Methodologies for the Precise Modification of Guest Molecules by Proteins
Precise modification of guest molecules on proteins is a crucial technological foundation for supramole-cular modulation of protein activity.This is especially true for aromatic functional group guests containing positive charges,which can be efficiently bound to cucurbituril.However,precise modification of these molecules on proteins using non-canonical amino acid site specific modification technology can be challenging.The linkers of bioorthogonal reactions are often large,which can affect the recognition of the host and guest molecules.To address this issue,the target proteins were modified by adding iodine-or alkynyl-functional amino acids using the non-canonical amino acid site specific modification technology.The pyridine molecules with a positive charge were efficiently bound to cucurbi-turil molecules using the palladium-catalyzed Suzuki and Sonogashira coupling reaction.Subsequently,a non-natural amino acid with an alkynyl functional group was successfully incorporated into the target proteins using a series of reaction conditions.Furthermore,a Sonogashira coupling reaction was utilized to attach a positively charged pyridine molecule to the protein surface.These accomplishments establish a crucial technological basis for the chemical regulation of proteins through host-guest interactions.
Precise modificationNon-canonical amino acidHost and guestProtein
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