Selection of a buried salt bridge by phage display
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- 作者：Toni Vagt ; Christian Jä ; ckel ; Sergey Samsonov ; M. Teresa Pisabarro ; Beate Koksch
- 关键词：Phage display ; α ; -Helical coiled coil ; Molecular dynamics ; Protein design
- 刊名：Bioorganic and Medicinal Chemistry Letters
- 出版年：2009
- 出版时间：15 July 2009
- 年：2009
- 卷：19
- 期：14
- 页码：3924-3927
- 全文大小：253 K
文摘
The α-helical coiled coil is a valuable folding motif for protein design and engineering. By means of phage display technology, we selected a capable binding partner for one strand of a coiled coil bearing a charged amino acid in a central hydrophobic core position. This procedure resulted in a novel coiled coil pair featuring an opposed Glu-Lys pair arranged staggered within the hydrophobic core of a coiled coil structure. Structural investigation of the selected coiled coil dimer by CD spectroscopy and MD simulations suggest that a buried salt bridge within the hydrophobic core enables the specific dimerization of two peptides.