Molecular recognition of methylated amino acids and peptides by Pillar[6]MaxQ

David King; Chelsea R Wilson; Lukas Herron; Chun-Lin Deng; Shams Mehdi; Pratyush Tiwary; Fraser Hof; Lyle Isaacs

doi:10.1039/d2ob01487d

Molecular recognition of methylated amino acids and peptides by Pillar[6]MaxQ

Org Biomol Chem. 2022 Sep 28;20(37):7429-7438. doi: 10.1039/d2ob01487d.

Authors

David King¹, Chelsea R Wilson², Lukas Herron^{3

4}, Chun-Lin Deng¹, Shams Mehdi^{3

4}, Pratyush Tiwary^{1

4}, Fraser Hof², Lyle Isaacs¹

Affiliations

¹ Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, USA. lisaacs@umd.edu.
² Department of Chemistry, University of Victoria, Victoria, BC, V8W 3V6, Canada. fhof@uvic.ca.
³ Biophysics Program, University of Maryland, College Park, MD 20742, USA.
⁴ Institute for Physical Science and Technology, University of Maryland, College Park, MD 20742, USA. ptiwary@umd.edu.

Abstract

We report the molecular recognition properties of Pillar[n]MaxQ (P[n]MQ) toward a series of (methylated) amino acids, amino acid amides, and post-translationally modified peptides by a combination of ¹H NMR, isothermal titration calorimetry, indicator displacement assays, and molecular dynamics simulations. We find that P6MQ is a potent receptor for N-methylated amino acid side chains. P6MQ recognized the H3K4Me₃ peptide with K_d = 16 nM in phosphate buffered saline.

Publication types

Research Support, U.S. Gov't, Non-P.H.S.
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

MeSH terms

Amides
Amino Acids* / chemistry
Calorimetry
Peptides* / chemistry
Phosphates

Substances

Amides
Amino Acids
Peptides
Phosphates

Abstract

Publication types

MeSH terms

Substances

Grants and funding