| Literature DB >> 18191882 |
Carlos Giovanni Pinzón1, Hernando Curtidor, Adriana Bermúdez, Martha Forero, Magnolia Vanegas, Jorge Rodríguez, Manuel E Patarroyo.
Abstract
Plasmodium falciparum rhoptry-associated membrane antigen (RAMA) peptides used in normal red blood cell (RBC) binding assays revealed that peptides 33426 (79NINILSSVHRKGRILYDSF97) and 33460 (777HKKREKSISPHSYQKVSTKVQ797) bound with high activity, presenting nanomolar affinity constants. Such high binding activity peptides (HABPs) displayed helicoid and random coil structures as determined by circular dichroism. HABPs inhibited P. falciparumin vitro invasion of normal RBC by up to 61% (depending on concentration), suggesting that some RAMA protein regions could be involved in P. falciparum invasion of RBC. The nature and localisation of receptors on RBC surface responsible for HABP binding were studied using enzyme-treated erythrocytes and structural analysis.Entities:
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Year: 2007 PMID: 18191882 DOI: 10.1016/j.vaccine.2007.11.086
Source DB: PubMed Journal: Vaccine ISSN: 0264-410X Impact factor: 3.641