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| Bioadhesives When a peptide or protein folds, it of necessity creates an "outer" and an "inner" surface. This raises the possibility the fold could protect a reactive amino acid, and prevent it from undergoing the reactions in which it normally participates.The amino acid cystine has a reactive sulfur atom which normally forms disulfides in the presence of oxygen. If this reaction is prevented by a fold, then it is conceivable the folded peptide would be inert under normal conditions, but then become reactive if the peptide were made to unfold (i.e., denatured). If such a folded peptide were attached to one surface, and the same or a mutated peptide, also with a protected cystine, were attached to another surface, the two surfaces could be joined together by covalent S-S bonds by merely adding a denaturant to the liquid film between the surfaces. |
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Arginine Turn A serendipitous discovery made while designing small molecule binding peptides, this six amino acid peptide folds well in solution around a central arginine core to bring its amino and carboxy termini close together, which can be easily detected using IMAC chromatography. If the ends of the peptide are elaborated with three amino acid long "arms," the arms are held in close proximity, which imparts interesting binding features to the peptide, including the ability to bind phosphate and hydroxylated aromatics. We are exploring this as well as a two-cysteine mutant which has the ability to control its binding allosterically via formation of a disulfide bond. |
| Clam Shell If the Arginine Turn is simply expressed twice in a peptide, with a two-amino acid spacer, the two turns fold separately and arrange themselves with their amino and carboxy ends close together (as in a clam shell), as judged by the GFP-peptide fusion's high IMAC affinity. These clam shells have a deep cleft (that is, the clam's "mouth") that is a potential binding pocket for ligands. |
Clam Shell Binding The binding observed so far for the Arginine Turn is impressive. The clam shell structure, with its high degree of structure and pre-organization, is envisioned to also have small organic molecule binding capabilities. So far we have seen reasonable binding to certain dyes which opens the possibility of energy transfer from GFP to the dye molecule (FRET). |