Using Peptide Arrays to Discover the Sequence-Specific Acetylation of the Histidine-Tyrosine Dyad

Lindsey C. Szymczak, Milan Mrksich*

*Corresponding author for this work

Research output: Contribution to journalArticle

Abstract

Reactions that can selectively modify amino acid sequences within peptides and proteins are important for preparing protein reagents, immobilizing proteins, and making antibody-drug conjugates. The development of new reactions often begins with known chemistries and optimizes yields using a small set of peptide reactants. This article describes the use of peptide arrays and self-assembled monolayers for matrix-assisted laser desorption/ionization mass spectrometry (SAMDI-MS) to discover and characterize unanticipated sequence-selective reactions of peptides. This work reports the selective acetylation of HY (histidine-tyrosine) and YH (tyrosine-histidine) dyads when treated with acetic anhydride in aqueous conditions. More broadly, this example illustrates the benefits of using peptide arrays and a label-free analysis method to discover peptide-modifying reactions and gain mechanistic insight into their sequence specificity.

Original languageEnglish (US)
Pages (from-to)1810-1817
Number of pages8
JournalBiochemistry
Volume58
Issue number13
DOIs
StatePublished - Apr 2 2019

ASJC Scopus subject areas

  • Biochemistry

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