194
1. Merkx M, Golynskiy MV, Lindenburg LH et al
(2013) Rational design of FRET sensor proteins based on mutually exclusive domain interactions. Biochem Soc Trans 41:1201–1205
2. Ricci F, Vallée-Bélisle A, Porchetta A et al (2012)
Rational design of allosteric inhibitors and activators using the population-shift model: In vitro
validation and application to an artificial biosensor. J Am Chem Soc 134:15177–15180
3. Arts R, den Hartog I, Zijlema SE et al (2016)
Detection of antibodies in blood plasma using
bioluminescent sensor proteins and a smartphone. Anal Chem 88:4525–4532
4. Vinkenborg JL, Nicolson TJ, Bellomo EA et al
(2009) Genetically encoded FRET sensors to
monitor intracellular Zn
2+
homeostasis. Nat
Methods 6:737–740
5. Hessels AM, Chabosseau P, Bakker MH et al
(2015) eZinCh-2: a versatile, genetically
encoded FRET sensor for cytosolic and intraorganelle Zn
2+
imaging, ACS Chem. Biol
10:2126–2134
6. van der Velden LM, Golynskiy MV, Bijsmans
ITGW et al (2013) Monitoring bile acid transport in single living cells using a genetically
encoded Förster resonance energy transfer sensor. Hepatology 57:740–752
7. Golynskiy MV, Rurup WF, Merkx M (2010)
Antibody detection by using a FRET-based
protein conformational switch. ChemBioChem
11:2264–2267
8. Banala S, Aper SJA, Schalk W et al (2013)
Switchable reporter enzymes based on mutually exclusive domain interactions allow antibody detection directly in solution. ACS Chem
Biol 8:2127–2132
9. Furman JL, Badran AH, Ajulo O et al (2010)
Toward a general approach for RNA-templated
hierarchical assembly of split-proteins. J Am
Chem Soc 132:11692–11701
10. Sancho Oltra N, Bos J, Roelfes G (2010)
Control over enzymatic activity by DNAdirected split enzyme reassembly. ChemBio
Chem 11:2255–2258
11. Strynadka NC, Jensen SE, Alzari PM et al
(1996) A potent new mode of beta-lactamase
inhibition revealed by the 1.7 Å X-ray crystallographic structure of the TEM-1-BLIP complex. Nat Struct Biol 3:290–297
12. Wang J, Palzkill T, Chow DC (2009) Structural
insight into the kinetics and ΔCp of interactions between TEM-1 β-lactamase and
β-lactamase inhibitory protein (BLIP). J Biol
Chem 284:595–609
13. Janssen BMG, Engelen W, Merkx M (2015)
DNA-directed control of enzyme–inhibitor
complex formation: a modular approach to
reversibly switch enzyme activity. ACS Synth
Biol 4:547–553
14. Tyagi S, Kramer FR (1996) Molecular beacons:
probes that fluoresce upon hybridization. Nat
Biotechnol 14:303–308
Acknowledgments
The authors would like to thank Dr. Brian Janssen for co-developing
the methods described in this chapter. This work was supported
by an ERC Starting grant (ERC-2011- StG-280255) and by
NanoNextNL, a micro and nanotechnology consortium of the
government of The Netherlands and 130 partners.
References
Wouter Engelen and Maarten Merkx
1. Merkx M, Golynskiy MV, Lindenburg LH et al
(2013) Rational design of FRET sensor proteins based on mutually exclusive domain interactions. Biochem Soc Trans 41:1201–1205
2. Ricci F, Vallée-Bélisle A, Porchetta A et al (2012)
Rational design of allosteric inhibitors and activators using the population-shift model: In vitro
validation and application to an artificial biosensor. J Am Chem Soc 134:15177–15180
3. Arts R, den Hartog I, Zijlema SE et al (2016)
Detection of antibodies in blood plasma using
bioluminescent sensor proteins and a smartphone. Anal Chem 88:4525–4532
4. Vinkenborg JL, Nicolson TJ, Bellomo EA et al
(2009) Genetically encoded FRET sensors to
monitor intracellular Zn
2+
homeostasis. Nat
Methods 6:737–740
5. Hessels AM, Chabosseau P, Bakker MH et al
(2015) eZinCh-2: a versatile, genetically
encoded FRET sensor for cytosolic and intraorganelle Zn
2+
imaging, ACS Chem. Biol
10:2126–2134
6. van der Velden LM, Golynskiy MV, Bijsmans
ITGW et al (2013) Monitoring bile acid transport in single living cells using a genetically
encoded Förster resonance energy transfer sensor. Hepatology 57:740–752
7. Golynskiy MV, Rurup WF, Merkx M (2010)
Antibody detection by using a FRET-based
protein conformational switch. ChemBioChem
11:2264–2267
8. Banala S, Aper SJA, Schalk W et al (2013)
Switchable reporter enzymes based on mutually exclusive domain interactions allow antibody detection directly in solution. ACS Chem
Biol 8:2127–2132
9. Furman JL, Badran AH, Ajulo O et al (2010)
Toward a general approach for RNA-templated
hierarchical assembly of split-proteins. J Am
Chem Soc 132:11692–11701
10. Sancho Oltra N, Bos J, Roelfes G (2010)
Control over enzymatic activity by DNAdirected split enzyme reassembly. ChemBio
Chem 11:2255–2258
11. Strynadka NC, Jensen SE, Alzari PM et al
(1996) A potent new mode of beta-lactamase
inhibition revealed by the 1.7 Å X-ray crystallographic structure of the TEM-1-BLIP complex. Nat Struct Biol 3:290–297
12. Wang J, Palzkill T, Chow DC (2009) Structural
insight into the kinetics and ΔCp of interactions between TEM-1 β-lactamase and
β-lactamase inhibitory protein (BLIP). J Biol
Chem 284:595–609
13. Janssen BMG, Engelen W, Merkx M (2015)
DNA-directed control of enzyme–inhibitor
complex formation: a modular approach to
reversibly switch enzyme activity. ACS Synth
Biol 4:547–553
14. Tyagi S, Kramer FR (1996) Molecular beacons:
probes that fluoresce upon hybridization. Nat
Biotechnol 14:303–308
Acknowledgments
The authors would like to thank Dr. Brian Janssen for co-developing
the methods described in this chapter. This work was supported
by an ERC Starting grant (ERC-2011- StG-280255) and by
NanoNextNL, a micro and nanotechnology consortium of the
government of The Netherlands and 130 partners.
References
Wouter Engelen and Maarten Merkx