N -Aminoglycine and Its Derivatives Stabilize PPII Secondary Structure.
Benjamin H RajewskiMadison M WrightTaylor A GerreinJuan R Del VallePublished in: Organic letters (2023)
The identification of unnatural residues that stabilize polyproline type 2 (PPII) folds can aid in the design of peptidomimetics targeting PPII-binding domains. Here, we examine the impact of peptide backbone N-amination on PPII helix stability and find N -aminoglycine (aGly) to be an effective PPII promoter. Further derivatization of an aGly-containing peptide affords N '-alkylated analogues with increased helical propensity. Backbone N-amination of glycine represents a convenient approach to stabilize PPII conformation and allows for the diversity-oriented synthesis of optimally constrained folds.
Keyphrases
- dna binding
- dna methylation
- transcription factor
- ms ms
- gene expression
- structure activity relationship
- liquid chromatography tandem mass spectrometry
- molecular dynamics simulations
- molecular docking
- liquid chromatography
- cancer therapy
- simultaneous determination
- gas chromatography mass spectrometry
- high performance liquid chromatography
- tandem mass spectrometry
- mass spectrometry
- crystal structure
- binding protein
- solid phase extraction
- gas chromatography