Lysine Bioconjugation on Native Albumin with a Sulfonyl Acrylate Reagent

• Type: Chapter or Part of a Book
• Date: 2019

Authors

Matos, MJ (Author) FCUP; Jiménez Osés, G (Author) Other; Bernardes, GJL (Author) Other

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Other information

Authenticus ID: P-00Q-YDH

DOI: 10.1007/978-1-4939-9654-4_3

Abstract (EN): This protocol details a novel bioconjugation strategy that uses a methanesulfonyl acrylate reagent that is directed to the most reactive lysine on human serum albumin, which enables the construction of chemically defined and stable bioconjugates. The reaction proceeds rapidly and a regioselective modification is achieved using a single molar equivalent of the reagent under biocompatible conditions (37 °C, pH 8.0). Importantly, the bioconjugate retains both the secondary structural content and function of the unmodified protein. During the reaction of the amino group of lysine and the sulfonyl acrylate reagent, methanesulfinic acid is released after the conjugate addition, which then generates an electrophilic acrylate moiety on the protein. This acrylate can be further used for site-specific protein labeling using a synthetic molecule bearing a reactive amine under biocompatible conditions (21 °C, pH 8.0). © Springer Science+Business Media, LLC, part of Springer Nature 2019.

Language: English

Type (Professor's evaluation): Scientific