Synthetic peptides corresponding to a repetitive sequence of malarial histidine rich protein bind haem and inhibit haemozoin formation in vitro

Pandey, Amit V.; Joshi, Ratanmani; Tekwani, Babu L.; Singh, Ram L.; Chauhan, Virender S. (1997). Synthetic peptides corresponding to a repetitive sequence of malarial histidine rich protein bind haem and inhibit haemozoin formation in vitro. Molecular and biochemical parasitology, 90(1), pp. 281-287. Elsevier 10.1016/S0166-6851(97)00161-8

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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.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > BioMedical Research (DBMR) > DCR Unit Tiefenau Hospital (discontinued) > Forschungsgruppe Endokrinologie/Diabetologie/Metabolik (Pädiatrie) (discontinued)

UniBE Contributor:

Pandey, Amit Vikram

Subjects:

500 Science > 570 Life sciences; biology

ISSN:

0166-6851

Publisher:

Elsevier

Language:

English

Submitter:

Amit Vikram Pandey

Date Deposited:

25 Aug 2014 10:43

Last Modified:

06 Dec 2014 19:06

Publisher DOI:

10.1016/S0166-6851(97)00161-8

PubMed ID:

9497049

Uncontrolled Keywords:

Malaria, Haemoglobin, Haem, Haemozoin, Histidine-rich protein, Chloroquine

BORIS DOI:

10.7892/boris.41754

URI:

https://boris.unibe.ch/id/eprint/41754

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