Maltose-binding protein: a versatile platform for prototyping biosensing.
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.
Medintz
Igor L
IL
Center for Bio/Molecular Science and Engineering, Code 6900, Laboratory for the Structure of Matter, Code 6812, US Naval Research Laboratory, WA 20375-5320, USA. imedintz@cbmse.nrl.navy.mil
Deschamps
Jeffrey R
JR
D015374:Biosensing Techniques; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D004563:Electrochemistry; D005453:Fluorescence; D031541:Fluorescence Resonance Energy Transfer; D005456:Fluorescent Dyes; D058619:Maltose-Binding Proteins; D033902:Periplasmic Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D045663:Quantum Dots
D002352:Carrier Proteins; D005456:Fluorescent Dyes; D058619:Maltose-Binding Proteins; D033902:Periplasmic Binding Proteins