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Rational design of amphiphilic fluorinated peptides: evaluation of self-assembly properties and hydrogel formation
Nanoscale ( IF 5.8 ) Pub Date : 2022-06-22 , DOI: 10.1039/d2nr01648f Suvrat Chowdhary 1 , Robert Franz Schmidt 2 , Anil Kumar Sahoo 3, 4 , Tiemo Tom Dieck 1 , Thomas Hohmann 1 , Boris Schade 5 , Kerstin Brademann-Jock 6 , Andreas F Thünemann 6 , Roland R Netz 3 , Michael Gradzielski 2 , Beate Koksch 1
Nanoscale ( IF 5.8 ) Pub Date : 2022-06-22 , DOI: 10.1039/d2nr01648f Suvrat Chowdhary 1 , Robert Franz Schmidt 2 , Anil Kumar Sahoo 3, 4 , Tiemo Tom Dieck 1 , Thomas Hohmann 1 , Boris Schade 5 , Kerstin Brademann-Jock 6 , Andreas F Thünemann 6 , Roland R Netz 3 , Michael Gradzielski 2 , Beate Koksch 1
Affiliation
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Advanced peptide-based nanomaterials composed of self-assembling peptides (SAPs) are of emerging interest in pharmaceutical and biomedical applications. The introduction of fluorine into peptides, in fact, offers unique opportunities to tune their biophysical properties and intermolecular interactions. In particular, the degree of fluorination plays a crucial role in peptide engineering as it can be used to control the characteristics of fluorine-specific interactions and, thus, peptide conformation and self-assembly. Here, we designed and explored a series of amphipathic peptides by incorporating the fluorinated amino acids (2S)-4-monofluoroethylglycine (MfeGly), (2S)-4,4-difluoroethylglycine (DfeGly) and (2S)-4,4,4-trifluoroethylglycine (TfeGly) as hydrophobic components. This approach enabled studying the impact of fluorination on secondary structure formation and peptide self-assembly on a systematic basis. We show that the interplay between polarity and hydrophobicity, both induced differentially by varying degrees of side chain fluorination, does affect peptide folding significantly. A greater degree of fluorination promotes peptide fibrillation and subsequent formation of physical hydrogels in physiological conditions. Molecular simulations revealed the key role played by electrostatically driven intra-chain and inter-chain contact pairs that are modulated by side chain fluorination and give insights into the different self-organization behaviour of selected peptides. Our study provides a systematic report about the distinct features of fluorinated oligomeric peptides with potential applications as peptide-based biomaterials.
中文翻译：
两亲性氟化肽的合理设计：自组装特性和水凝胶形成的评价
由自组装肽 (SAP) 组成的先进的基于肽的纳米材料在制药和生物医学应用中引起了人们的兴趣。事实上，将氟引入肽中，为调整其生物物理特性和分子间相互作用提供了独特的机会。特别是，氟化程度在肽工程中起着至关重要的作用，因为它可用于控制氟特异性相互作用的特征，从而控制肽构象和自组装。在这里，我们通过结合氟化氨基酸 (2 S )-4-单氟乙基甘氨酸 ( MfeGly )、(2 S )-4,4-二氟乙基甘氨酸 ( DfeGly ) 和 (2 S)-4,4,4-三氟乙基甘氨酸 ( TfeGly) 作为疏水成分。这种方法能够系统地研究氟化对二级结构形成和肽自组装的影响。我们表明极性和疏水性之间的相互作用，两者都由不同程度的侧链氟化引起，确实显着影响肽折叠。更大程度的氟化促进肽原纤维化和随后在生理条件下形成物理水凝胶。分子模拟揭示了由侧链氟化调节的静电驱动的链内和链间接触对所起的关键作用，并深入了解所选肽的不同自组织行为。
更新日期：2022-06-22
中文翻译：
两亲性氟化肽的合理设计：自组装特性和水凝胶形成的评价
由自组装肽 (SAP) 组成的先进的基于肽的纳米材料在制药和生物医学应用中引起了人们的兴趣。事实上，将氟引入肽中，为调整其生物物理特性和分子间相互作用提供了独特的机会。特别是，氟化程度在肽工程中起着至关重要的作用，因为它可用于控制氟特异性相互作用的特征，从而控制肽构象和自组装。在这里，我们通过结合氟化氨基酸 (2 S )-4-单氟乙基甘氨酸 ( MfeGly )、(2 S )-4,4-二氟乙基甘氨酸 ( DfeGly ) 和 (2 S)-4,4,4-三氟乙基甘氨酸 ( TfeGly) 作为疏水成分。这种方法能够系统地研究氟化对二级结构形成和肽自组装的影响。我们表明极性和疏水性之间的相互作用，两者都由不同程度的侧链氟化引起，确实显着影响肽折叠。更大程度的氟化促进肽原纤维化和随后在生理条件下形成物理水凝胶。分子模拟揭示了由侧链氟化调节的静电驱动的链内和链间接触对所起的关键作用，并深入了解所选肽的不同自组织行为。
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