ANYL 327 |
| Covalent immobilization of peptides on solid supports plays an important role in biochemistry with applications ranging from characterization of molecular recognition events at the amino acid level and identification of biologically active motifs in proteins to development of novel biosensors and substrates for improved cell adhesion. Self-assembled monolayer surfaces (SAMs) provide a simple and convenient platform for tailoring chemical properties of a variety of substrates. Existing techniques for linking peptides to SAMs are based on solution-phase synthetic strategies and require relatively large quantities of purified material. Here, we report a novel approach for highly selective covalent binding of peptides to SAMs using soft-landing (SL) of mass-selected ions. SL is defined as intact deposition of ions onto suitable substrates at hyperthermal (<100 eV) energies. Recent studies have demonstrated that SAMs are excellent deposition targets for SL due to their ability to dissipate kinetic energies of the projectiles and their efficiency in trapping captured species. It has been proposed that SL could be utilized for controlled preparation of protein arrays. This study is the first account of covalent immobilization of mass-selected peptides on SAM surfaces using SL. We demonstrate efficient reactive landing (RL) of several model peptides onto the SAM of N-hydroxysuccinimidyl ester terminated alkylthiol on gold (NHS-SAM) and compare the efficiency of RL with the efficiency of surface modification using reaction in solution. We will discuss the effect of the charge state and ion's kinetic energy on the efficiency of RL. This method introduces unprecedented selectivity and specificity into the surface preparation step by eliminating the effect of solvent and sample contamination on the quality of the film. |
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Frank H. Field and Joe L. Franklin Award for Outstanding Achievement in Mass Spectrometry in Honor of Jean H. Futrell
8:30 AM-12:20 PM, Tuesday, August 21, 2007 BCEC -- 104B, Oral
Division of Analytical Chemistry |