Asset Details
Do you wish to reserve the book?
In Vitro and In Vivo Antimalarial Activity of LZ1, a Peptide Derived from Snake Cathelicidin
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
In Vitro and In Vivo Antimalarial Activity of LZ1, a Peptide Derived from Snake Cathelicidin
Do you wish to request the book?
In Vitro and In Vivo Antimalarial Activity of LZ1, a Peptide Derived from Snake Cathelicidin
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
In Vitro and In Vivo Antimalarial Activity of LZ1, a Peptide Derived from Snake Cathelicidin
2019
Overview
Antimalarial drug resistance is an enormous global threat. Recently, antimicrobial peptides (AMPs) are emerging as a new source of antimalarials. In this study, an AMP LZ1 derived from snake cathelicidin was identified with antimalarial activity. In the in vitro antiplasmodial assay, LZ1 showed strong suppression of blood stage Plasmodium falciparum (P. falciparum) with an IC50 value of 3.045 μM. In the in vivo antiplasmodial assay, LZ1 exerted a significant antimalarial activity against Plasmodium berghei (P. berghei) in a dose- and a time- dependent manner. In addition, LZ1 exhibited anti-inflammatory effects and attenuated liver-function impairment during P. berghei infection. Furthermore, by employing inhibitors against glycolysis and oxidative phosphorylation in erythrocytes, LZ1 specifically inhibited adenosine triphosphate (ATP) production in parasite-infected erythrocyte by selectively inhibiting the pyruvate kinase activity. In conclusion, the present study demonstrates that LZ1 is a potential candidate for novel antimalarials development.
Publisher
MDPI AG,MDPI
Subject
/ Adenosine Triphosphate - metabolism
/ Alanine Transaminase - metabolism
/ Animals
/ Antiinfectives and antibacterials
/ Antimalarials - pharmacology
/ Antimalarials - therapeutic use
/ Antimicrobial Cationic Peptides - chemistry
/ Antimicrobial Cationic Peptides - pharmacology
/ Antimicrobial Cationic Peptides - therapeutic use
/ Aspartate Aminotransferases - metabolism
/ ATP
/ cytokine
/ Kinases
/ Liver
/ Malaria
/ Male
/ Mice
/ Peptides
/ Plasmodium falciparum - drug effects
/ Plasmodium falciparum - growth & development
/ Pyruvate Kinase - metabolism
/ Snakes
We currently cannot retrieve any items related to this title. Kindly check back at a later time.