Publication:
Near-physiological-temperature serial crystallography reveals conformations of SARS-CoV-2 main protease active site for improved drug repurposing

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SCHOOL OF NURSING
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Durdağı, Serdar
Doğan, Berna
Avşar, Timuçin
Erol, İsmail
Çalış, Şeyma
Orhan, Müge D.
Aksoydan, Busecan
Şahin, Kader
Oktay, Lalehan
Tolu, İlayda

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The COVID-19 pandemic has resulted in 198 million reported infections and more than 4 million deaths as of July 2021 (covid19.who.int). Research to identify effective therapies for COVID-19 includes: (1) designing a vaccine as future protection; (2) de novo drug discovery; and (3) identifying existing drugs to repurpose them as effective and immediate treatments. To assist in drug repurposing and design, we determine two apo structures of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) main protease at ambient temperature by serial femtosecond X-ray crystallography. We employ detailed molecular simulations of selected known main protease inhibitors with the structures and compare binding modes and energies. The combined structural and molecular modeling studies not only reveal the dynamics of small molecules targeting the main protease but also provide invaluable opportunities for drug repurposing and structure-based drug design strategies against SARS-CoV-2.

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Elsevier

Subject

Biochemistry and molecular biology, Biophysics, Cell biology

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DOI

10.1016/j.str.2021.07.007

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