Chymotrypsinogen / chemistry Cold Temperature Fluorescence Neutron Diffraction Pressure Protein Conformation Protein Folding Protein Stability Scattering, Small Angle Thermodynamics
conformational stability fluorescence spectroscopy folding in situ approaches pressure protein denaturation small-angle neutron scattering subzero temperature

Journal

Molecular pharmaceutics
ISSN: 1543-8392
Titre abrégé: Mol Pharm
Pays: United States
ID NLM: 101197791

Informations de publication

Date de publication:
06 12 2021
Historique:
pubmed: 27 10 2021
medline: 15 3 2022
entrez: 26 10 2021
Statut: ppublish

Résumé

Biopharmaceutical formulations may be compromised by freezing, which has been attributed to protein conformational changes at a low temperature, and adsorption to ice-liquid interfaces. However, direct measurements of unfolding/conformational changes in sub-0 °C environments are limited because at ambient pressure, freezing of water can occur, which limits the applicability of otherwise commonly used analytical techniques without specifically tailored instrumentation. In this report, small-angle neutron scattering (SANS) and intrinsic fluorescence (FL) were used to provide

Identifiants

DOI: 10.1021/acs.molpharmaceut.1c00604 PMID: 34699230
pubmed: 34699230
doi: 10.1021/acs.molpharmaceut.1c00604
doi:

Substances chimiques

Chymotrypsinogen 9035-75-0

Types de publication

Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

4415-4427

Auteurs

Diana C Gomes (DC)

Centro de Química Estrutural, Departamento de Engenharia Química, Instituto Superior Técnico, Universidade de Lisboa, Av. Rovisco Pais, 1049-001 Lisboa, Portugal.
Department of Chemical and Biomolecular Engineering, University of Delaware, 590 Avenue 1743, Newark, Delaware 19713, United States.

Susana C M Teixeira (SCM)

Department of Chemical and Biomolecular Engineering, University of Delaware, 590 Avenue 1743, Newark, Delaware 19713, United States.
NIST Center for Neutron Research, National Institute of Standards and Technology, 100 Bureau Drive, Gaithersburg, Maryland 20899, United States.

Juscelino B Leão (JB)

NIST Center for Neutron Research, National Institute of Standards and Technology, 100 Bureau Drive, Gaithersburg, Maryland 20899, United States.

Vladimir I Razinkov (VI)

Drug Product Development, Amgen Inc., Thousand Oaks, California 91320, United States.

Wei Qi (W)

Drug Product Development, Amgen Inc., Thousand Oaks, California 91320, United States.

Miguel A Rodrigues (MA)

Centro de Química Estrutural, Departamento de Engenharia Química, Instituto Superior Técnico, Universidade de Lisboa, Av. Rovisco Pais, 1049-001 Lisboa, Portugal.

Christopher J Roberts (CJ)

Department of Chemical and Biomolecular Engineering, University of Delaware, 590 Avenue 1743, Newark, Delaware 19713, United States.
ORCID: 0000-0001-9978-2767

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Précurseurs de protéines › Proenzymes › Chymotrypsinogène ›
questionsmedicales.fr › Environnement et santé publique › Environnement › Concepts météorologiques › Atmosphère › Temps (météorologie) › Température › Basse température ›
questionsmedicales.fr › Phénomènes physiques › Phénomènes optiques › Fluorescence ›
questionsmedicales.fr › Phénomènes chimiques › Diffraction de neutrons ›
questionsmedicales.fr › Phénomènes physiques › Phénomènes mécaniques › Pression ›
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines ›
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Pliage des protéines ›
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Stabilité protéique ›
questionsmedicales.fr › Phénomènes physiques › Diffusion de rayonnements › Diffusion aux petits angles ›
questionsmedicales.fr › Phénomènes physiques › Thermodynamique ›