Discovering de novo peptide substrates for enzymes using machine learning

Nat Commun. 2018 Dec 7;9(1):5253. doi: 10.1038/s41467-018-07717-6.

Abstract

The discovery of peptide substrates for enzymes with exclusive, selective activities is a central goal in chemical biology. In this paper, we develop a hybrid computational and biochemical method to rapidly optimize peptides for specific, orthogonal biochemical functions. The method is an iterative machine learning process by which experimental data is deposited into a mathematical algorithm that selects potential peptide substrates to be tested experimentally. Once tested, the algorithm uses the experimental data to refine future selections. This process is repeated until a suitable set of de novo peptide substrates are discovered. We employed this technology to discover orthogonal peptide substrates for 4'-phosphopantetheinyl transferase, an enzyme class that covalently modifies proteins. In this manner, we have demonstrated that machine learning can be leveraged to guide peptide optimization for specific biochemical functions not immediately accessible by biological screening techniques, such as phage display and random mutagenesis.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Bayes Theorem
  • Machine Learning*
  • Peptides / genetics
  • Peptides / metabolism*
  • Protein Binding
  • Recombinant Proteins / metabolism
  • Substrate Specificity
  • Transferases (Other Substituted Phosphate Groups) / genetics
  • Transferases (Other Substituted Phosphate Groups) / metabolism*

Substances

  • Bacterial Proteins
  • Peptides
  • Recombinant Proteins
  • phosphopantetheinyl transferase
  • Transferases (Other Substituted Phosphate Groups)