Ice Recrystallization in a Solution of a Cryoprotector and Its Inhibition by a Protein: Synchrotron X-Ray Diffraction Study | Sciact - CRIS-система Института катализа

Ice Recrystallization in a Solution of a Cryoprotector and Its Inhibition by a Protein: Synchrotron X-Ray Diffraction Study Научная публикация

Журнал

Journal of Pharmaceutical Sciences
ISSN: 0022-3549 , E-ISSN: 1520-6017

Вых. Данные

Год: 2016, Том: 105, Номер: 7, Страницы: 2129-2138 Страниц : 10 DOI: 10.1016/j.xphs.2016.04.020

Ключевые слова

calorimetry (DSC), crystal defects, freeze drying/lyophilization, phase transition, proteins, X-ray powder diffractometry

Авторы

Zakharov Boris ^1,2 , Fisyuk Aleksander ^3,4 , Fitch Andy ⁵ , Watier Yves ⁵ , Kostyuchenko Anastasia ^3,4 , Varshney Dushyant ⁶ , Sztucki Michael ⁵ , Boldyreva Elena ¹ , Shalaev Evgenyi ⁷

Организации

1	Institute of Solid State Chemistry and Mechanochemistry SB RAS, ul. Kutateladze, 18, Novosibirsk 630128, Russian Federation
2	Novosibirsk State University, ul. Pirogova, 2, Novosibirsk 630090, Russian Federation
3	Department of Organic Chemistry, Omsk F. M. Dostoevsky State University, Mira Avenue 55A, Omsk 644077, Russian Federation
4	Laboratory of New Organic Materials, Omsk State Technical University, Mira Avenue 11, Omsk 644050, Russian Federation
5	ESRF—The European Synchrotron Radiation Facility, 71 av des Martyrs, Grenoble 38043, France
6	Novartis Vaccines and Diagnostics, Holly Springs, North Carolina 27540
7	Pharmaceutical R&D, Allergan Inc., Irvine, California 92612

Ice formation and recrystallization is a key phenomenon in freezing and freeze-drying of pharmaceuticals and biopharmaceuticals. In this investigation, high-resolution synchrotron X-ray diffraction is used to quantify the extent of disorder of ice crystals in binary aqueous solutions of a cryoprotectant (sorbitol) and a protein, bovine serum albumin. Ice crystals in more dilute (10 wt%) solutions have lower level of microstrain and larger crystal domain size than these in more concentrated (40 wt%) solutions. Warming the sorbitol–water mixtures from 100 to 228 K resulted in partial ice melting, with simultaneous reduction in the microstrain and increase in crystallite size, that is, recrystallization. In contrast to sorbitol solutions, ice crystals in the BSA solutions preserved both the microstrain and smaller crystallite size on partial melting, demonstrating that BSA inhibits ice recrystallization. The results are consistent with BSA partitioning into quasi-liquid layer on ice crystals but not with a direct protein–ice interaction and protein sorption on ice surface. The study shows for the first time that a common (i.e., not-antifreeze) protein can have a major impact on ice recrystallization and also presents synchrotron X-ray diffraction as a unique tool for quantification of crystallinity and disorder in frozen aqueous systems.

Zakharov B. , Fisyuk A. , Fitch A. , Watier Y. , Kostyuchenko A. , Varshney D. , Sztucki M. , Boldyreva E. , Shalaev E.
Ice Recrystallization in a Solution of a Cryoprotector and Its Inhibition by a Protein: Synchrotron X-Ray Diffraction Study
Journal of Pharmaceutical Sciences. 2016. V.105. N7. P.2129-2138. DOI: 10.1016/j.xphs.2016.04.020 WOS Scopus РИНЦ CAPlusCA OpenAlex

Поступила в редакцию:	30 дек. 2015 г.
Принята к публикации:	11 апр. 2016 г.
Опубликована online:	7 июн. 2016 г.
Опубликована в печати:	1 июл. 2016 г.

Web of science:	WOS:000381770300013
Scopus:	2-s2.0-84975842553
РИНЦ:	27140116
Chemical Abstracts:	2016:1064842
Chemical Abstracts (print):	165:144846
OpenAlex:	W2418386331

БД	Цитирований
Web of science	14
Scopus	20
OpenAlex	22