Synthesis of a negatively charged dibenzofuran-based beta-turn mimetic and its incorporation into the WW miniprotein-enhanced solubility without a loss of thermodynamic stability

J Am Chem Soc. 2002 Oct 9;124(40):11900-7. doi: 10.1021/ja020675x.

Abstract

A versatile synthesis has been developed to functionalize the 4-(2-aminoethyl)-6-dibenzofuran propionic acid residue (1a) at the 2 and 8 positions with a variety of different substructures. The unfunctionalized version of this peptidomimetic (1a) is known to facilitate beta-hairpin formation in a variety of small peptides and proteins in aqueous solution when incorporated in place of the i + 1 and i + 2 residues of a beta-turn. In this study, we append propionate substituents on 1a at the 2 and 8 positions to successfully overcome solubility problems encountered with the incorporation of 1a in place of the i + 1 and i + 2 residues of the beta-turn in loop 1 of the WW domain. The thermodynamic stability of several WW domain analogues incorporating residues 1a and 1b was compared to that of the wild-type sequence revealing comparable DeltaG(H(2)O) unfolding values at 4 degrees C ranging from 3 to 3.6 kcal/mol. WW domains incorporating residue 1b exhibit improved solubility (exceeding 100 microM) and resistance to aggregation without compromising thermodynamic stability.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Benzofurans / chemical synthesis
  • Benzofurans / chemistry*
  • Biophysics / methods
  • Models, Molecular
  • Molecular Mimicry
  • Molecular Sequence Data
  • NIMA-Interacting Peptidylprolyl Isomerase
  • Peptide Fragments / chemistry
  • Peptidylprolyl Isomerase / chemistry*
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Thermodynamics

Substances

  • Benzofurans
  • NIMA-Interacting Peptidylprolyl Isomerase
  • Peptide Fragments
  • Peptidylprolyl Isomerase