Modifying the surface of peptide nanofibers utilizing a thiol‐thioester exchange,Peptide Science

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Modifying the surface of peptide nanofibers utilizing a thiol‐thioester exchange
Peptide Science ( IF 1.5 ) Pub Date : 2020-04-29 , DOI: 10.1002/pep2.24169
Ramiz Haddad ₁ , Elizabeth Ferraro ₁ , Ashley Halmans ₁ , Jillian E. Smith‐Carpenter ₁

Affiliation

Herein, we report on the incorporation of a dithioester modification to a self‐assembling peptide and characterize a thiol‐thioester exchange on the nanofiber's surface with respect to amount of soluble exogenous thiol present and pH of the reaction. The ratios of all peptide species throughout the exchange reaction were reproducibly monitored by matrix‐assisted laser desorption ionization time‐of‐flight (MALDI‐TOF) mass spectrometry, highlighting the utility of MALDI to characterize heterogeneous and dynamic supramolecular systems. The tuneable revealing of thiols through a dynamic covalent chemical reaction presents a new strategy for labeling supramolecular surfaces. This strategy of combining reversible peptide self‐assembly and dynamic covalent chemistry opens another route for the post‐assembly modification of amyloid‐based supramolecular structures and the design of functional biomaterials.

中文翻译：

利用硫醇-硫酯交换修饰肽纳米纤维的表面

在本文中，我们报道了将二硫酯修饰基团结合到自组装肽中，并表征了纳米纤维表面硫醇-硫酯交换相对于可溶性外源硫醇的存在量和反应的pH值。通过基质辅助激光解吸电离飞行时间（MALDI-TOF）质谱可重现地监测整个交换反应中所有肽类的比率，突出了MALDI在表征异质和动态超分子系统中的实用性。通过动态共价化学反应可调节地揭示硫醇，为标记超分子表面提出了一种新策略。

更新日期：2020-04-29

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