We have located links that may give you full text access.
In Vivo ; In Vitro Interaction of Silver Nanoparticles with Leucine Aminopeptidase from Human and Plasmodium falciparum .
Journal of Nanoscience and Nanotechnology 2018 Februrary 2
There is increasing requirement for the development of new drug protocols against malaria, a fatal disease caused by the lethal parasite Plasmodium falciparum. Leucine aminopeptidase (Pf LAP) of Plasmodium falciparum, is being pursued as a promising target for the discovery of novel antimalarials. The effects of silver nanoparticles (AgNPs) against P. falciparum leucine amino-peptidase (Pf LAP) and the human homolog (HsLAP) were compared. Pf LAP and HsLAP were expressed in Escherichia coli, and AgNPs (3-10 nm) characterized by ultra-violet spectroscopy and transmission electron microscopy. Pf LAP indicated a Km of 694 μM towards leucine-p-nitroanilide and a Vmax of 57.9 μmol.ml-1 · min-1 while HsLAP had a Km of 1.6 mM and Vmax of 119.6 μmol · ml-1 · min-1. On interaction with AgNPs (670 nM) Pf LAP was selectively inhibited (57.1%; Ki = 610 nM) relative to HsLAP (10.8%; Ki = 5.22 μM). Structural differences between the enzyme variants, particularly the orientation and distance of surface Met349 in Pf LAP and Met306 in HsLAP to the zinc binding sites were significant and may allow for selective targeting of Pf LAP by AgNPs. The viability of P. falciparum parasites was decreased when exposed to silver nanoparticles, with an IC50 value of 6.96 μM, compared to an IC50 value of 647.7 μM for human HeLa cells.
Full text links
Related Resources
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app
All material on this website is protected by copyright, Copyright © 1994-2024 by WebMD LLC.
This website also contains material copyrighted by 3rd parties.
By using this service, you agree to our terms of use and privacy policy.
Your Privacy Choices
You can now claim free CME credits for this literature searchClaim now
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app