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Protein Science (2007), 16:582-588. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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Computational design and biochemical characterization of maize nonspecific lipid transfer protein variants for biosensor applications

Eun Jung Choi1,3, Jessica Mao1,3, and Stephen L. Mayo2

1 Division of Biology, California Institute of Technology, Pasadena, California 91125, USA
2 Howard Hughes Medical Institute, Division of Biology and Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA

(RECEIVED October 9, 2006; FINAL REVISION October 9, 2006; ACCEPTED December 9, 2006)

Lipid transfer proteins (LTPs) are a family of proteins that bind and transfer lipids. Utilizing the maize LTP, we have successfully engineered fluorescent reagentless biosensors for the natural ligand of LTPs; this was achieved by using computational protein design to remove a disulfide bridge and attaching a thio-reactive fluorophore. Conformational change induced by ligand titration is thought to affect the fluorescence of the fluorophore, allowing detection of ligand binding. Fluorescence measurements show that our LTP variants have affinity to palmitate that is consistent with wild-type LTP. These molecules have the potential to be utilized as scaffolds to design hydrophobic ligand biosensors or to serve as drug carriers.

Keywords: biosensor; disulfide bond; fluorescence; lipid transfer protein; protein design


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