Immobilization of sunflower trypsin inhibitor (SFTI-1) peptide onto a gold surface and analysis of its interaction with trypsin

Sunflower trypsin inhibitor (SFTI-1) derived peptide having one disulfide bond could be immobilized via a thiol-disulfide exchange reaction onto a gold surface on a quartz crystal microbalance (QCM) chip. This permitted quantitative analysis of the specific interaction with trypsin.

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Bibliographic Details
Published in:Analyst (London) 2004-01, Vol.129 (10), p.888-889
Main Authors: OHTSUKA, Keiichi, KAJIKI, Ryo, WAKI, Michinori, NOJIMA, Takahiko, TAKENAKA, Shigeori
Format: Article
Language:English
Subjects:
Analytical chemistry
Biosensing Techniques
Chemistry
Exact sciences and technology
General, instrumentation
Gold
Helianthus
Peptides, Cyclic - chemistry
Protein Interaction Mapping - methods
Trypsin - chemistry
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Description
Summary:Sunflower trypsin inhibitor (SFTI-1) derived peptide having one disulfide bond could be immobilized via a thiol-disulfide exchange reaction onto a gold surface on a quartz crystal microbalance (QCM) chip. This permitted quantitative analysis of the specific interaction with trypsin.
ISSN:0003-2654
1364-5528
DOI:10.1039/b409178g