Peptide Hall of Fame
Saratide is the first example of a beta-hairpin that functions as a molecular receptor. Saratide was first found to bind ATP. It was also shown to bind flavins and tune their redox potential. A dimer of Saratide binds to single stranded and duplex DNA with low micromolar affinity, mimicking certain DNA-binding protein motifs. This is an example of a mini-protein in that the sequence defines the structure which defines the function.
S. M. Butterfield, M. L. Waters*, "A Rationally Designed β-Hairpin Peptide for Molecular Recognition of ATP in Water", J. Am. Chem. Soc., 2003, 125, 9580-9581.
S. M. Butterfield, C. M. Goodman, V. M. Rotello, M. L. Waters*, "A Peptide Flavoprotein Mimic: Flavin Recognition and Redox Potential Modulation in Water Using a Designed β-Hairpin" Angew. Chem. Int. Ed., 2004, 43, 724-727.
S. M. Butterfield, M. M. Sweeney, M. L. Waters*, "Recognition of Nucleotides with Model β-Hairpin Receptors: Investigation of Critical Contacts and Recognition Selectivity", J. Org. Chem., 2005, 70, 1105 - 1114 (highlighted on the cover of issue 4).
S. M. Butterfield, W. J. Cooper, M. L. Waters*, “Minimalist Protein Design: a β-Hairpin Peptide that Binds ssDNA”, J. Am. Chem. Soc., 2005, 127, 24-25.