Sequence-Controlled Polymers by Lutz Jean-François

Sequence-Controlled Polymers by Lutz Jean-François

Author:Lutz, Jean-François
Language: eng
Format: epub
ISBN: 9783527806102
Publisher: John Wiley & Sons, Inc.
Published: 2017-11-22T00:00:00+00:00


Chapter 8

Sequence and Architectural Control in Glycopolymer Synthesis

Yamin Abdouni1, Gokhan Yilmaz1,2,3 and C. Remzi Becer1

1Queen Mary University of London, School of Engineering and Materials Science, Polymer Chemistry Laboratory, 221, Eng, Mile End, London, E1 4NS, UK

2University of Warwick, Department of Chemistry, Coventry, CV4 7AL, UK

3Turkish Military Academy, Department of Basic Sciences, 06650, Ankara, Turkey

8.1 Introduction: Glycopolymer–Lectin Binding

Multivalent protein–carbohydrate interactions play a pivotal role in a wide range of complex biological processes, such as intercellular recognition, signal transduction, and host–pathogen recognition [1–5]. Carbohydrates have great interaction capacity with specific lectins thanks to their monomeric units and their inherent highly branched nature [6–8]. This specific interaction is greatly enhanced by a multivalency effect of densely packed carbohydrate molecules with unique functionalities, which is known as the “glycocluster effect” [9, 10]. The interactions between carbohydrates and lectins are created by hydrogen bonding, Van der Waals' interactions, and hydrophobic stacking at the molecular level [11, 12]. In contrast to other types of proteins, lectins are a critical part of the immune system and display a great diversity in terms of their structure and size [13–15]. Glycopolymers, which are essentially synthetic carbohydrate-containing macromolecules, are able to mimic the structural and functional features of oligosaccharides thanks to variations in anomeric status, linkage positions, branching, and introduction of site-specific substitutions [16–20]. A wide range of oligosaccharides have the capability of covering functionally important areas of lectins, of modulating the interactions with other biomolecules, and of affecting the rate of biological processes, which in turn involves conformational changes due to their very sensitive sugar coding [21, 22]. This special sugar coding system allows them to play crucial biological roles with unusual oligosaccharide sequences, unusual presentations of common terminal sequences, and even modifications of the sugars themselves [23, 24]. Hence, even though so far there has been great progress on the synthesis of well-defined glycopolymers and glyconanoparticles, there is still a demand for more precision control on monomer sequences, compositions, and architectures in order to understand the nature of the carbohydrate–lectin interactions in more detail.

During the last decade, there has been a great deal of interest in the integration of carbohydrates in nanotechnology [25–28]. Advances in glyconanotechnology have allowed for the creation of different bioactive glyconanostructures for various health-related applications such as drug delivery, gene therapy, pathogen detection, and toxin inhibition, as well as the development of lectin-based biosensors [29–32]. Nanoparticles functionalized with carbohydrates present a highly multivalent way for lectin interactions and allow for high local concentrations of ligands on a relatively small surface [33, 34]. Glyconanoparticles as carbohydrate-based systems provide a controlled platform for glycobiological studies because of their ability to mimic the behavior of the naturally existing glycocalyx [34]. Therefore, the design and engineering of highly innovative glyconanoparticles with unique physiochemical properties will help further enhancement of specific recognition properties on multivalent scaffolds in glycoscience.

In the last couple of years, “single-chain technology” has been explored for a deeper understanding of the multivalent functions and the precise folding mechanism of naturally occurring single-chain architectures of macromolecules in biological systems, such as secondary and tertiary structures of proteins and enzymes [35–37].



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