Nuclear export of viral mRNAs, is an essential step in the HIV replication cycle. This role is played by a small regulatory protein of HIV-1 called Rev.The N-terminal region of Rev contains an arginine-rich sequence. The arginine-rich motif (ARM) is located between amino acids 38-50 and forms an alpha-helical secondary structure. Expression of the structural proteins of human immunodeficiency virus type 1 requires the direct interaction of multiple copies of the viral Rev protein with its highly structured RNA target sequence, the Rev Response element (RRE). The major viral proteins are not produced if this transport of RNA is stopped. Therefore, knowledge of Rev structure is essential for understanding of its cooperative binding to the RRE, for understanding the mechanism of HIV infection and for the development of antiviral drugs that interfere with Rev’s essential functions and for acknowledgment of good candidate drugs for treatment of AIDS. To understand how REV interact with RRE element of HIV-RNA and its formation of oligomeric complex it is better to characterize the domain wise structure of REV with regard in function of each domain. Due to lack of structural data on Rev no single compound is reported as inhibitor of REV expect antiviral drugs. Identification of a high-affinity RNA-binding site for the human immunodeficiency virus type 1 Rev Protein is much more important. The ARM is a highly specific sequence which allows for the multimerization of Rev and also binding of REV with RNA. Here we are first time exploring the structural characteristics of REV protein both in free form and in complex with RNA at domain function level especially explore the role of ARM motif in REV HIV-1 protein as RNA binding sites by molecular dynamics (MD) simulation and homology modeling studies. Results indicate that the arginine-rich motif (ARM) is crucial in stability of this complex. The residues ARG38, 39, 41, 43, 44, 48, 50, and ASN40 are most interacting with nucleobases of RRE in Crystal structure of Rev and Rev-response-element RNA complex. Our study plays a major role in elaboration of binding of RNA with REV and pave the way for further investigation for therapeutically agent for HIV.

Due to their wide range of uses in modern technology, nanomaterial’s of silver metallic (Ag-NPs) have engaged considerable concern, driving significant research with development efforts. This study focuses on investigating the antimicrobial properties of Ag-NPs, encompassing their production, characterization, and biological aspects. The eco-friendly extracellular biosynthetic method employed in this work utilized extracts from the marine fungus Aspergillus flavus MK4 as reducing agents for nanoparticle synthesis. Analyzing the colloidal Ag-NPs using UV-visible spectroscopy revealed a peak in absorbance at 460 nm, indicating the presence of plasmonic properties. The electrons imaging of internal structure (TEM) elucidated spherical shape of the Ag-NPs by 15 nm size. Testing against bacterial diversities (Gr-ve & Gr+ve) revealed potent antibacterial and antifungal efficacy. Cytotoxicity versus HepG-2 cell line was assessed using the MTT assay, and antioxidant properties were examined through the radical scavenging (DPPH) assay. In wise of their conceivable applications in the fields of antibacterial, anticancer, and wound-healing, the Ag-NPs that were synthesized exhibit promising features. With its powerful ability to synthesize silver nanoparticles (Ag-NP), Aspergillus flavus MK4 Aspergillus flavus MK4 can generate nanoparticles extensively characterized, demonstrating their antibacterial, antioxidant, anticancer, and wound-healing properties.