Abstract
Surface plasmon resonance (SPR) analytical method was initially used as biosensor for analyzing diverse biomolecular interactions and recently gained important place in the drug discovery. Here, I describe the procedures for screening of inhibitors against the viral proteins using the SPR. Using the described procedures, in the past, we were able to identify several antiviral products that interfere viral-host receptor proteins interactions.
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References
Shuker SB, Hajduk PJ, Meadows RP et al (1996) Discovering high-affinity ligands for proteins: SAR by NMR. Science 274:1531–1534
Mayer M, Meyer B (1999) Characterization of ligand binding by saturation transfer difference NMR spectroscopy. Angew Chem Int Ed 38:1784–1788
Blundell TL, Jhoti H, Abell C (2002) High-throughput crystallography for lead discovery in drug design. Nat Rev Drug Discov 1:45–54
Duong-Thi MD, Bergstrom M, Fex T et al (2013) High-throughput fragment screening by affinity LC-MS. J Biomol Screen 18:160–171
Ladbury JE, Klebe G, Freire E (2010) Adding calorimetric data to decision making in lead discovery: a hot tip. Nat Rev Drug Discov 9:23–27
Kranz JK, SChalk-Hihi C (2011) Protein thermal shifts to identify low molecular weight fragments. Methods Enzymol 493:277–298
Lewis LM, Engle LJ, Pierceall WE et al (2004) Affinity capillary electrophoresis for the screening of novel antimicrobial targets. J Biomol Screen 9:303–308
Duong-Thi MD, Meiby E, Bergstrom M et al (2011) Weak affinity chromatography as a new approach for fragment screening in drug discovery. Anal Biochem 414:138–146
Proll F, Fechner P, Proll G (2001) Direct optical detection in fragment-based screening. Anal Bioanal Chem 393:1557–1562
Myszka DG, Rich RL (2000) Implementing surface plasmon resonance biosensors in drug discovery. Pharm Sci Technol Today 3:310–317
Cooper MA (2003) Label-free screening of biomolecular interactions. Anal Bioanal Chem 377:834–842
Lofas S (2004) Optimizing the hit-to-lead process using SPR analysis. Assay Drug Dev Technol 2:407–416
Huber W (2005) A new strategy for improved secondary screening and lead optimization using high-resolution SPR characterization of compound-target interactions. J Mol Recognit 18:273–281
Geschwindner S, Olsson LL, Albert JS et al (2007) Discovery of a novel warhead β-secretase through fragment-based lead generation. J Med Chem 50:5903–5911
Godemann R, Madden J, Kramer J et al (2009) Fragment-based discovery of BACE1 inhibitors using functional assays. Biochemistry 48:10743–10751
Cole DC, Olland AM, Jacob J et al (2010) Identification and characterization of acidic mammalian chitinase inhibitors. J Med Chem 53:6122–6128
Giannetti AM (2011) From experimental design to validation hits a comprehensive walk-through of fragment lead identification using surface plasmon resonance. Methods Enzymol 493:169–218
Gopinath SC, Hayashi K, Kumar PKR (2012) Aptamer that binds to the gD protein of herpes simplex virus 1 and efficiently inhibits viral entry. J Virol 86:6732–6744
Gopinath SC, Hayashi K, Lee JB et al (2013) Analysis of compounds that interfere with herpes simplex virus-host receptor interactions using surface plasmon resonance. Anal Chem 85:10455–10462
Suenaga E, Kumar PKR (2014) An aptamer that binds efficiently to the hemagglutinins of highly pathogenic avian influenza viruses (H5N1 and H7N7) and inhibits hemagglutinin-glycan interactions. Acta Biomater 10:1314–1323
Zhang N, Yan J, Lu G et al (2011) Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion. Nat Commun 2:577. https://doi.org/10.1038/ncomms1571
Karlesson R, Katsamba PS, Nordin H et al (2006) Analyzing a kinetic titration series using affinity biosensors. Anal Biochem 349:136–147
Suenaga E, Mizuno H, Kumar PKR (2012) Monitoring influenza hemagglutinin and glycan interactions using surface plasmon resonance. Biosens Bioelectron 32:195–201
Biacore: Concentration analysis Handbook BR-1005-12 Edition AB (2007) GE Healthcare, Supplied with T100 Biacore machine. 53–54
Hayashi K, Kawauchi M, Nakai C et al (2001) Characterization of inhibitory action of concanamycins against herpes simplex virus. Antivir Chem Chemother 12:51–59
Srisomporn P, Hayashi K, Lee JB et al (2001) Effects of structural modification of calcium spirulan, a sulfated polysaccharide from spirulina platensis, on antiviral activity. Chem Pharm Bull 49:484–485
Shukla D, Liu J, Blaiklock P et al (1999) A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry. Cell 99:13–22
Liu J, Shriver Z, Pope RM (2002) Characterization of a heparan sulfate octasaccharide that binds to herpes simplex virus type 1 glycoprotein D. J Biol Chem 277:33456–33467
Acknowledgment
This work was supported by grants from JST and AIST to P.K.R.K.
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Kumar, P.K.R. (2020). Systematic Screening of Viral Entry Inhibitors Using Surface Plasmon Resonance. In: Labrou, N. (eds) Targeting Enzymes for Pharmaceutical Development. Methods in Molecular Biology, vol 2089. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0163-1_8
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DOI: https://doi.org/10.1007/978-1-0716-0163-1_8
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