Te. Wilson et al., ENZYMATIC MODIFICATION AND X-RAY PHOTOELECTRON-SPECTROSCOPY ANALYSIS OF A FUNCTIONALIZED POLYDIACETYLENE THIN-FILM, Langmuir, 10(5), 1994, pp. 1512-1516
The mild conditions and specificity of biological catalysts are attrac
tive incentives for their use in the formation of surfaces with well-d
efined chemical functionality. Herein, we describe the synthesis, char
acterization, and enzymatic modification of a functionalized polymeric
bilayer assembly. The assembly is composed of a self-assembled monola
yer of octadecylsilane and a Langmuir-Blodgett monolayer of polydiacet
ylene functionalized with the dipeptide phenylalanine-alanine (Phe-Ala
). We demonstrate via X-ray photoelectron spectroscopy surface analysi
s that the surface-bound Phe-Ala dipeptide is a substrate for specific
cleavage by the enzyme subtilisin BPN'. In-situ surface transformatio
ns via enzymatic synthesis or cleavage offer an alternative to chemica
l treatments of organic thin films.