FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W3164045142> ?p ?o ?g. }

• W3164045142 endingPage "2964" @default.
• W3164045142 startingPage "2943" @default.
• W3164045142 abstract "New concepts that develop supramolecular assemblies from intricate biofunctional carbohydrates are yet to come. Currently, the design of most carbohydrate amphiphiles for supramolecular biomaterials is limited to simple (mono- and di-) saccharides as biofunctional units while the cells are surrounded by complex polysaccharides in their native environment. Moreover, assembly strategies and principles used so far are typically similar to the ones applied for peptide amphiphiles and do not consider specific carbohydrate features such as carbohydrate-carbohydrate interactions. Carbohydrates' structural diversity represented by the chiral and topological abundance, as well as multivalency, is also largely unexplored. Exploitation of this diversity is expected to bring breakthroughs in the field of supramolecular biomaterials, potentially resulting in biomaterials that more closely resemble the key features of the extracellular matrix. Carbohydrate-containing biopolymers such as glycoproteins, proteoglycans, and glycolipids are an incredibly diverse and complex set of natural building blocks used by biological systems to endorse a wide range of molecular functions that are critical to life processes. Simplified synthetic analogs of these polymeric glycoconjugates can capture some of these functions and are increasingly exploited toward the development of supramolecular biomaterials. These carbohydrate amphiphiles can mimic structural aspects through cooperative molecular self-assembly or target distinct signaling pathways through engineered (multivalent) interactions with biological systems. Herein, we discuss the supramolecular principles that regulate the glycome function(s) and the translation of these in the design of supramolecular biomaterials in which carbohydrates are used as information-rich structural elements with huge potential as therapeutic supramolecular biomaterials. Carbohydrate-containing biopolymers such as glycoproteins, proteoglycans, and glycolipids are an incredibly diverse and complex set of natural building blocks used by biological systems to endorse a wide range of molecular functions that are critical to life processes. Simplified synthetic analogs of these polymeric glycoconjugates can capture some of these functions and are increasingly exploited toward the development of supramolecular biomaterials. These carbohydrate amphiphiles can mimic structural aspects through cooperative molecular self-assembly or target distinct signaling pathways through engineered (multivalent) interactions with biological systems. Herein, we discuss the supramolecular principles that regulate the glycome function(s) and the translation of these in the design of supramolecular biomaterials in which carbohydrates are used as information-rich structural elements with huge potential as therapeutic supramolecular biomaterials. IntroductionCarbohydrates are involved in numerous essential processes within the life cycle of cells and organisms—they are a source of energy and important metabolites; they sustain the swelling pressure and mechanical properties of different tissues; and are also responsible for activating cascades of cellular events, ranging from adhesion to differentiation and apoptosis. Their functions are exerted mainly through combinatorial presentation of multiple non-covalent interactions. Because of their structural diversity (Figure 1), carbohydrates can display a vast number of ligand structures with induced fit and cooperativity that render their multivalent interactions specific and selective. The incorporation of carbohydrates in biomedical systems increases the level of molecular complexity, thus giving rise to an exclusive class of bioinformation coding materials that are not accessible using more conventional materials based on peptides, proteins, and other polymers.1Gim S. Zhu Y.T. Seeberger P.H. Delbianco M. Carbohydrate-based nanomaterials for biomedical applications.Wiley Interdiscip. Rev. Nanomed. Nanobiotechnol. 2019; 11: e1558Crossref PubMed Scopus (13) Google Scholar,2Delbianco M. Bharate P. Varela-Aramburu S. Seeberger P.H. Carbohydrates in supramolecular chemistry.Chem. Rev. 2016; 116: 1693-1752Crossref PubMed Scopus (134) Google ScholarTo capitalize on multivalency and the structural richness of carbohydrates, supramolecular approaches are better suited than covalent synthesis for several reasons: they introduce a dynamic aspect to the system, offering the possibility of more complex communication with its environment through reversible formation, responsiveness, and adaptability; they can generate larger functional and organized structures that would extend the multivalent interactions over longer distances; and their morphology can be tuned to match the targeted biointerface.3Dong R.J. Zhou Y.F. Huang X.H. Zhu X.Y. Lu Y.F. Shen J. Functional supramolecular polymers for biomedical applications.Adv. Mater. 2015; 27: 498-526Crossref PubMed Scopus (303) Google Scholar,4Aida T. Meijer E.W. Stupp S.I. Functional supramolecular polymers.Science. 2012; 335: 813-817Crossref PubMed Scopus (2282) Google Scholar However, intermolecular carbohydrate-carbohydrate interactions (CCIs) in simple sugars are not strong enough to generate structured supramolecular scaffolds amenable to biomedical applications. Thus, diverse approaches have been used to display carbohydrates onto functional biomaterials. In this review, we will discuss different types of carbohydrate amphiphiles and strategies employed in their self-assembly, which can generate a plethora of biomaterials with multivalent presentation of carbohydrates that can be tuned in terms of morphology, function, and bioactivity. Finally, we will highlight some of the recent biological applications of supramolecular carbohydrate systems.The role of multivalency in carbohydrate biorecognitionNon-covalent interactions can be up to 100 times weaker than covalent bonds. To compensate for the weakness of these interactions while preserving their reversibility, nature has adopted the concept of multivalency—the ability of a substrate to form multiple individual bonds with a ligand to enhance binding affinity and ensure selectivity and specificity of recognition.5Fasting C. Schalley C.A. Weber M. Seitz O. Hecht S. Koksch B. Dernedde J. Graf C. Knapp E.W. Haag R. Multivalency as a chemical organization and action principle.Angew. Chem. Int. Ed. Engl. 2012; 51: 10472-10498Crossref PubMed Scopus (670) Google Scholar Simultaneously occurring multiple binding events increase the binding contact surface resulting in an interaction that is much stronger and more selective than the individual bonds.Molecular basis of carbohydrate-binding interactionsCarbohydrates interact with their environment through well-defined signatures determined by their sequence and preferred (induced) three-dimensional conformations. Decades of crystallographic and NMR studies have identified the molecular interactions that govern carbohydrate binding and recognition in biological systems.6Solís D. Bovin N.V. Davis A.P. Jiménez-Barbero J. Romero A. Roy R. Smetana K. Gabius H.J. A guide into glycosciences: how chemistry, biochemistry and biology cooperate to crack the sugar code.Biochim. Biophys. Acta. 2015; 1850: 186-235Crossref PubMed Scopus (0) Google Scholar Each carbohydrate, ranging from simple monosaccharide to proteoglycans, has a unique imprint that can be recognized by other biomolecules.7McMahon C.M. Isabella C.R. Windsor I.W. Kosma P. Raines R.T. Kiessling L.L. Stereoelectronic effects impact glycan recognition.J. Am. Chem. Soc. 2020; 142: 2386-2395Crossref PubMed Scopus (11) Google Scholar The position and arrangement of the functional groups determine the formation of hydrophilic and hydrophobic regions through which polar and non-polar interactions can take place, respectively. Despite the structural diversity of the carbohydrate interactome, the nature of interactions at the molecular level are a conserved set: hydrogen bonding is the main driving force, whereas hydrophobic interactions and metal bridges balance and stabilize the complexes (Figure 2).Figure 2Schematic presentation of non-covalent interactions in which carbohydrates can be engagedShow full caption(A) Hydrogen bonding can be either (A1) cooperative or (A2) bidentate.(B) Complexation with cations, in which (B1) proteins’ amino acids, (B2) carbohydrates, and/or (B1) water can also occupy coordination sites.(C) Hydrophobic CH-π stacking that results from the London dispersion forces and stereoelectronic effects (electron-defficient CH bonds are formed via hyperconjugations, as shown in C2).View Large Image Figure ViewerDownload Hi-res image Download (PPT)Hydrogen bondingTwo types of hydrogen bonding have been identified in carbohydrate interactions: (1) cooperative hydrogen bonds in which the carbohydrate’s hydroxyl groups act as both acceptor via the oxygen and donor through the hydrogen (red arrows in Figure 2A1) and (2) bidentate hydrogen bonds (Figure 2A2) in which two adjacent hydroxyl groups of the carbohydrate bind to two different atoms of a planar polar amino-acid side chain (typically aspartate, glutamate, asparagine, glutamine, or arginine).8López de la Paz M.L. Ellis G. Pérez M. Perkins J. Jiménez-Barbero J. Vicent C. Carbohydrate hydrogen-bonding cooperativity − intramolecular hydrogen bonds and their cooperative effect on intermolecular processes − binding to a hydrogen-bond acceptor molecule.Eur. J. Org. Chem. 2002; 2002: 840-855Crossref Scopus (56) Google Scholar,9Gaiser O.J. Piotukh K. Ponnuswamy M.N. Planas A. Borriss R. Heinemann U. Structural basis for the substrate specificity of a Bacillus 1,3–1,4-beta-glucanase.J. Mol. Biol. 2006; 357: 1211-1225Crossref PubMed Scopus (0) Google Scholar Cooperative hydrogen bonding occurs intramolecularly and/or in CCI, while bidentate hydrogen bonds are mainly involved in carbohydrate-protein interactions (CPIs) in which amide groups of asparagine act as donors and the acidic side chains of aspartate and glutamate as acceptors, thus providing a specific arrangement, selective for adjacent equatorial/equatorial or equatorial/axial hydroxyl groups. (In the biological milieu, water plays an important role in hydrogen bonds networks: the loss of bound water in protein binding pockets at the expense of carbohydrates comes with an entropic cost. For more details on this issue, the reader is referred to Lemieux’s work on the role of water in carbohydrate biorecognition.)10Lemieux R.U. How water provides the impetus for molecular recognition in aqueous solution.Acc. Chem. Res. 1996; 29: 373-380Crossref Google ScholarInteractions with cationsThe X-ray crystal structures of some lectins reveal the presence of divalent cations near the carbohydrate-binding site. The metal ions either fix the positions of certain amino acids that interact with the carbohydrate or form bridges between the carbohydrate ligand and the binding pocket (Figure 2B1). Among different metals, calcium ions (Ca2+) are the most common coordination centers with the carbohydrates’ hydroxyl groups or the ring oxygen as ligands, and the other coordination sites can be occupied either by amino-acid residues or water molecules (Figure 2B1).11Drickamer K. Ca2+-dependent sugar recognition by animal lectins.Biochem. Soc. Trans. 1996; 24: 146-150Crossref PubMed Scopus (0) Google Scholar In CCIs, the coordination sites are occupied by hydroxyl groups or water molecules (Figure 2B2). In complex carbohydrates (e.g., glycoconjugates, glycosaminoglycans), such coordination can result in formation of bridges between different carbohydrate chains—an indispensable feature in cell-cell adhesion, which increases the adhesion force. Cations can also compensate the negative charge of carbohydrates that contain acidic groups. Thus, the concentration of the cations plays a crucial role not only in balancing the adhesive forces versus the charge repulsion but also in modulating the cell surface charge.Hydrophobic interactionsDespite being highly polar and solvated molecules, carbohydrates can engage in hydrophobic interactions through non-polar regions that are created by the localization of several axial protons on the same face of the carbohydrate ring. Hydrogen bonds provide a structural framework that enables molecules approaching to close proximities where van der Waals forces contribute to the stability of carbohydrate-protein complexes. The additional contribution of CH-π interactions was demonstrated experimentally and theoretically relatively recently.12del Carmen Fernández-Alonso M.D. Cañada F.J. Jiménez-Barbero J. Cuevas G. Molecular recognition of saccharides by proteins. Insights on the origin of the carbohydrate-aromatic interactions.J. Am. Chem. Soc. 2005; 127: 7379-7386Crossref PubMed Scopus (0) Google Scholar, 13Hudson K.L. Bartlett G.J. Diehl R.C. Agirre J. Gallagher T. Kiessling L.L. Woolfson D.N. Carbohydrate-aromatic interactions in proteins.J. Am. Chem. Soc. 2015; 137: 15152-15160Crossref PubMed Scopus (180) Google Scholar, 14Ramírez-Gualito K. Alonso-Ríos R. Quiroz-García B. Rojas-Aguilar A. Díaz D. Jiménez-Barbero J. Cuevas G. Enthalpic nature of the CH/pi interaction involved in the recognition of carbohydrates by aromatic compounds, confirmed by a novel interplay of NMR, calorimetry, and theoretical calculations.J. Am. Chem. Soc. 2009; 131: 18129-18138Crossref PubMed Scopus (0) Google Scholar These studies showed that aromatic amino-acid residues can interact with different faces of the carbohydrate ring giving rise to a parallel stacking geometry (Figure 2C1). While London dispersion forces are the main attractive forces of CH-π interactions, the weaker electrostatic interaction between the electron-rich aromatic ring and electron-deficient C–H bonds of the carbohydrate (Figure 2C2) controls the directionality of the bond. A comparison between different aromatic amino acids shows that all four of them, namely, tryptophan, tyrosine, phenylalanine, and histidine, engage in CH-π interactions with carbohydrates but there is a strong preference for tryptophan followed by tyrosine, phenylalanine, and histidine.13Hudson K.L. Bartlett G.J. Diehl R.C. Agirre J. Gallagher T. Kiessling L.L. Woolfson D.N. Carbohydrate-aromatic interactions in proteins.J. Am. Chem. Soc. 2015; 137: 15152-15160Crossref PubMed Scopus (180) Google Scholar This order reflects the electrostatic surface potential and electron-richness of their respective π-systems.Multivalent carbohydrate-binding modesA key feature of carbohydrate interactions is the combinatorial impact of the above interactions that must be multiplied and organized in a cooperative fashion to enhance and modulate the strength of binding and render it biologically functional (Figure 3). Of note, multiple simultaneous interactions have unique collective properties that are different than the simple arithmetic sum of the respective monovalent interactions. Multivalent ligands usually bind to their receptors in a sequential manner so that the entropic cost is paid in the initial binding. The entropic barrier of subsequent interactions is therefore lower, resulting in favorable binding.5Fasting C. Schalley C.A. Weber M. Seitz O. Hecht S. Koksch B. Dernedde J. Graf C. Knapp E.W. Haag R. Multivalency as a chemical organization and action principle.Angew. Chem. Int. Ed. Engl. 2012; 51: 10472-10498Crossref PubMed Scopus (670) Google ScholarFigure 3Examples of multivalencyShow full caption(A and B) (A) Carbohydrate-carbohydrate interactions that take place during (A1) cell-to-cell interactions or (A2) alginate chains in the presence of metal ions (gray) and (B) protein-carbohydrate interactions between: (B1) glycan-binding proteins and glycosaminoglycans; (B2) lectins and glycoconjugates with multivalent carbohydrates presentation can promote lectin clustering; and (B3) multiple lectins and multivalent carbohydrate forming cross-linked nets. Cells are presented in blue, receptors in light green, and the metal ions in dark gray.View Large Image Figure ViewerDownload Hi-res image Download (PPT)Multivalent CCIsIn biological systems, CCIs draw attention owing to their involvement in cell-cell adhesion and recognition processes.15Bucior I. Scheuring S. Engel A. Burger M.M. Carbohydrate-carbohydrate interaction provides adhesion force and specificity for cellular recognition.J. Cell Biol. 2004; 165: 529-537Crossref PubMed Scopus (97) Google Scholar,16Hakomori S. Carbohydrate-to-carbohydrate interaction, through glycosynapse, as a basis of cell recognition and membrane organization.Glycoconj. J. 2004; 21: 125-137Crossref PubMed Scopus (124) Google Scholar The weak CCI are advantageous during the first step of cell surface screening and together with their induced fit, as compared with protein-protein interactions (e.g., integrins, cadherins), allow fine-tuning for primary connections between the cells’ glycocalyx through the formation of low-affinity and reversible bonds (Figure 3A1).16Hakomori S. Carbohydrate-to-carbohydrate interaction, through glycosynapse, as a basis of cell recognition and membrane organization.Glycoconj. J. 2004; 21: 125-137Crossref PubMed Scopus (124) Google Scholar,17Lai C.H. Hütter J. Hsu C.W. Tanaka H. Varela-Aramburu S. De Cola L. Lepenies B. Seeberger P.H. Analysis of carbohydrate-carbohydrate interactions using sugar-functionalized silicon nanoparticles for cell imaging.Nano Lett. 2016; 16: 807-811Crossref PubMed Google Scholar These are then reinforced, if the fit is right, through multiple, simultaneous, and specific interactions, before less reversible processes can take place to form dynamic but stable complexes. In most biological systems, bivalent ions, particularly Ca2+, promote CCIs by locking the carbohydrate chains in their complementary arrangement to provide an optimal fit between cells and/or by crosslinking the carbohydrate chains from interacting cells. Such cross-links might only be involved as a driving force in the initial cell-to-cell approach or provide additional adhesion forces per binding site, leading to the formation of the so-called carbohydrate zippers (Figure 3A2). The zippers are usually formed by the systematic repetition of membrane proteoglycans at the cell surface and their adhesion strengths are within the piconewton range. While this binding mechanism is considered to be general for CCI, other binding modes may also occur, illustrating the tremendous value of multivalency in creating specificity and modulating binding forces.Multivalent CPIsMost of the specific biological roles of carbohydrates are mediated by CPIs. If we exclude the glycan-specific antibodies, the proteins that interact with carbohydrates can be categorized into two major groups: lectins and glycosaminoglycan-binding proteins (GBPs). Their monovalent interactions, i.e., protein binding to a monosaccharide at a single site, are generally weak (Kd in the micromolar range) but the binding affinities can be enhanced dramatically by adopting protein conformations that facilitate multivalent binding. The spatial arrangement of the binding sites can modulate the affinity of the interaction and thus allows selectivity. The carbohydrate density is also important because of the avidity (collective affinity) effect, but too high density can cause steric hindrance and compromise the selectivity.Various binding modes exist and depend on the protein structure, the nature and complexity of carbohydrate, the environment, and the particular function (Figure 3B). GBPs interact with sulfated glycosaminoglycans via clusters of positively charged amino acids, e.g., Cardin-Weintraub sequences (Figure 3B1). On the other hand, lectins recognize specific carbohydrate termini and bind them into structurally defined pockets (Figures 3B2 and 3B3). Multivalent carbohydrates can either bind to subsites of single or multiple lectins. In the case of single lectins, the subsites are generally clustered to face the carbohydrate, facilitating face-to-face binding through multiple identical interactions. The clustering of receptor subsites increases the valency on the protein side, thereby strengthening the interaction. This phenomenon is known as the “cluster glycoside effect” and the overall interaction can be stronger than the sum of the individual interactions in some cases. Lectins that are involved in signal transduction processes use different binding modes with cross-linked nets between multiple lectins and one or more multivalent glycoconjugates (Figure 3B3). These cross-links create networks of non-covalent interactions that can be either linear, two dimensional, or three dimensional. One-dimensional cross-links result from interactions between bivalent carbohydrates and bivalent lectins, where each carbohydrate site is bound to a different lectin. More complex two- and three-dimensional networks are formed with carbohydrate ligands and proteins with higher valencies, often causing aggregation and precipitation.Design of carbohydrate self-assembling blocksThe interactions of carbohydrates showcase how cooperative supramolecular multivalent interactions can (1) build specificity through spatial complementarity and (2) increase binding affinity through the multiplication of interaction sites. A fundamental understanding of these molecular features provides opportunities for exploiting multivalency, which illustrates the potential of designed carbohydrate systems for biomedical applications.General principles in the design of self-assembling building blocksSelf-assembly is a bottom-up approach that uses non-covalent (reversible) interactions to generate dynamic multivalent systems.18Lehn J.M. Toward self-organization and complex matter.Science. 2002; 295: 2400-2403Crossref PubMed Scopus (1974) Google Scholar,19Whitesides G.M. Grzybowski B. Self-assembly at all scales.Science. 2002; 295: 2418-2421Crossref PubMed Scopus (5464) Google Scholar It is ubiquitously used by nature to create complex structures whose biofunctionality is tailored by the generated (nanoscale) morphology and the incorporation and presentation of bioactive moieties. In biological self-assembled systems, carbohydrates are often conjugated to lipids, proteins, or aromatic nitrogenous bases (Figures 4A–4C ). Such conjugation imparts the hydrophilic carbohydrates with amphiphilic properties and thus enhances their self-assembling propensity. The diversity of the generated morphologies is striking (Figure 4D) and suggests that synthetic amphiphilic carbohydrate building blocks can be tuned to drive a structure-targeted assembly. Indeed, assembly of diverse synthetic analogs of natural glycoconjugates has shown that the size and structure of the linker20Yan N. He G. Zhang H.L. Ding L.P. Fang Y. Glucose-based fluorescent low-molecular mass compounds: creation of simple and versatile supramolecular gelators.Langmuir. 2010; 26: 5909-5917Crossref PubMed Scopus (95) Google Scholar, 21Clemente M.J. Fitremann J. Mauzac M. Serrano J.L. Oriol L. Synthesis and characterization of maltose-based amphiphiles as supramolecular hydrogelators.Langmuir. 2011; 27: 15236-15247Crossref PubMed Scopus (51) Google Scholar, 22Mathiselvam M. Loganathan D. Varghese B. Synthesis and characterization of thiourea- and urea-linked glycolipids as low-molecular-weight hydrogelators.RSC Adv. 2013; 3: 14528-14542Crossref Scopus (14) Google Scholar, 23Goyal N. Cheuk S. Wang G.J. Synthesis and characterization of D-glucosamine-derived low molecular weight gelators.Tetrahedron. 2010; 66: 5962-5971Crossref Scopus (45) Google Scholar and the hydrophobic portion22Mathiselvam M. Loganathan D. Varghese B. Synthesis and characterization of thiourea- and urea-linked glycolipids as low-molecular-weight hydrogelators.RSC Adv. 2013; 3: 14528-14542Crossref Scopus (14) Google Scholar, 23Goyal N. Cheuk S. Wang G.J. Synthesis and characterization of D-glucosamine-derived low molecular weight gelators.Tetrahedron. 2010; 66: 5962-5971Crossref Scopus (45) Google Scholar, 24Huang Y.W. Wang J.C. Wei Z.X. Modulating supramolecular helicity and electrical conductivity of perylene dyes through an achiral alkyl chain.Chem. Commun. (Camb). 2014; 50: 8343-8345Crossref PubMed Scopus (32) Google Scholar, 25Jung J.H. Rim J.A. Han W.S. Lee S.J. Lee Y.J. Cho E.J. Kim J.S. Ji Q.M. Shimizu T. Hydrogel behavior of a sugar-based gelator by introduction of an unsaturated moiety as a hydrophobic group.Org. Biomol. Chem. 2006; 4: 2033-2038Crossref PubMed Scopus (43) Google Scholar, 26Ono F. Watanabe H. Shinkai S. Structural optimization of super-gelators derived from naturally-occurring mannose and their morphological diversity.RSC Adv. 2014; 4: 25940-25947Crossref Google Scholar affect the assembly, morphology, and properties of the generated supramolecular systems. The main driving force of the assembly process depends on the structure of the hydrophobic component: CH-π interactions and aromatic stacking prompt the assembly of aromatic amphiphiles,24Huang Y.W. Wang J.C. Wei Z.X. Modulating supramolecular helicity and electrical conductivity of perylene dyes through an achiral alkyl chain.Chem. Commun. (Camb). 2014; 50: 8343-8345Crossref PubMed Scopus (32) Google Scholar,27Brito A. Abul-Haija Y.M. da Costa D.S. Novoa-Carballal R. Reis R.L. Ulijn R.V. Pires R.A. Pashkuleva I. Minimalistic supramolecular proteoglycan mimics by co-assembly of aromatic peptide and carbohydrate amphiphiles.Chem. Sci. 2019; 10: 2385-2390Crossref PubMed Scopus (15) Google Scholar,28Birchall L.S. Roy S. Jayawarna V. Hughes M. Irvine E. Okorogheye G.T. Saudi N. De Santis E. Tuttle T. Edwards A.A. Ulijn R.V. Exploiting CH-pi interactions in supramolecular hydrogels of aromatic carbohydrate amphiphiles.Chem. Sci. 2011; 2: 1349-1355Crossref Scopus (59) Google Scholar hydrogen bonding patterns (including β-stacking) usually underpins the assembly of glycopeptides,29Lee S.S. Fyrner T. Chen F. Álvarez Z. Sleep E. Chun D.S. Weiner J.A. Cook R.W. Freshman R.D. Schallmo M.S. et al.Sulfated glycopeptide nanostructures for multipotent protein activation.Nat. Nanotechnol. 2017; 12: 821-829Crossref PubMed Scopus (103) Google Scholar,30Restuccia A. Tian Y.F. Collier J.H. Hudalla G.A. Self-assembled glycopeptide nanofibers as modulators of galectin-1 bioactivity.Cell. Mol. Bioeng. 2015; 8: 471-487Crossref PubMed Scopus (38) Google Scholar and hydrophobic interactions are critical to the assembly of glycolipids.26Ono F. Watanabe H. Shinkai S. Structural optimization of super-gelators derived from naturally-occurring mannose and their morphological diversity.RSC Adv. 2014; 4: 25940-25947Crossref Google Scholar Some linkers might enhance the aggregates’ stability by participating in supramolecular interactions as well.22Mathiselvam M. Loganathan D. Varghese B. Synthesis and characterization of thiourea- and urea-linked glycolipids as low-molecular-weight hydrogelators.RSC Adv. 2013; 3: 14528-14542Crossref Scopus (14) Google Scholar,24Huang Y.W. Wang J.C. Wei Z.X. Modulating supramolecular helicity and electrical conductivity of perylene dyes through an achiral alkyl chain.Chem. Commun. (Camb). 2014; 50: 8343-8345Crossref PubMed Scopus (32) Google Scholar Finally, the carbohydrate component can also influence the assembly process usually by enhancing the solubility of the amphiphile in water and/or by influencing the morphology and hierarchical order of the self-assembled structures.31Roytman R. Adler-Abramovich L. Kumar K.S.A. Kuan T.C. Lin C.C. Gazit E. Brik A. Exploring the self-assembly of glycopeptides using a diphenylalanine scaffold.Org. Biomol. Chem. 2011; 9: 5755-5761Crossref PubMed Scopus (23) Google Scholar, 32Tsuzuki T. Kabumoto M. Arakawa H. Ikeda M. The effect of carbohydrate structures on the hydrogelation ability and morphology of self-assembled structures of peptide-carbohydrate conjugates in water.Org. Biomol. Chem. 2017; 15: 4595-4600Crossref PubMed Google Scholar, 33Restuccia A. Seroski D.T. Kelley K.L. O'Bryan C.S. Kurian J.J. Knox K.R. Farhadi S.A. Angelini T.E. Hudalla G.A. Hierarchical self-assembly and emergent function of densely glycosylated peptide nanofibers.Commun. Chem. 2019; 2: 53Crossref Scopus (8) Google Scholar Additional functionalization of the carbohydrate with polar and charged groups, such as sulfates and phosphates, can be required for some amphiphiles to enhance their solubility.27Brito A. Abul-Haija Y.M. da Costa D.S. Novoa-Carballal R. Reis R.L. Ulijn R.V. Pires R.A. Pashkuleva I. Minimalistic supramolecular proteoglycan mimics by co-assembly of aromatic peptide and carbohydrate amphiphiles.Chem. Sci. 2019; 10: 2385-2390Crossref PubMed Scopus (15) Google Scholar Such functionalization can also introduce/change the repulsive Coulombic forces and thus affect the assembly.27Brito A. Abul-Haija Y.M. da Costa D.S. Novoa-Carballal R. Reis R.L. Ulijn R.V. Pires R.A. Pashkuleva I. Minimalistic supramolecular proteoglycan mimics by co-assembly of aromatic peptide and carbohydrate amphiphiles.Chem. Sci. 2019; 10: 2385-2390Crossref PubMed Scopus (15) Google Scholar,34Carvalho A.M. Teixeira R. Novoa-Carballal R. Pires R.A. Reis R.L. Pashkuleva I. Redox-responsive micellar nanoparticles from glycosaminoglycans for CD44 targeted drug delivery.Biomacromolecules. 2018; 19: 2991-2999Crossref PubMed Scopus (15) Google Scholar In supramolecular biomaterials, however, the carbohydrate is primarily designed in function of a targeted biorecognition.29Lee S.S. Fyrner T. Chen F. Álvarez Z. Sleep E. Chun D.S. Weiner J.A. Cook R.W. Freshman R.D. Schallmo M.S. et al.S" @default.
• W3164045142 created "2021-06-07" @default.
• W3164045142 creator A5019096622 @default.
• W3164045142 creator A5026317542 @default.
• W3164045142 creator A5061230022 @default.
• W3164045142 creator A5070933663 @default.
• W3164045142 creator A5080219954 @default.
• W3164045142 creator A5081499203 @default.
• W3164045142 date "2021-11-01" @default.
• W3164045142 modified "2023-10-18" @default.
• W3164045142 title "Carbohydrate amphiphiles for supramolecular biomaterials: Design, self-assembly, and applications" @default.
• W3164045142 cites W1433445337 @default.
• W3164045142 cites W1545971277 @default.
• W3164045142 cites W1965243534 @default.
• W3164045142 cites W1967892211 @default.
• W3164045142 cites W1974738601 @default.
• W3164045142 cites W1976242944 @default.
• W3164045142 cites W1977235269 @default.
• W3164045142 cites W1978090683 @default.
• W3164045142 cites W1982304014 @default.
• W3164045142 cites W1982775823 @default.
• W3164045142 cites W1984882363 @default.
• W3164045142 cites W1985471166 @default.
• W3164045142 cites W1987448788 @default.
• W3164045142 cites W1991248930 @default.
• W3164045142 cites W1991281527 @default.
• W3164045142 cites W1991660232 @default.
• W3164045142 cites W1991799520 @default.
• W3164045142 cites W1994486848 @default.
• W3164045142 cites W1994726645 @default.
• W3164045142 cites W1994980982 @default.
• W3164045142 cites W1998608797 @default.
• W3164045142 cites W1999331381 @default.
• W3164045142 cites W2003312569 @default.
• W3164045142 cites W2012300039 @default.
• W3164045142 cites W2012619409 @default.
• W3164045142 cites W2013883394 @default.
• W3164045142 cites W2015492344 @default.
• W3164045142 cites W2017114349 @default.
• W3164045142 cites W2018834778 @default.
• W3164045142 cites W2024022415 @default.
• W3164045142 cites W2024385066 @default.
• W3164045142 cites W2026841503 @default.
• W3164045142 cites W2031372108 @default.
• W3164045142 cites W2031956256 @default.
• W3164045142 cites W2033083169 @default.
• W3164045142 cites W2044800984 @default.
• W3164045142 cites W2048582601 @default.
• W3164045142 cites W2051338296 @default.
• W3164045142 cites W2054587080 @default.
• W3164045142 cites W2054752014 @default.
• W3164045142 cites W2057539529 @default.
• W3164045142 cites W2064974400 @default.
• W3164045142 cites W2067823628 @default.
• W3164045142 cites W2069507241 @default.
• W3164045142 cites W2070428966 @default.
• W3164045142 cites W2073571484 @default.
• W3164045142 cites W2076647491 @default.
• W3164045142 cites W2085737445 @default.
• W3164045142 cites W2090595154 @default.
• W3164045142 cites W2094121768 @default.
• W3164045142 cites W2095517367 @default.
• W3164045142 cites W2096202597 @default.
• W3164045142 cites W2096667986 @default.
• W3164045142 cites W2096804208 @default.
• W3164045142 cites W2099416001 @default.
• W3164045142 cites W2103742020 @default.
• W3164045142 cites W2109168526 @default.
• W3164045142 cites W2121011186 @default.
• W3164045142 cites W2121071685 @default.
• W3164045142 cites W2131382809 @default.
• W3164045142 cites W2131605097 @default.
• W3164045142 cites W2138159091 @default.
• W3164045142 cites W2148583242 @default.
• W3164045142 cites W2154115123 @default.
• W3164045142 cites W2160602446 @default.
• W3164045142 cites W2160752868 @default.
• W3164045142 cites W2163352384 @default.
• W3164045142 cites W2164505756 @default.
• W3164045142 cites W2204953460 @default.
• W3164045142 cites W2208241823 @default.
• W3164045142 cites W2217782303 @default.
• W3164045142 cites W2234597993 @default.
• W3164045142 cites W2283939652 @default.
• W3164045142 cites W2313148645 @default.
• W3164045142 cites W2315564955 @default.
• W3164045142 cites W2319855705 @default.
• W3164045142 cites W2320216103 @default.
• W3164045142 cites W2402088633 @default.
• W3164045142 cites W2434410156 @default.
• W3164045142 cites W2517201556 @default.
• W3164045142 cites W2568465711 @default.
• W3164045142 cites W2604255532 @default.
• W3164045142 cites W2610412742 @default.
• W3164045142 cites W2625065858 @default.
• W3164045142 cites W2751992247 @default.
• W3164045142 cites W2754876553 @default.
• W3164045142 cites W2793186572 @default.

• next