Functionalized protein-like structures from conformationally defined synthetic combinatorial libraries Article

Pérez-Payá, E, Houghten, RA, Blondelle, SE. (1996). Functionalized protein-like structures from conformationally defined synthetic combinatorial libraries . JOURNAL OF BIOLOGICAL CHEMISTRY, 271(8), 4120-4126. 10.1074/jbc.271.8.4120

cited authors

  • Pérez-Payá, E; Houghten, RA; Blondelle, SE

abstract

  • An approach is described for the de novo design of protein-like structures in which synthetic combinatorial libraries (SCLs) were incorporated into an amphipathic α-helical scaffold (an 18-mer sequence made up of leucine and lysine residues) to generate conformationally defined SCLs. In particular, the SCLs in which the 'combinatorialized' positions were on the hydrophilic face showed an α-helical conformation in mild buffer. These SCLs were used to generate context-independent but position-dependent scales of α-helical propensity for the L-amino acids. These scales were then used to design highly α-helical peptides that self-associated in mild buffer. The same approach was also found to permit the identification of conformation- dependent decarboxylation catalysts.

publication date

  • February 23, 1996

published in

Digital Object Identifier (DOI)

start page

  • 4120

end page

  • 4126

volume

  • 271

issue

  • 8