Cited by 223Computational Drug Discovery MethodsChemical Synthesis and AnalysisReceptor Mechanisms and Signaling

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Ligand efficiency and fragment-based drug discovery

Bembenek, Scott D., Tounge, Brett A., Reynolds, Charles H.·2009·Drug Discovery Today

DOI 10.1016/j.drudis.2008.11.007

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Abstract

The use of fragment-based drug discovery (FBDD) has increased in recent years since it is more likely to produce a better optimized compound of lower molecular weight. Ligand efficiency (LE) has become important for assessing fragments, HTS hits, and resulting optimized ligands. LE is useful for comparing ligands of equal molecular weight, but is ineffective for comparisons of ligands of differing molecular weight. LE has a strong dependence on molecular size, which has led us to develop a size-independent efficiency score termed fit quality. Evaluating FBDD examples from the literature using LE and fit quality, we find that, in general, the LEs of starting fragments are greater than those of larger, more elaborated, structures. Fit quality scores, however, tend to improve upon optimization of the fragments.

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Lead- and drug-like compounds: the rule-of-five revolution
Lipinski, C. A. (2004) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2004.11.007 · Cited by 6,455
Discovering High-Affinity Ligands for Proteins: SAR by NMR
Shuker, S. B., Hajduk, P. J., Meadows, R. P., & Fesik, S. W. (1996) · Science · doi:10.1126/science.274.5292.1531 · Cited by 2,045
Ligand efficiency: a useful metric for lead selection
Hopkins, A. L., Groom, C. R., & Alex, A. (2004) · Drug Discovery Today · doi:10.1016/s1359-6446(04)03069-7 · Cited by 1,895
Avidin
Green, N. M. (1975) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60411-8 · Cited by 1,472
A decade of fragment-based drug design: strategic advances and lessons learned
Hajduk, P., & Greer, J. (2007) · Nature reviews. Drug discovery · doi:10.1038/nrd2220 · Cited by 1,004
On the attribution and additivity of binding energies
Jencks, W. P. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.7.4046 · Cited by 938
Molecular Complexity and Its Impact on the Probability of Finding Leads for Drug Discovery
Hann, M. M., Leach, A. R., & Harper, G. (2001) · Journal of Chemical Information and Computer Sciences · doi:10.1021/ci000403i · Cited by 904
The maximal affinity of ligands
Kuntz, I. D., Chen, K., Sharp, K. A., & Kollman, P. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.9997 · Cited by 859
Fragment-based lead discovery
Rees, D. C., Congreve, M., Murray, C. W., & Carr, R. A. E. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1467 · Cited by 812
Fragment-Based Drug Discovery
Erlanson, D. A., McDowell, R. S., & O'Brien, T. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm040031v · Cited by 645

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HsuMohane, J. T. A., & Coumar, S. (2015)
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Authors: Bembenek, S. D., Tounge, B. A., & Reynolds, C. H.
Affiliations: Janssen Research & Development (United States) (US)
Corresponding author: Bembenek, Scott D.
ORCID: Bembenek, Scott D.
Reynolds, Charles H.
Venue: Drug Discovery Today
Publisher: Elsevier BV
Published: 2009-03
Volume: 14
Issue: 5-6
Pages: 278-283
ISSN: 1359-6446 (ISSN-L)
DOI: 10.1016/j.drudis.2008.11.007
OpenAlex: W2086070714
Cited by: 196
References: 23
Citations by year: 2026: 8 · 2025: 7 · 2024: 8 · 2023: 6 · 2022: 4 · 2021: 13 · 2020: 2 · 2019: 12 · 2018: 8 · 2017: 10 · 2016: 12 · 2015: 13 · 2014: 15 · 2013: 15 · 2012: 19
FWCI: 21.88
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Drug Discovery Today (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Drug Discovery › Computational Drug Discovery Methods
Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords: ligand efficiency, fragment-based drug discovery, molecular weight, fragment optimization, hit-to-lead optimization, molecular size dependence
MeSH terms: Humans, Ligands, Molecular Weight, Protein Binding, Drug Delivery Systems, Small Molecule Libraries, Drug Discovery

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Ligand efficiency and fragment-based drug discovery

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