Tryptophan-Based Self-Assembling Peptides with Bacterial Flocculation and Antimicrobial Properties.,Langmuir

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Tryptophan-Based Self-Assembling Peptides with Bacterial Flocculation and Antimicrobial Properties.
Langmuir ( IF 3.7 ) Pub Date : 2020-09-09 , DOI: 10.1021/acs.langmuir.0c01957
Jikun Zhang ₁ , Shengnan Liu ₁ , Hang Li ₁ , Xin Tian ₂ , Xinming Li ₁

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Tryptophan as an aromatic amino acid with a hydrophobic indole group plays important roles in stabilizing protein structures and enhancing molecular bindings in nature, but was rarely used in the molecular design of self-assembling peptides or gelators. Therefore, we prepared a series of short peptides from Trp amino acids and examined the potential roles of Trp residues for regulating peptide self-assembly and gelation. The introduced Trp amino acids not only diversify the molecular structures of peptide gelators, but also promote aromatic and hydrogen-bonding interactions for supramolecular self-assembling and gelation, which generates self-assembled nanostructures with twisted helical morphologies and supramolecular hydrogels with low minimal gelation concentrations. More importantly, the self-assembling peptides with Trp residues displayed strong preference for interacting with the lipidic membranes of bacteria, which resulted in bacterial flocculation and the death of E. coli and S. aureus.

中文翻译：

基于色氨酸的自组装肽，具有细菌絮凝作用和抗菌特性。

色氨酸作为具有疏水性吲哚基团的芳香族氨基酸，在稳定蛋白质结构和增强自然界中的分子结合方面起着重要作用，但很少用于自组装肽或胶凝剂的分子设计中。因此，我们从Trp氨基酸制备了一系列短肽，并研究了Trp残基在调节肽自组装和凝胶化中的潜在作用。引入的Trp氨基酸不仅使肽胶凝剂的分子结构多样化，而且还促进了超分子自组装和凝胶化的芳族和氢键相互作用，从而产生了具有扭曲的螺旋形态的自组装纳米结构和具有最低最低胶凝浓度的超分子水凝胶。更重要的是，大肠杆菌和金黄色葡萄球菌。

更新日期：2020-09-29

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