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Self-assembling systems comprising intrinsically disordered protein polymers like elastin-like recombinamers
Journal of Peptide Science ( IF 2.1 ) Pub Date : 2021-09-20 , DOI: 10.1002/psc.3362
Diana Juanes-Gusano 1 , Mercedes Santos 1 , Virginia Reboto 1 , Matilde Alonso 1 , José Carlos Rodríguez-Cabello 1
Affiliation  

Despite lacking cooperatively folded structures under native conditions, numerous intrinsically disordered proteins (IDPs) nevertheless have great functional importance. These IDPs are hybrids containing both ordered and intrinsically disordered protein regions (IDPRs), the structure of which is highly flexible in this unfolded state. The conformational flexibility of these disordered systems favors transitions between disordered and ordered states triggered by intrinsic and extrinsic factors, folding into different dynamic molecular assemblies to enable proper protein functions. Indeed, prokaryotic enzymes present less disorder than eukaryotic enzymes, thus showing that this disorder is related to functional and structural complexity. Protein-based polymers that mimic these IDPs include the so-called elastin-like polypeptides (ELPs), which are inspired by the composition of natural elastin. Elastin-like recombinamers (ELRs) are ELPs produced using recombinant techniques and which can therefore be tailored for a specific application. One of the most widely used and studied characteristic structures in this field is the pentapeptide (VPGXG)n. The structural disorder in ELRs probably arises due to the high content of proline and glycine in the ELR backbone, because both these amino acids help to keep the polypeptide structure of elastomers disordered and hydrated. Moreover, the recombinant nature of these systems means that different sequences can be designed, including bioactive domains, to obtain specific structures for each application. Some of these structures, along with their applications as IDPs that self-assemble into functional vesicles or micelles from diblock copolymer ELRs, will be studied in the following sections. The incorporation of additional order- and disorder-promoting peptide/protein domains, such as α-helical coils or β-strands, in the ELR sequence, and their influence on self-assembly, will also be reviewed. In addition, chemically cross-linked systems with controllable order–disorder balance, and their role in biomineralization, will be discussed. Finally, we will review different multivalent IDPs-based coatings and films for different biomedical applications, such as spatially controlled cell adhesion, osseointegration, or biomaterial-associated infection (BAI).

中文翻译:

自组装系统包含本质上无序的蛋白质聚合物,如弹性蛋白样重组体

尽管在天然条件下缺乏协同折叠结构,但许多内在无序蛋白质 (IDP) 仍然具有重要的功能。这些 IDP 是包含有序和固有无序蛋白质区域 (IDPR) 的杂种,其结构在这种未折叠状态下高度灵活。这些无序系统的构象灵活性有利于由内在和外在因素触发的无序和有序状态之间的转变,折叠成不同的动态分子组装体以实现适当的蛋白质功能。事实上,原核酶比真核酶表现出更少的紊乱,因此表明这种紊乱与功能和结构的复杂性有关。模拟这些 IDP 的基于蛋白质的聚合物包括所谓的弹性蛋白样多肽 (ELP),灵感来自天然弹性蛋白的成分。弹性蛋白样重组体 (ELR) 是使用重组技术产生的 ELP,因此可以针对特定应用进行定制。该领域中使用最广泛和研究最广泛的特征结构之一是五肽(VPGXG)n. ELR 中的结构紊乱可能是由于 ELR 主链中脯氨酸和甘氨酸含量高,因为这两种氨基酸都有助于保持弹性体的多肽结构无序和水合。此外,这些系统的重组性质意味着可以设计不同的序列,包括生物活性结构域,以获得每种应用的特定结构。以下部分将研究其中一些结构,以及它们作为 IDPs 的应用,这些 IDPs 从二嵌段共聚物 ELRs 中自组装成功能性囊泡或胶束。还将回顾在 ELR 序列中加入额外的有序和无序促进肽/蛋白质结构域,例如 α-螺旋线圈或 β-链,以及它们对自组装的影响。此外,将讨论具有可控有序-无序平衡的化学交联系统及其在生物矿化中的作用。最后,我们将回顾用于不同生物医学应用的不同多价 IDP 涂层和薄膜,例如空间控制的细胞粘附、骨整合或生物材料相关感染 (BAI)。
更新日期:2021-09-20
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