三价阳离子在气-水界面诱导功能性肽的凝胶化
Gelation of functional peptides by trivalent cations at the air-water interface
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中文总结 AI 辅助
研究气-水界面由多价阳离子介导桥接驱动的凝胶化机制，肽结合镧系阳离子后配位几何转变，电荷反转形成凝胶，其由可逆金属-配体配位键稳定，揭示肽配位球破裂是独特界面凝胶化途径，独立于体相蛋白质聚集的静电机制。
中文摘要 AI 辅助
我们报告了一种由多价阳离子介导的桥接驱动的流体界面凝胶化机制。在气-水界面，结合镧系阳离子的肽经历配位几何转变，使金属从单肽结合态转变为多肽桥接态，引发电荷反转和凝胶形成。表面吸附和非理想界面静电作用参与此转变。凝胶由可逆金属-配体配位键稳定，能抵抗体相盐屏蔽，与蛋白质中的静电电荷反转凝胶化根本不同。这揭示了肽配位球的破裂是界面凝胶化的独特途径，独立于控制体相蛋白质聚集的扩散静电机制。
英文摘要
We report a mechanism for gelation at fluid interfaces driven by multivalent-cation-mediated bridging. At the air-water interface, peptides with bound lanthanide cations undergo a coordination-geometry transition that converts the metal from a single-peptide bound state to a multi-peptide bridging state, driving charge inversion and gel formation. Surface adsorption and non-ideal interfacial electrostatics are implicated in this transition. The gel is stabilized by reversible metal-ligand coordination bonds that resist bulk salt screening, fundamentally distinct from electrostatic charge-inversion gelation in proteins. This reveals the breakdown of the peptide's coordinating sphere as a distinct pathway for interfacial gelation, independent of the diffuse electrostatic mechanisms governing bulk protein aggregation.
