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Engineering Amino Acid and Peptide Supramolecular Architectures through Fluorination
Chemistry - A European Journal ( IF 4.3 ) Pub Date : 2024-04-18 , DOI: 10.1002/chem.202400617
Eleonora Veronese 1 , Pierangelo Metrangolo 2 , Valentina Dichiarante 1
Affiliation  

Fluorinated non-natural amino acids are attracting considerable research interest, especially in the biomedical field and in materials science, thanks to their ability to self-assemble into peculiar supramolecular structures. The conformational changes induced by the presence of fluorine atoms obviously affect their functions, as well as the biological activity of the deriving peptides and proteins. Here, we will briefly describe the main effects of fluorination on the aggregation behavior of such building blocks, focusing in particular on their improved tendency to form fibrils, and gels therefrom. Our aim is to underline the promising potential of fluorination as a tool to affect the self-assembly features of amino acids, both when used alone and when inserted into polypeptide sequences. The ability of fluorine to influence physical, chemical, and structural properties of these substrates offers the possibility to engineer bioinspired materials with specific and tunable functions.

中文翻译:

通过氟化工程氨基酸和肽超分子结构

氟化非天然氨基酸由于具有自组装成特殊超分子结构的能力而吸引了相当大的研究兴趣,特别是在生物医学领域和材料科学领域。氟原子的存在引起的构象变化明显影响其功能以及衍生肽和蛋白质的生物活性。在这里,我们将简要描述氟化对此类结构单元的聚集行为的主要影响,特别关注它们形成原纤维及其凝胶的改善趋势。我们的目的是强调氟化作为影响氨基酸自组装特征的工具的巨大潜力,无论是单独使用还是插入多肽序列时。氟影响这些基材的物理、化学和结构特性的能力为设计具有特定和可调功能的仿生材料提供了可能性。
更新日期:2024-04-18
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