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Controlling orientations of immobilized oligopeptides using N-terminal cysteine labels.
- Source :
-
Langmuir : the ACS journal of surfaces and colloids [Langmuir] 2008 May 20; Vol. 24 (10), pp. 5238-40. Date of Electronic Publication: 2008 Apr 10. - Publication Year :
- 2008
-
Abstract
- This letter reports a strategy of using N-terminal cysteine labels for controlling the immobilization of oligopeptides on aldehyde-terminated surfaces through the formation of stable thiazolidine rings. We also study the effect of cysteine position (either N-terminal or C-terminal) and lysine residue on the immobilization of oligopeptides. On the basis of our ellipsometry and quartz crystal microbalance (QCM) results, we conclude that the proposed immobilization strategy is highly site-specific. It works only when cysteine is in the N-terminal position, and the formation of thiazolidine is much faster than the formation of imines between lysine residues and aldehydes, even in the presence of a reducing agent such as NaBH(3)CN. By labeling an oligopeptide CSNKTRIDEANNKATKML with an N-terminal cysteine, we immobilize this oligopeptide on an aldehyde-terminated surface and investigate the enzymatic activity of trypsin acting on the oligopeptide. It is found that trypsin is able to cleave the immobilized oligopeptide having a single anchoring point at the N-terminal cysteine. No cleavage is observed when the oligopeptide is immobilized through multiple anchoring points at lysine residues.
Details
- Language :
- English
- ISSN :
- 0743-7463
- Volume :
- 24
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- Langmuir : the ACS journal of surfaces and colloids
- Publication Type :
- Academic Journal
- Accession number :
- 18399669
- Full Text :
- https://doi.org/10.1021/la800458s