Structure−Function Relationship in the Antifreeze Activity of Synthetic Alanine−Lysine Antifreeze Polypeptides
- 11 May 2000
- journal article
- Published by American Chemical Society (ACS) in Biomacromolecules
- Vol. 1 (2) , 268-274
- https://doi.org/10.1021/bm000004w
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.Keywords
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