Synthetic peptides corresponding to a repetitive sequence of malarial histidine rich protein bind haem and inhibit haemozoin formation in vitro
Publisher DOI
PubMed ID
9497049
Abstract
Synthetic peptides containing a repetitive hexapeptide sequence (Ala-His-His-Ala-Ala-Asp) of malarial histidine-rich protein II were evaluated for binding with haem in vitro. The pattern of haem binding suggested that each repeat unit of this sequence provides one binding site for haem. Chloroquine inhibited the haem-peptide complex formation with preferential formation of a haem chloroquine complex. In vitro studies on haem polymerisation showed that none of the peptides could initiate haemozoin formation. However, they could inhibit haemozoin formation promoted by a malarial parasite extract, possibly by competitively binding free haem. These results indicate this hexapeptide sequence represents the haem binding site of the malarial histidine-rich protein and possibly the site of nucleation for haem polymerisation.
Date Issued
1997-12-01
Publication Type
Article
Subjects
Malaria
•
Haemoglobin
•
Haem
•
Haemozoin
•
Histidine-rich protein
•
Chloroquine
Language(s)
en
Author(s)
Joshi, Ratanmani | |
Tekwani, Babu L. | |
Singh, Ram L. | |
Chauhan, Virender S. |
Additional Credits
Journal
Molecular and biochemical parasitology
Publisher
Elsevier
ISSN
0166-6851
Access(Rights)
restricted