Recommended

Register now: Enhancing biopharma workflows with the power of UV/Vis spectroscopy webinar
Register now: Managing the complexities of NDSRI method development: The N-nitroso propranolol case story
Learn more about leveraging real-world data, the practical applications of AI and adopting configurable LC/NC solutions.
Download this compendium to discover how hot-melt extrusion can help to overcome pharmaceutical formulation challenges
Join this webinar to hear about the latest RMM technology and how it aligns with USP testing criteria.
Join now: Pharmaceutical continuous manufacturing: what’s next for industry?

List view / Grid view

Search results for Freire - 11 results

 

DSC image
DSC image
article

Can calorimetry provide accurate estimates of long‑term stability for monoclonal antibodies?

3 September 2019 | By

Differential scanning calorimetry (DSC) has been one of the most widely used techniques to characterise the temperature stability of monoclonal antibodies (mAbs) and provide important information in formulation optimisation. However, despite its widespread use, not all the information contained in DSC data, especially denaturation kinetics, is routinely extracted. In this…

A new era for microcalorimetry in drug development
article

A new era for microcalorimetry in drug development

21 September 2007 | By Dr Ernesto Freire, Faculty Professor, Johns Hopkins University, Baltimore

Drug development involves the identification and subsequent optimisation of low molecular weight compounds with a desired biological activity. Often, the initial binding affinity of those compounds towards their intended target needs to be improved by five or more orders of magnitude before they become viable drug candidates; a process that…

ITC: affinity is not everything
article

ITC: affinity is not everything

7 February 2009 | By

During the optimisation of drug candidates, improvements in affinity and selectivity play a critical role. This task is usually accomplished by establishing accurate correlations between the affinity/selectivity of different chemical scaffolds and through chemical modifications to a selected scaffold.

Enthalpic efficiency and the role of thermodynamic data in drug development: possibility or a pipeline dream!
article

Enthalpic efficiency and the role of thermodynamic data in drug development: possibility or a pipeline dream!

23 November 2007 | By

The determination of accurate thermodynamic data for the interactions of biomolecules has been enhanced over the last decade by the use of isothermal titration calorimetric (ITC) instrumentation. These instruments are now standard kits in many biophysical/structural biochemistry laboratories of pharmaceutical companies. Despite this, there is little evidence for the input…

Figure 1 Free energy diagram for a single step binding interaction between protein (P) and ligand (L). For a binding reaction of this type increasing affinity is achieved by lowering the free energy of the PL complex. Increasing residence (decreasing koff) time is achieved by lowering the free energy of the PL complex and/or destabilizing the transition state
Figure 1 Free energy diagram for a single step binding interaction between protein (P) and ligand (L). For a binding reaction of this type increasing affinity is achieved by lowering the free energy of the PL complex. Increasing residence (decreasing koff) time is achieved by lowering the free energy of the PL complex and/or destabilizing the transition state
article

Thermodynamics and kinetics driving quality in drug discovery

31 August 2011 | By Geoff Holdgate, AstraZeneca

Recently, there has been renewed interest in using thermodynamic and kinetic data, alongside empirical rules (particularly focused upon cLogP and molecular weight) and guiding metrics such as ligand efficiency and lipophilic ligand efficiency developed for fragments, leads and drugs in order to facilitate the design of compounds with a greater…

Figure 1 Comparison of ITC and TSA data for lead compound 3b binding to the N-terminal domain of Hsp90 target protein4. Left panels show ITC data, right panels – TSA data. Upper panels (a) and (c) show raw data while lower panels show the dosing curves
Figure 1 Comparison of ITC and TSA data for lead compound 3b binding to the N-terminal domain of Hsp90 target protein4. Left panels show ITC data, right panels – TSA data. Upper panels (a) and (c) show raw data while lower panels show the dosing curves
article

Isothermal titration calorimetry and thermal shift assay in drug design

20 June 2011 | By Asta Zubrienė, Egidijus Kazlauskas, Lina Baranauskienė, Vytautas Petrauskas and Daumantas Matulis, Department of Biothermodynamics and Drug Design, Vilnius University Institute of Biotechnology

Isothermal titration calorimetry (ITC) is a method of choice in the pharmaceutical industry for determination of equilibrium binding enthalpy, entropy, and the Gibbs free energy. The method is very powerful for determination of intrinsic binding parameters that could be used in structure-energetics correlations. Here we discuss how to overcome several…