Claus-W. von der Lieth , Martin Frank , Thisbe K. Lindhorst
{"title":"Molecular dynamics simulations of glycoclusters and glycodendrimers","authors":"Claus-W. von der Lieth , Martin Frank , Thisbe K. Lindhorst","doi":"10.1016/S1389-0352(01)00072-1","DOIUrl":"10.1016/S1389-0352(01)00072-1","url":null,"abstract":"<div><p><span>Protein–carbohydrate recognition plays a crucial role in a wide range of biological processes, required both for normal physiological functions and the onset of disease. Nature uses multivalency in carbohydrate–protein interactions as a strategy to overcome the low affinity found for singular binding of an individual </span>saccharide<span> epitope to a single carbohydrate recognition domain of a lectin<span>. To mimic the complex multi-branched oligosaccharides<span><span> found in glycoconjugates, which form the structural basis of multivalent carbohydrate–protein interactions, so-called glycoclusters and glycodendrimers have been designed to serve as high-affinity ligands of the respective receptor proteins. To allow a rational design of glycodendrimer-type molecules with regard to the receptor structures involved in carbohydrate recognition, a deeper knowledge of the dynamics of such molecules is desirable. Most glycodendrimers have to be considered highly flexible molecules with their conformational preferences most difficult to elucidate by experimental methods. Longtime molecular dynamics (MD) simulations with inclusion of explicit solvent molecules are suited to explore the conformational space accessible to glycodendrimers. Here, a detailed geometric and conformational analysis of 15 glycodendrimers and glycoclusters has been accomplished, which differ with regard to their core moieties, spacer characteristics and the type of terminal carbohydrate units. It is shown that the accessible conformational space depends strongly on the structural features of the core and spacer moieties and even on the type of terminating sugars. The obtained knowledge about possible spatial distributions of the sugar epitopes exposed on the investigated hyperbranched </span>neoglycoconjugates is detailed for all examples and forms important information for the interpretation and prediction of affinity data, which can be deduced from biological testing of these multivalent neoglycoconjugates.</span></span></span></p></div>","PeriodicalId":101090,"journal":{"name":"Reviews in Molecular Biotechnology","volume":"90 3","pages":"Pages 311-337"},"PeriodicalIF":0.0,"publicationDate":"2002-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1389-0352(01)00072-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"56530710","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}
Stephan Diekmann , Jennie Weston , Ernst Anders , Wilhelm Boland , Bruno Schönecker , Thomas Hettmann , Johannes von Langen , Stefan Erhardt , Michael Mauksch , Michael Bräuer , Christoph Beckmann , Matthias Rost , Petra Sperling , Ernst Heinz
{"title":"Metal-mediated reactions modeled after nature","authors":"Stephan Diekmann , Jennie Weston , Ernst Anders , Wilhelm Boland , Bruno Schönecker , Thomas Hettmann , Johannes von Langen , Stefan Erhardt , Michael Mauksch , Michael Bräuer , Christoph Beckmann , Matthias Rost , Petra Sperling , Ernst Heinz","doi":"10.1016/S1389-0352(01)00067-8","DOIUrl":"10.1016/S1389-0352(01)00067-8","url":null,"abstract":"<div><p><span>The Collaborative Research Center (CRC) 436 ‘Metal-Mediated Reactions Modeled after Nature’ was founded for the express purpose of analyzing the catalytic principles of metallo-enzymes in order to construct efficient catalysts on a chemical basis. The structure of the active center and neighboring chemical environment in enzymes serves as a focal point for developing reactivity models for the chemical redesign of catalysts. Instead of simply copying enzyme construction, we strive to achieve new chemical intuition based on the results of long-lasting natural evolution. We hope for success, since nature uses a limited set of building blocks, whereas we can apply the full repertoire of chemistry. Key substrates in this approach are small molecules, such as CO</span><sub>2</sub>, O<sub>2</sub>, NO<sub>3</sub><sup>−</sup> and N<sub>2</sub><span>. Nature complexes these substrates, activates them and performs chemical transformations — all within the active center of a metalloenzyme. In this article, we report on some aspects and first results of the Collaborative Research Center (CRC) 436, such as nitrate reductase<span>, sphingolipid<span> desaturase, carbonic anhydrase<span>, leucine<span> aminopeptidase and dopamine β-monooxygenase.</span></span></span></span></span></p></div>","PeriodicalId":101090,"journal":{"name":"Reviews in Molecular Biotechnology","volume":"90 2","pages":"Pages 73-94"},"PeriodicalIF":0.0,"publicationDate":"2002-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1389-0352(01)00067-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"56530575","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}
{"title":"Recent progress in artificial receptors for phosphate anions in aqueous solution","authors":"Shin Aoki, Eiichi Kimura","doi":"10.1016/S1389-0352(01)00070-8","DOIUrl":"10.1016/S1389-0352(01)00070-8","url":null,"abstract":"<div><p><span><span><span>Phosphate esters exist ubiquitously in nature in the form of nucleoside phosphates<span> (nucleotides) as components of RNA (or DNA), sugar nucleotides for </span></span>glycosylation<span> of oligosaccharides<span><span> or proteins, activated form of proteins responding to extracellular signals, and chemical mediators playing central roles in intracellular signaling signals. Phosphorylation of anti-viral nucleoside analogues by intracellular kinases yields nucleoside phosphates (nucleotide) as biologically active forms as anti-viral agents. Development of artificial phosphate receptors would afford new methodologies for detection, separation, or transport of biologically important phosphates. Herein, a recent progress of artificial phosphate receptors is reviewed with special focus on macrocyclic polyamines and their metal complexes as a new prototype. In comparison to most of the previous artificial receptors (most of them are organic molecules), our system characteristically works in aqueous solution at neutral pH with extremely strong affinities with phosphate anions. Moreover, zinc(II)–macrocyclic tetraamine (cyclen) complexes were discovered to selectively bind </span>thymine and </span></span></span>uracil, so that nucleotides of these bases are specifically recognized by the bis(Zn</span><sup>2+</sup>–cyclen) complexes.</p></div>","PeriodicalId":101090,"journal":{"name":"Reviews in Molecular Biotechnology","volume":"90 2","pages":"Pages 129-155"},"PeriodicalIF":0.0,"publicationDate":"2002-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1389-0352(01)00070-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"56530611","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}
{"title":"Development of environmentally friendly syntheses: use of enzymes and biomimetic systems for the direct carboxylation of organic substrates","authors":"Michele Aresta, Angela Dibenedetto","doi":"10.1016/S1389-0352(01)00069-1","DOIUrl":"10.1016/S1389-0352(01)00069-1","url":null,"abstract":"<div><p>Carboxylation reactions<span> widely occur in nature by the direct use of carbon dioxide or hydrogen carbonate and are mediated by enzymes, which may or may not have a metal as an active center. Such direct carboxylation reactions have found only very few applications for synthetic purposes at industrial level. In this paper we review a part of the work we have done on the use of carbon dioxide and describe: (i) the use of a carboxylation enzyme for the conversion of phenol into 4-OH benzoic acid; and (ii) the potential of biomimetic mixed anhydrides for the synthesis of compounds of industrial interest. The enzymatic production of acetic acid from carbon dioxide is compared with known and new transition metal catalyzed reactions that are fully biomimetic.</span></p></div>","PeriodicalId":101090,"journal":{"name":"Reviews in Molecular Biotechnology","volume":"90 2","pages":"Pages 113-128"},"PeriodicalIF":0.0,"publicationDate":"2002-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1389-0352(01)00069-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"56530596","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}
Ingrid Blain, Patrick Slama, Michel Giorgi, Thierry Tron, Marius Réglier
{"title":"Copper-containing monooxygenases: enzymatic and biomimetic studies of the O-atom transfer catalysis","authors":"Ingrid Blain, Patrick Slama, Michel Giorgi, Thierry Tron, Marius Réglier","doi":"10.1016/S1389-0352(01)00068-X","DOIUrl":"10.1016/S1389-0352(01)00068-X","url":null,"abstract":"<div><p><span>This review reports our recent studies or the mechanism of O-atom transfer to a benzylic C–H bond promoted by Dopamine β-Hydroxylase (DBH) and its biomimetic models. We demonstrate that it is possible to carry out parallel and comparative studies on this enzyme (DBH) and its biomimetic models with the same substrate: 2-aminoindane (</span><strong>3</strong><span>). It was chosen because its two stereogenic centers, both in benzylic positions, make it very powerful for studying the stereochemistry of an O-atom transfer reaction. DBH-catalyzed hydroxylation of </span><strong>3</strong> produced exclusively 14% of <em>trans</em>-(1<em>S</em>,2<em>S</em>)-2-amino-1-indanol (<strong>4</strong>) (93% ee). Studies with stereospecifically deuterium-labeled 2-aminoindanes (1<em>R</em>,2<em>S</em>)-<strong>3b</strong> and (1<em>S</em>,2<em>S</em>)-<strong>3a</strong> showed that the formation of <strong>4</strong> was the result of an overall process with retention of configuration where an O-atom is stereospecifically inserted in the <em>trans</em> <em>pro</em>-<em>S</em> position of the substrate. With copper(I) and (II) complexes of IndPY2 ligands we studied the reaction with dioxygen and observed an O-atom transfer to a benzylic C–H bond which was performed in the same manner as that of DBH. With the deuterium-labeled <em>cis</em>-2-d-IndPY2 ligand, we demonstrated that the reaction occurs by a stereospecific process with retention of configuration. In both cases (enzymatic vs. biomimetic) the O-atom transfers occur in a two-step process involving radical intermediates.</p></div>","PeriodicalId":101090,"journal":{"name":"Reviews in Molecular Biotechnology","volume":"90 2","pages":"Pages 95-112"},"PeriodicalIF":0.0,"publicationDate":"2002-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1389-0352(01)00068-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"56530584","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}
{"title":"Layer-by-layer self-assembly of supramolecular and biomolecular films","authors":"Tim Salditt , Ulrich S Schubert","doi":"10.1016/S1389-0352(01)00049-6","DOIUrl":"10.1016/S1389-0352(01)00049-6","url":null,"abstract":"<div><p><span>In this paper, we give a short account on recent studies of layer-by-layer self-assembly of supramolecular and biomolecular films. Such films are built up from layers of macro-ions with opposing charge. A simple film can be obtained by alternating the adsorption of two components: a flexible, synthetic polycation chains and a supramolecular or biomolecular moiety. We focus on three examples, in which the second component consists either of a supramolecular metal–organic complex (MOC), a nucleic acid, or a biological membrane patch (purple membrane). While the flexible polycation chains (as well as eventual annealing layers) ensure a uniform build-up of the chain, the second macromolecular component may be used to functionalize the films. The combination of layer-by-layer self-assembly and biotechnologically relevant </span>macromolecules may lead to new devices or biomaterial applications. To this end, precise studies of the deposition process and the film structure are needed. Here, we focus on interface sensitive scattering techniques for the structural analysis.</p></div>","PeriodicalId":101090,"journal":{"name":"Reviews in Molecular Biotechnology","volume":"90 1","pages":"Pages 55-70"},"PeriodicalIF":0.0,"publicationDate":"2002-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1389-0352(01)00049-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"56528276","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}
{"title":"Poly(ethylene glycol) block copolymers","authors":"N Tirelli, M.P Lutolf, A Napoli, J.A Hubbell","doi":"10.1016/S1389-0352(01)00057-5","DOIUrl":"10.1016/S1389-0352(01)00057-5","url":null,"abstract":"<div><p>The ubiquitous use of poly(ethylene glycol) in the biomaterials field has also boosted the research activity in the chemical derivatization of this polymer. We focused our interest on the preparation of tailor-made poly(ethylene glycol)-based structures and on the study of structure–activity relationships for its functionalization, as preliminary steps for the preparation of smart functional materials. More specifically, amphiphilic and cationic block copolymers were prepared for prospective use in the preparation of self-assembled carriers, and Michael-type addition of thiols onto acrylates was studied as a model for end-group reaction leading to hydrogel formation.</p></div>","PeriodicalId":101090,"journal":{"name":"Reviews in Molecular Biotechnology","volume":"90 1","pages":"Pages 3-15"},"PeriodicalIF":0.0,"publicationDate":"2002-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1389-0352(01)00057-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"56528385","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}
{"title":"Porous polymers and resins for biotechnological and biomedical applications","authors":"H.-P Hentze, M Antonietti","doi":"10.1016/S1389-0352(01)00046-0","DOIUrl":"10.1016/S1389-0352(01)00046-0","url":null,"abstract":"<div><p>This review describes conventional and modern techniques of porous organic polymer synthesis. A huge variety of polymer architectures and functions can be gained by foaming, phase separation, imprinting or templating approaches. Several applications of porous polymers are discussed, focusing on biotechnological and biomedical applications, such as chromatography, protein synthesis, drug carrier systems, tissue engineering and others.</p></div>","PeriodicalId":101090,"journal":{"name":"Reviews in Molecular Biotechnology","volume":"90 1","pages":"Pages 27-53"},"PeriodicalIF":0.0,"publicationDate":"2002-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1389-0352(01)00046-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"56528250","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}