Carbonic Anhydrase as Drug Target Thermodynamics and Structure of Inhibitor Binding /

• Corporate Author: SpringerLink (Online service)
• Other Authors: Matulis, Daumantas (Editor, http://id.loc.gov/vocabulary/relators/edt)
• Format: Electronic eBook
• Language: English
• Published: Cham : Springer International Publishing : Imprint: Springer, 2019.
• Edition: 1st ed. 2019.
• Subjects: Molecular biology.; Medical biochemistry.; Proteins .; Medicinal chemistry.; Pharmaceutical technology.; Molecular Medicine.; Medical Biochemistry.; Protein-Ligand Interactions.; Medicinal Chemistry.; Pharmaceutical Sciences/Technology.

This book offers deep insights into the thermodynamics and molecular structures of the twelve catalytically active isoforms of human carbonic anhydrase (CA) with a particular focus on inhibitor binding for drug design. X-ray crystallographic structures in combination with enzyme kinetic testing prov...

Table of Contents:

• Final ToC tbd. 1) Description of human carbonic anhydrases (12 catalytically active human isoforms; isoforms as drug targets, enzymatic activity, catalytic mechanism, thermodynamics of protonation of the water molecule in the active site)
• 2) Thermal stabilities of all isoform CA catalytic domains
• Thermodynamics of inhibitor binding to CAs (incl. intrinsic thermodynamics - not mentioned important subject in most CA literature)
• 3) Comparison of methods to determine inhibitor binding to CAs (ITC, FTSA, enzymatic activity assays)
• 4) Chemical synthesis of CA inhibitors
• 5) X-ray crystallographic structures of CAs and their complexes with inhibitors
• 6) Antibodies against CAs.