In silico characterization of human-malarial parasite species based on their DHFR and GST targets leading to a change in binding conformations of anti-malarial drugs

In this study, we mainly focused on three anti-malarial drugs which were analyzed against the two malarial targets. Chloroquine, Mefloquine and, Proguanil was chosen as anti-malarial drugs while DHFR and GST targets from human malarial parasites like Plasmodium falciparum, Plasmodium malariae, Plasmodium ovale, and Plasmodium vivax were considered for the study. This study was conducted to understand the sequence and structural similarity between protein DHFR and GST among four Plasmodium species as well as to find out there in silico interactions with above-stated drug candidates. There were many bioinformatics databases, tools, and software’s were run to bring out research. Our data showed not many structural differences between Plasmodium sequences but yet other characteristics of them that make them different from each other. Hence that variation has shown a difference in the binding patterns of drugs with target proteins.

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In silico characterization of human-malarial parasite species based on their DHFR and GST targets leading to a change in binding conformations of anti-malarial drugs

International Journal of Research in Pharmaceutical Sciences ◽

10.26452/ijrps.v11i4.4183 ◽

2020 ◽

Vol 11 (4) ◽

pp. 7958-7972

Author(s):

Shrutika Sakpal ◽

Alpana Bastikar ◽

Shanker Lal Kothari ◽

Virupaksha Bastikar

Keyword(s):

In Silico ◽

Plasmodium Species ◽

Structural Similarity ◽

Plasmodium Malariae ◽

Malarial Parasite ◽

Drug Candidates ◽

Structural Differences ◽

Bioinformatics Databases ◽

In Silico Characterization

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IN VITRO/IN SILICO CHARACTERIZATION OF ACTIVE AND PASSIVE STRESSES IN CARDIAC MUSCLE

International Journal for Multiscale Computational Engineering ◽

10.1615/intjmultcompeng.2011002352 ◽

2012 ◽

Vol 10 (2) ◽

pp. 171-188 ◽

Cited By ~ 7

Author(s):

Markus Boel ◽

Oscar J. Abilez ◽

Ahmed N Assar ◽

Christopher K. Zarins ◽

Ellen Kuhl

Keyword(s):

Cardiac Muscle ◽

In Silico ◽

In Silico Characterization

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In-Vitro and In-Silico Characterization of Xylose Reductase from Emericella nidulans

Current Chemical Biology ◽

10.2174/2212796812666180622103906 ◽

2019 ◽

Vol 13 (2) ◽

pp. 159-170 ◽

Cited By ~ 1

Author(s):

Vishal Ahuja ◽

Aashima Sharma ◽

Ranju Kumari Rathour ◽

Vaishali Sharma ◽

Nidhi Rana ◽

...

Keyword(s):

Production Process ◽

In Silico ◽

Xylose Reductase ◽

In Silico Analysis ◽

Emericella Nidulans ◽

Higher Temperature ◽

In Silico Characterization ◽

Silico Analysis

Background: Lignocellulosic residues generated by various anthropogenic activities can be a potential raw material for many commercial products such as biofuels, organic acids and nutraceuticals including xylitol. Xylitol is a low-calorie nutritive sweetener for diabetic patients. Microbial production of xylitol can be helpful in overcoming the drawbacks of traditional chemical production process and lowring cost of production. Objective: Designing efficient production process needs the characterization of required enzyme/s. Hence current work was focused on in-vitro and in-silico characterization of xylose reductase from Emericella nidulans. Methods: Xylose reductase from one of the hyper-producer isolates, Emericella nidulans Xlt-11 was used for in-vitro characterization. For in-silico characterization, XR sequence (Accession No: Q5BGA7) was used. Results: Xylose reductase from various microorganisms has been studied but the quest for better enzymes, their stability at higher temperature and pH still continues. Xylose reductase from Emericella nidulans Xlt-11 was found NADH dependent and utilizes xylose as its sole substrate for xylitol production. In comparison to whole cells, enzyme exhibited higher enzyme activity at lower cofactor concentration and could tolerate higher substrate concentration. Thermal deactivation profile showed that whole cell catalysts were more stable than enzyme at higher temperature. In-silico analysis of XR sequence from Emericella nidulans (Accession No: Q5BGA7) suggested that the structure was dominated by random coiling. Enzyme sequences have conserved active site with net negative charge and PI value in acidic pH range. Conclusion: Current investigation supported the enzyme’s specific application i.e. bioconversion of xylose to xylitol due to its higher selectivity. In-silico analysis may provide significant structural and physiological information for modifications and improved stability.

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