Metal-Mediated Ligand Affinity Chemistry (MLAC)

Sailajah Gukathasan, Samuel G. Awuah

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review


Metal-mediated ligand affinity chemistry (MLAC) enables site-specific protein modification and represents a powerful bioorthogonal strategy. Conventional bioorthogonal methods often involve two steps: (i) incorporation of the bioorthogonal handle (e.g., non-canonical amino acid, enzyme domain, peptide sequences) and (ii) the binding of functional molecules such as drugs, affinity tags, and fluorophores. This two-step protocol often involves genetic manipulation, which makes it impossible to chemically modify endogenous proteins in living systems. Thus, we propose the development of a transition metal-based chemical strategy that is ligand-directed to the endogenous protein of interest in a single step, which we refer to as metal-mediated ligand affinity chemistry (MLAC).

Original languageEnglish
Title of host publicationMethods in Molecular Biology
Number of pages13
StatePublished - 2024

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029

Bibliographical note

Publisher Copyright:
© The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature 2024.


  • Bioconjugation
  • MLAC
  • Metal-based covalent modification
  • Protein modification

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics


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