Sequential and Specific Exchange of Multiple Coiled-Coil Components

The capacity for sequential and specific exchange of single peptides from coiled-coil heterotrimers is investigated. Dual hydrophobic−hydrophilic interface systems permit iterative cycles of pH-triggered strand exchange that can specifically replace one, two, or even all three initial trimer compone...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2003-10, Vol.125 (43), p.13046-13051
Main Authors: Schnarr, Nathan A, Kennan, Alan J
Format: Article
Language:English
Subjects:
Alanine - chemistry
Amino Acid Sequence
Biological and medical sciences
Cross-Linking Reagents - chemistry
Fundamental and applied biological sciences. Psychology
Hydrogen-Ion Concentration
Hydrophobic and Hydrophilic Interactions
Intermolecular dynamics
Intermolecular phenomena
Molecular biophysics
Molecular Sequence Data
Nitrilotriacetic Acid - analogs & derivatives
Nitrilotriacetic Acid - chemistry
Organometallic Compounds - chemistry
Peptides - chemistry
Phenylalanine - analogs & derivatives
Phenylalanine - chemistry
Protein Structure, Quaternary
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Summary:The capacity for sequential and specific exchange of single peptides from coiled-coil heterotrimers is investigated. Dual hydrophobic−hydrophilic interface systems permit iterative cycles of pH-triggered strand exchange that can specifically replace one, two, or even all three initial trimer components. The resultant new complexes are either resistant to or capable of further exchange. Control experiments demonstrate that background exchange among different complexes is negligible. When triggered, however, selective displacement of the same peptide from only one of two distinct heterotrimers is feasible. Previously documented peptidic cross-linking strategies remain operative in these more intricate environments.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja035666i