Corrections to “Banks DD, Latypov RF, Ketchem RR, Woodard J, Scavezze JL, Siska CC, Razinkov VI. 2012. Native-State Solubility and Transfer Free Energy as Predictive Tools for Selecting Excipients to Include in Protein Formulation Development Studies. J Pharm Sci 101:2720-2732.”

2013 ◽  
Vol 102 (3) ◽  
pp. 1137-1138 ◽  
Author(s):  
Douglas D. Banks ◽  
Ramil F. Latypov ◽  
Randal R. Ketchem ◽  
Jon Woodard ◽  
Joanna L. Scavezze ◽  
...  
Keyword(s):  
Free Energy ◽  
Protein Formulation ◽  
Development Studies ◽  
Formulation Development ◽  
Native State ◽  
Transfer Free Energy ◽  
Predictive Tools

Native-State Solubility and Transfer Free Energy as Predictive Tools for Selecting Excipients to Include in Protein Formulation Development Studies

2012 ◽  
Vol 101 (8) ◽  
pp. 2720-2732 ◽  
Author(s):  
Douglas D. Banks ◽  
Ramil F. Latypov ◽  
Randal R. Ketchem ◽  
Jon Woodard ◽  
Joanna L. Scavezze ◽  
...  
Keyword(s):  
Free Energy ◽  
Protein Formulation ◽  
Development Studies ◽  
Formulation Development ◽  
Native State ◽  
Transfer Free Energy ◽  
Predictive Tools

Transfer Free Energy of Micro-hydrated Ion Clusters from Water into Acetonitrile Solvent

2021 ◽  
pp. 116561
Author(s):  
Weiqiang Tang ◽  
Zijiang Dou ◽  
Yu Li ◽  
Xiaofei Xu ◽  
Shuangliang Zhao
Keyword(s):  
Free Energy ◽  
Transfer Free Energy ◽  
Ion Clusters ◽  
Hydrated Ion

scholarly journals Improved Fluorescence Methods for High-Throughput Protein Formulation Screening

2018 ◽  
Vol 23 (6) ◽  
pp. 516-528 ◽  
Author(s):  
Yangjie Wei ◽  
Nicholas R. Larson ◽  
Siva K. Angalakurthi ◽  
C. Russell Middaugh
Keyword(s):  
Steady State ◽  
High Throughput ◽  
Protein Formulation ◽  
Formulation Development ◽  
High Concentration ◽  
Direct Optimization ◽  
Biophysical Characterization ◽  
Formulation Optimization ◽  
Long Term Storage ◽  
High Protein Concentration

The goal of protein formulation development is to identify optimal conditions for long-term storage. Certain commercial conditions (e.g., high protein concentration or turbid adjuvanted samples) impart additional challenges to biophysical characterization. Formulation screening studies for such conditions are usually performed using a simplified format in which the target protein is studied at a low concentration in a clear solution. The failure of study conditions to model the actual formulation environment may cause a loss of ability to identify the optimal condition for target proteins in their final commercial formulations. In this study, we utilized a steady-state/lifetime fluorescence-based, high-throughput platform to develop a general workflow for direct formulation optimization under analytically challenging but commercially relevant conditions. A high-concentration monoclonal antibody (mAb) and an Alhydrogel-adjuvanted antigen were investigated. A large discrepancy in screening results was observed for both proteins under these two different conditions (simplified and commercially relevant). This study demonstrates the feasibility of using a steady-state/lifetime fluorescence plate reader for direct optimization of challenging formulation conditions and highlights the importance of performing formulation optimization under commercially relevant conditions.

scholarly journals Polymorphism at 129 dictates metastable conformations of the human prion protein N-terminal β-sheet

2017 ◽  
Vol 8 (2) ◽  
pp. 1225-1232 ◽  
Author(s):  
S. Alexis Paz ◽  
Eric Vanden-Eijnden ◽  
Cameron F. Abrams
Keyword(s):  
Free Energy ◽  
Prion Protein ◽  
Thermodynamic Stability ◽  
Energy Method ◽  
Replica Exchange ◽  
Native State ◽  
Human Prion Protein ◽  
Β Sheet

We study the thermodynamic stability of the native state of the human prion protein using a new free-energy method, replica-exchange on-the-fly parameterization.

Hydrogen exchange and structural dynamics of proteins and nucleic acids

1983 ◽  
Vol 16 (4) ◽  
pp. 521-655 ◽  
Author(s):  
S. Walter Englander ◽  
Neville R. Kallenbach
Keyword(s):  
Free Energy ◽  
Nucleic Acids ◽  
Structural Dynamics ◽  
Hydrogen Exchange ◽  
Native State ◽  
Structural Work

Though the structures presented in crystallographic models of macromolecules appear to possess rock-like solidity, real proteins and nucleic acids are not particularly rigid. Most structural work to date has centred upon the native state of macromolecules, the most probable macromolecular form. But the native state of a molecule is merely its most abundant form, certainly not its only form. Thermodynamics requires that all other possible structural forms, however improbable, must also exist, albeit with representation corresponding to the factor exp( — Gi/RT) for each state of free energy Gi (see Moelwyn-Hughes, 1961), and one appreciates that each molecule within a population of molecules will in time explore the vast ensemble of possible structural states.

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