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Maltose-binding protein: a versatile platform for prototyping biosensing

Paper ID Volume ID Publish Year Pages File Format Full-Text
16645 42516 2006 11 PDF Available
Title
Maltose-binding protein: a versatile platform for prototyping biosensing
Abstract

The bacterial periplasmic-binding protein (PBP) superfamily members, in particular the maltose-binding protein, have been used extensively to prototype a variety of biosensing platforms. Although quite diverse at the primary sequence level, this protein superfamily retains the same basic two-domain structure, and upon binding a recognized ligand almost all PBPs undergo a conformational change to a closed structure. This process forms the basis for most, but not all, PBP-based biosensor signal transduction. Many direct detection or reagentless sensing modalities have been utilized with maltose-binding protein for both in vitro and in vivo detection of target compounds. Signal transduction modalities developed to date include direct fluorescence, electrochemical detection, fluorescence resonance energy transfer (FRET)-based detection, surface-tethered FRET sensing, hybrid quantum dot FRET sensing, and enzymatic detection, each of which have different benefits, potential applications and limitations.

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Maltose-binding protein: a versatile platform for prototyping biosensing
Publisher
Database: Elsevier - ScienceDirect
Journal: Current Opinion in Biotechnology - Volume 17, Issue 1, February 2006, Pages 17–27
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering