An efficient strategy to enhance binding affinity and specificity of a known isozyme inhibitor-Reference-Cited by-同舟云学术

An efficient strategy to enhance binding affinity and specificity of a known isozyme inhibitor

Published:2016 Issue:28 Volume:14 Page:6833-6839
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Jee Joo-Eun¹²³,Lim Jaehong¹²³,Ong Yong Siang¹²³,Oon Jessica¹²³,Gao Liqian¹²³,Choi Hak Soo⁴⁵⁶⁷⁸,Lee Su Seong¹²³

Affiliation:

1. Institute of Bioengineering and Nanotechnology

2. Singapore 138669

3. Singapore

4. Gordon Center for Medical Imaging

5. Department of Radiology

6. Massachusetts General Hospital and Harvard Medical School

7. Boston

8. USA

Abstract

The binding profile of a known inhibitor, benzenesulfonamide, against a family of carbonic anhydrase isozymes was efficiently enhanced via high-throughput screening of customized combinatorial one-bead-one-compound peptide libraries.

Funder

National Institutes of Health

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2016/OB/C6OB01104G

Reference41 articles.

1. Carbonic anhydrases: novel therapeutic applications for inhibitors and activators

2. 7-Substituted-sulfocoumarins are isoform-selective, potent carbonic anhydrase II inhibitors

3. 1,3,5-Trisubstituted benzenes as fluorescent photoaffinity probes for human carbonic anhydrase II capture

4. Structural Insights on Carbonic Anhydrase Inhibitory Action, Isoform Selectivity, and Potency of Sulfonamides and Coumarins Incorporating Arylsulfonylureido Groups

5. Multiple Binding Modes of Inhibitors to Carbonic Anhydrases: How to Design Specific Drugs Targeting 15 Different Isoforms?

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