Protein/ice Interaction: High-Resolution Synchrotron X-Ray Diffraction Differentiates Pharmaceutical Proteins From Lysozyme | Sciact - CRIS-система Института катализа

Protein/ice Interaction: High-Resolution Synchrotron X-Ray Diffraction Differentiates Pharmaceutical Proteins From Lysozyme Научная публикация

Журнал

The Journal of Physical Chemistry B
ISSN: 1520-6106 , E-ISSN: 1520-5207

Вых. Данные

Год: 2019, Том: 123, Номер: 27, Страницы: 5690-5699 Страниц : 10 DOI: 10.1021/acs.jpcb.9b02443

Ключевые слова

Crystalline materials Enzymes Ice Monoclonal antibodies X ray diffraction

Авторы

Bhatnagar Bakul ¹ , Zakharov Boris ^2,3 , Fisyuk Alexander ^4,5 , Wen Xin ⁶ , Karim Fawziya ¹ , Lee Kimberly ⁶ , Seryotkin Yurii ^3,7 , Mogodi Mashikoane ⁸ , Fitch Andy ⁸ , Boldyreva Elena ^2,3 , Kostyuchenko Anastasia ⁵ , Shalaev Evgenyi ⁹

Организации

1	BTx PharmSci Pharmaceutical R&D, Pfizer, Inc.
2	Boreskov Institute of Catalysis SB RAS
3	Novosibirsk State University
4	Laboratory of Organic Synthesis, Chemistry Department, Omsk F.M. Dostoevsky State University
5	Laboratory of New Organic Materials, Omsk State Technical University
6	Department of Chemistry and Biochemistry, California State University, Los Angeles
7	Sobolev Institute of Geology and Mineralogy, Siberian Branch of the RAS
8	The European Synchrotron Radiation Facility (ESRF)
9	Allergan Inc., Pharmaceutical Development

Информация о финансировании (5)

1	Министерство науки и высшего образования Российской Федерации (с 15 мая 2018)	0239-2019-0003
2	European Synchrotron Radiation Facility	LS-2601
3	European Synchrotron Radiation Facility	LS-2742
4	National Institutes of Health	SC3GM086249
5	National Science Foundation	1644917

Protein/ice interactions are investigated by a novel method based on measuring the characteristic features of X-ray diffraction (XRD) patterns of hexagonal ice (Ih). Aqueous solutions of four proteins and other solutes are studied using high-resolution synchrotron XRD. Two pharmaceutical proteins, recombinant human albumin and monoclonal antibody (both at 100 mg/mL), have a pronounced effect on the properties of ice crystals, reducing the size of the Ih crystalline domains and increasing the microstrain. Lysozyme (100 mg/mL) and an antifreeze protein (1 mg/mL) have much weaker impact on Ih. Neither of the proteins studied exhibit preferred interactions with specific crystalline faces of Ih. It is proposed that the pharmaceutical proteins interact with ice crystals indirectly by accumulating in the quasi-liquid layer next to ice crystallization front, rather than directly, via a sorption on ice crystals. This is the first report, to the best of our knowledge, of major difference in the protein/ice interaction between non-antifreeze proteins. Another important finding is a detection of a second (minor) population of ice crystals, which is tentatively identified as a high-pressure form of ice, possibly IceIII or IceIX. This finding highlights a potential role of mechanical stresses in freeze-induced destabilization of proteins.

Bhatnagar B. , Zakharov B. , Fisyuk A. , Wen X. , Karim F. , Lee K. , Seryotkin Y. , Mogodi M. , Fitch A. , Boldyreva E. , Kostyuchenko A. , Shalaev E.
Protein/ice Interaction: High-Resolution Synchrotron X-Ray Diffraction Differentiates Pharmaceutical Proteins From Lysozyme
The Journal of Physical Chemistry B. 2019. V.123. N27. P.5690-5699. DOI: 10.1021/acs.jpcb.9b02443 WOS Scopus РИНЦ CAPlusCA PMID OpenAlex

Поступила в редакцию:	14 мар. 2019 г.
Принята к публикации:	11 июн. 2019 г.
Опубликована online:	17 июн. 2019 г.
Опубликована в печати:	11 июл. 2019 г.

Web of science:	WOS:000475540400003
Scopus:	2-s2.0-85069627446
РИНЦ:	41633050
Chemical Abstracts:	2019:1180275
Chemical Abstracts (print):	171:148513
PMID (PubMed):	31260313
OpenAlex:	W2953387380

БД	Цитирований
Web of science	24
Scopus	27
РИНЦ	26
OpenAlex	29