Structure-function relationship in the antifreeze activity of synthetic alanine-lysine antifreeze polypeptides.

Academic Article

Abstract

  • Recently antifreeze proteins (AFP) have been the subject of many structure-function relationship studies regarding their antifreeze activity. Attempts have been made to elucidate the structure-function relationship by various amino acid substitutions, but to our knowledge there has been no successful from first principles design of a polypeptide that would bind to designated ice planes along a specific direction. In this paper we show the results of our first attempt on an entirely de novo design of an alanine-lysine-rich antifreeze polypeptide. This 43 residue alanine-lysine peptide exhibits characteristic nonequilibrium freezing point depression and binds to the designated (210) planes of ice along the [122] vector. The structural and thermodynamic properties of this polypeptide were determined using circular dichroism spectroscopy and its nonequilibrium antifreeze properties were investigated using an ice-etching method and nanoliter osmometry.
  • Published In

  • Biomacromolecules  Journal
  • Keywords

  • Alanine, Amino Acid Sequence, Chemical Phenomena, Chemistry, Physical, Circular Dichroism, Crystallization, Freeze Etching, Freezing, Lysine, Molecular Conformation, Molecular Sequence Data, Peptides, Structure-Activity Relationship, Thermodynamics, Water
  • Author List

  • Wierzbicki A; Knight CA; Rutland TJ; Muccio DD; Pybus BS; Sikes CS
  • Start Page

  • 268
  • End Page

  • 274
  • Volume

  • 1
  • Issue

  • 2