Title
Authors
Hasanain Abdulhameed Odhar
Affiliation
Department of pharmacy, Al-Zahrawi University College, Karbala, Iraq
Hasanain Abdulhameed Odhar - Tel:
009647725300923; Email:
hodhar3@gmail.com; *Corresponding author:
Article Type
Views
Date
Received April 23, 2020; Accepted April 24, 2020; Published May 31, 2020
Abstract
The project for the report Dai et al.
(2020) [1] seems to be well funded and the authors had access to
many modern facilities and techniques. They were able to
successfully design, synthesize and evaluate two lead inhibitors of
SARS-CoV-2 main protease. Interestingly, they were able to
crystallize protease-inhibitor complex to visualize real chemical
interaction involved. According to x-ray diffraction images, they
found that the aldehyde group of synthesized
inhibitors is involved in covalent bond with Mpro active site. We
can appreciate this finding by noting that computational modeling
approaches like docking studies have difficulties in predicting
covalent bonds. The design of these two novel inhibitors may be
considered a continuation for several previous attempts of
structure-based design of coronavirus main protease inhibitors, for
example the well-known peptide inhibitor N3. I am only concerned
about the interaction between lead inhibitors and water molecules in
crystallization images. These water molecules may be active site
reserved water or merely the result of crystallization process. It
would be interesting to prepare several derivatives of these two
lead inhibitors and then establish a structure-activity relationship
study. This seems to be crucial for elucidating the structure of
core scaffold.
Keywords
SARS-CoV-2 main protease
Citation
Odhar, Bioinformation 16(5): 435-437 (2020)
Edited by
P Kangueane
ISSN
0973-2063
Publisher
License
This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.
