Stamping Out Peptides

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Science  20 Aug 2004:
Vol. 305, Issue 5687, pp. 1081
DOI: 10.1126/science.305.5687.1081a

To run a bimolecular reaction, a chemist typically mixes the two reagents in a flask and relies on collisions to bring them together. Sullivan et al. have taken a more forceful approach to inducing molecular encounters. They are able to create peptide (amide) linkages by first preparing a self-assembled monolayer (SAM) of thioamines on a gold surface, and then pressing down on it with a stamp that has been coated with a carboxylate ink. After the stamp is withdrawn and the surface rinsed, infrared spectroscopy and ellipsometry confirm the formation of C-N bonds. The stamp is a surface-oxidized poly(dimethylsiloxane) (PDMS) elastomer used in microcontact printing, and the ink contains any of a variety of N-protected amino acids. When reactions of this sort are run in solution, they generally require a coupling catalyst; none is used in the stamping process. Three successive stamp, rinse, and deprotection cycles produced a layer of Arg-Gly-Asp capable of binding mouse fibroblasts. — JSY

Angew. Chem. Int. Ed. 43, 2 (2004).

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