Structure-Function Relationship in the Antifreeze Activity of Synthetic Alanine-Lysine Antifreeze Polypeptides
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- 作者：Andrzej Wierzbicki ; Charles A. Knight ; Travis J. Rutland ; Donald D. Muccio ; Brandon S. Pybus ; and C. Steven Sikes
- 刊名：Biomacromolecules
- 出版年：2000
- 出版时间：June 2000
- 年：2000
- 卷：1
- 期：2
- 页码：268 - 274
- 全文大小：258K
- 年卷期：v.1,no.2(June 2000)
- ISSN：1526-4602
文摘
Recently antifreeze proteins (AFP) have been the subject of many structure-function relationship studiesregarding their antifreeze activity. Attempts have been made to elucidate the structure-function relationshipby various amino acid substitutions, but to our knowledge there has been no successful from first principlesdesign of a polypeptide that would bind to designated ice planes along a specific direction. In this paper weshow the results of our first attempt on an entirely de novo design of an alanine-lysine-rich antifreezepolypeptide. This 43 residue alanine-lysine peptide exhibits characteristic nonequilibrium freezing pointdepression and binds to the designated (2
0) planes of ice along the [122] vector. The structural andthermodynamic properties of this polypeptide were determined using circular dichroism spectroscopy andits nonequilibrium antifreeze properties were investigated using an ice-etching method and nanoliterosmometry.
0) planes of ice along the [122] vector. The structural andthermodynamic properties of this polypeptide were determined using circular dichroism spectroscopy andits nonequilibrium antifreeze properties were investigated using an ice-etching method and nanoliterosmometry.