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Paper Details

MOLECULAR DOCKING AND MUTATIONAL STUDIES OF HUMAN SURFACTANT PROTEIN D

Lubna Nousheen, Akkiraju PavanChand, Sreenivas Enaganti

Journal Title:World Journal of Pharmaceutical Research
Abstract


Surfactant protein-D (SP-D) is C-type lectin which is synthesized in various parts of the body, SP-D play a key role in the auto immune disorders and lung infections and also helpful in the postnatal pregnancy these also plays an active role in the host-defense mechanisms. In the host defense mechanism SP-D binds with various micro-organisms and other particles that enter the human body and act against the microorganisms. In our present study we targeted on the interactions of surfactant protein D with the lipid molecules where their interaction plays an important role in the defense mechanism. In our study lipid molecules were docked against the SP-D protein and interaction studies were carried-out. We have generated mutations at sites F335G and R343V and interactions of the lipids with the mutated protein molecules was studied. Among the wild and the mutant protein molecules mutant protein F335G showed highest interaction with the lipid molecule distearoylphosphatidylcholine with a CDocker energy of 94.726. These studied showed that mutant molecules are showing highest binding with the lipid molecules when compared to the wild protein molecule. Among all ligand molecules chosen distearoylphosphatidylcholine showed highest interaction followed by dilaurylphosphatidylcholine, dipalmitoylphosphatidylcholine and tocopherol showed the least binding affinity with both wild and the mutant protein molecules.

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