Modification of Amino Groups

doi:10.1002/cpps.17

Modification of Amino Groups

2016-11-01

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DOI：10.1002/cpps.17

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AbstractChemical modification of amino groups in proteins serves a diversity of preparative and analytical purposes. The most prominent is to attach nonpeptide groups with useful properties to proteins. Examples of these groups include biotin for affinity capture and fluorescent dyes for detectability. A widely applied chemistry, and one for which many reagents are available, is reaction of the activated ester of a carboxylic acid (often a succinimidyl ester) with amino groups at mildly basic pH. Reductive alkylation using a carbonyl compound and a hydride‐donating reducing agent is another valued reaction with multiple applications. Most proteins contain more than one amino group, so the extent of reaction desired must be considered in advance and the result assessed experimentally after the fact. The distinctive environment of the α‐amino group of a polypeptide sets it apart from the ɛ‐amino groups of lysine side chains, and can afford useful specificity. © 2016 by John Wiley & Sons, Inc.

Modification of Amino Groups

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