| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5380362 | Chemical Physics Letters | 2015 | 9 Pages |
Abstract
Surface immobilized peptides/proteins have important applications such as antimicrobial coating and biosensing. We report a study of such peptides/proteins using sum frequency generation vibrational spectroscopy and ATR-FTIR. Immobilization on surfaces via physical adsorption and chemical coupling revealed that structures of chemically immobilized peptides are determined by immobilization sites, chemical environments, and substrate surfaces. In addition, controlling enzyme orientation by engineering the surface immobilization site demonstrated that structures can be well-correlated to measured chemical activity. This research facilitates the development of immobilized peptides/proteins with improved activities by optimizing their surface orientation and structure.
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Authors
Lei Shen, Nathan W. Ulrich, Charlene M. Mello, Zhan Chen,