Department of Research in Biotechnology and Allied Sciences, Ashok and Rita Patel Institute of Integrated Study, India
*Corresponding author: Pinakin Dhandhukia, Ashok and Rita Patel Institute of Integrated Study and Research in Biotechnology and Allied Sciences (ARIBAS), New Vidhyanagar -388121, Gujarat, India, Email: email@example.com
Submission: August 10, 2017; Published: January 03, 2018
ISSN: 2576-9170Volume1 Issue4
The invasion of Plasmodium in RBC is the most important pathogenic step. Further proliferation is stopped if any drug or antibody can inhibit at this stage. Among two major invasive surface proteins PfRH5 and AMA-1, only multiple AMA-1 structures viz. 3ZWZ, 2Q8B, 2Z8V, 3SRJ are available at time of study which was selected to obtain information about the common ligand-bound interface residues. Three active sites were created and the amino acid properties provided information that some of these are polymorphic and some are hydrophobic and conserved. Docking was done using the ZINC library on the Web server. Interactions of H-bond of the crystal structure and docking results revealed that ASN223 and ILE225 amino acids were the common H-linkage formation in all structure. ILE225 is a polymorph that cannot be considered as an interaction, whereas ASN223 is a very important polar interacting residue. However, from the docking results, only the compounds interacting with ASN223 were analyzed. ZINC80342995 and ZINC95042198 have been selected as active compounds. Both have properties in the range of the ideal drug according to ADME/T properties. However, in vitro analysis will be needed to analyze the actual potential of these candidates to prevent invasion.
Keywords: Malaria; Drug design; Invasion inhibition