics s层纳米技术和仿生学研究进展

Advances in Biophysics Pub Date : 1997-01-01 DOI: 10.1016/S0065-227X(97)89632-3

Uwe B. Sleytr, Dietmar Pum, Margit Sára

引用次数: 24

Supramolecular assembly using helical peptides 利用螺旋肽进行超分子组装

Advances in Biophysics Pub Date : 1997-01-01 DOI: 10.1016/S0065-227X(97)89636-0

Katsuhiko Fujita , Shunsaku Kimura , Yukio Imanishi , Elmar Rump , Helmut Ringsdorf

{"title":"Supramolecular assembly using helical peptides","authors":"Katsuhiko Fujita , Shunsaku Kimura , Yukio Imanishi , Elmar Rump , Helmut Ringsdorf","doi":"10.1016/S0065-227X(97)89636-0","DOIUrl":"10.1016/S0065-227X(97)89636-0","url":null,"abstract":"<div>We investigated supramolecular assemblies of various hydrophobic helical peptides. The assemblies were formed at the air/water interface or in aqueous medium. The hexadecapeptide, Boc-(Ala-Aib)8-OMe (BA16M), was reported to take α-helical structure by X-ray analysis. Several derivatives were prepared, which have the repeating sequence of Ala-Aib, Lys(Z)-Aib or Leu-Aib, or have the terminal chemically modified. CD spectra of the peptides indicated helical conformation in ethanol solution. The surface pressure-area isotherms of the peptide monolayers showed an inflection at the surface area corresponding to the cross section along the helix axis, and the monolayers were collapsed by further compression. All the helical peptides oriented their helix axis parallel to the air/water interface on the basis of the results of transmission IR spectra and RAS of the monolayers transferred onto substrates.A small mound was observed in the isotherm of BA16M and other derivatives, which was ascribed to the phase transition from the liquid state to the solid state. One mol% of FITC-labeled peptide was mixed into the monolayers to visualize the phase separation of the solid and liquid states at the surface pressure of the coexisting region. Various shapes of the dark domain were observed at the top of the mound in the isotherms by fluorescence microscopy. The helical peptides formed two-dimensional crystals at the air/water interface when they were compressed to the solid state.An amino-terminated helical peptide, HA16B, was suspended in an aqueous medium by a sonication method and transparent dispersion was obtained. The dynamic light scattering measurement of the dispersion revealed the particle size of 75 nm with a narrow size distribution. The molecular assembly of the helical peptide in water was called “Peptosome”, because it takes a vesicular structure.</div>","PeriodicalId":50880,"journal":{"name":"Advances in Biophysics","volume":"34 ","pages":"Pages 127-137"},"PeriodicalIF":0.0,"publicationDate":"1997-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0065-227X(97)89636-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20149984","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 8

Protein arrays: Concepts and subjects 蛋白质阵列:概念和主题

Advances in Biophysics Pub Date : 1997-01-01 DOI: 10.1016/S0065-227X(97)89628-1

Kuniaki Nagayama

引用次数: 16