ENZYMATIC MODIFICATION AND X-RAY PHOTOELECTRON-SPECTROSCOPY ANALYSIS OF A FUNCTIONALIZED POLYDIACETYLENE THIN-FILM

被引：17

作者：

WILSON, TE ^{[1
]}

SPEVAK, W ^{[1
]}

CHARYCH, DH ^{[1
]}

BEDNARSKI, MD ^{[1
]}

机构：

[1] UNIV CALIF BERKELEY,DEPT CHEM,BERKELEY,CA 94720

来源：

LANGMUIR | 1994年 / 10卷 / 05期

关键词：

D O I：

10.1021/la00017a031

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The mild conditions and specificity of biological catalysts are attractive incentives for their use in the formation of surfaces with well-defined chemical functionality. Herein, we describe the synthesis, characterization, and enzymatic modification of a functionalized polymeric bilayer assembly. The assembly is composed of a self-assembled monolayer of octadecylsilane and a Langmuir-Blodgett monolayer of polydiacetylene functionalized with the dipeptide phenylalanine-alanine (Phe-Ala). We demonstrate via X-ray photoelectron spectroscopy surface analysis that the surface-bound Phe-Ala dipeptide is a substrate for specific cleavage by the enzyme subtilisin BPN'. In-situ surface transformations via enzymatic synthesis or cleavage offer an alternative to chemical treatments of organic thin films.

引用

页码：1512 / 1516

页数：5

共 27 条

[1] FORMATION OF MONOLAYERS BY THE COADSORPTION OF THIOLS ON GOLD - VARIATION IN THE HEAD GROUP, TAIL GROUP, AND SOLVENT [J].