Virtual special issue “Biomimetic Polymers”
Virtual special issue “Biomimetic Polymers”
复制标题
虚拟特刊“仿生聚合物”
DOI:
10.1016/j.eurpolymj.2019.109370
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发表时间:
2020
影响因子:
6
通讯作者:
Scheibel, Thomas
中科院分区:
文献类型:
--
作者:
Bruns, Nico;Scheibel, Thomas
Without macromolecules, life would not have evolved. The whole cell machinery relies on macromolecular compounds, such as DNA, RNA, proteins, and peptides. Moreover, biopolymers such as polysaccharides or lignin play important roles as structural components of living systems. Natural macromolecules have sophisticated functions and properties that have so far been rarely achieved in synthetic systems. That is why synthetic polymer chemists often look into nature for inspiration how to design functional polymers, or to mimic the function of natural systems with synthetic ones. Moreover, with the advent of biotechnology, the boundaries between natural and synthetic polymers become fluid. For example, the recombinant expression and engineering of genes allows using recombinant proteins in materiaĺs applications. The aim of this special issue of the European Polymer Journal is to highlight examples of research in the field of biomimetic and bioinspired polymer chemistry in order to showcase current trends and to emphasize the opportunities of biomimetic and bioinspired functional materials for novel applications. A classic example for a source of bioinspiration are the proteins of the mussel foot, which adhere strongly to surfaces in wet condition. Messersmith and coworkers review polymers that are inspired by this and other tricks of marine organisms to create adhesives for medical applications [1]. Scheibel and coworkers investigate the question how mussels control the oxidation and reduction of 3, 4-dihydroxyphenylalanine (DOPA) residues in their proteins, which is key to the adhesion properties of the mussel foot proteins [2]. To this end, they recombinantly expressed a mussel protein that can suppress DOPA oxidation. Not only the mussel foot, but also the byssal threads of mussels have fascinating properties. They exhibit high toughness and can self-heal. Harrington and coworkers developed a model polymer network composed of star-shaped PEG with peptides at the chain ends to investigate the role of histidin-rich domains in the self-assembly and self-healing of proteins in the byssal threads [3]. In general, structural proteins are widespread in nature. One class of structural proteins that has been used since ancient times for man-made materials is silk. Nowadays, silk fibroin is intensively investigated as material for biomedical applications because it is biocompatible, biodegradable, and has low immunogenicity. The processing of soluble silk fibroin into insoluble fibers is an essential process both in nature and during the preparation of fibroin-based biomaterials. Linder, Aranko and coworkers investigate the effect of dextran as a crowding agent during silk fibroin coacervation and show that the crowding agent drastically reduces the concentration at which the protein aggregates [4]. Collagen is the most important structural protein in mammals. Collagen-mimetic peptides consist of oligomeric collagen segments and are considered model systems to study the properties and behavior of collagen. The contribution by Börner and coworkers deciphers the effect of pH-dependent switch defects in various locations of the peptide chain on the formation of the collagen triple helix [5]. Polysaccharides, including cellulose, chitin, and starch are abundantly available natural polymers that are increasingly used in materials applications. Especially cellulose nanocrystals (CNCs) and cellulose nanofibrils have attained much interest as nanoscale reinforcing agents for polymeric matrices. Ikkala and Nonappa report nanocomposite fibers that were made by wet-spinning of gel-like mixtures of methylcellulose and CNCs [6]. The fibers showed high ductility …
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影响因子:
6
作者:
Chase B. Thompson;S. Chatterjee;L. Korley
通讯作者:
Chase B. Thompson;S. Chatterjee;L. Korley
影响因子:
6
作者:
Matthias Röber;Sophie Laroque;S. A. López;T. Scheibel;H. Börner
通讯作者:
H. Börner
影响因子:
6
作者:
Jia Wang;Michael H. Suhre;T. Scheibel
通讯作者:
T. Scheibel
影响因子:
6
作者:
Lemetti, Laura;Hirvonen, Sami-Pekka;Aranko, A. Sesilja
通讯作者:
Aranko, A. Sesilja
影响因子:
6
作者:
Trapaidze;D’Antuono;Fratzl;Harrington
通讯作者:
Harrington