Journal article

A partially structured region of a largely unstructured protein, Plasmodium falciparum merozoite surface protein 2 (MSP2), forms amyloid-like fibrils

Xiaodong Yang, Christopher G Adda, David W Keizer, Vince J Murphy, Michael M Rizkalla, Matthew A Perugini, David C Jackson, Robin F Anders, Raymond S Norton

JOURNAL OF PEPTIDE SCIENCE | JOHN WILEY & SONS LTD | Published : 2007

Abstract

Merozoite surface protein 2 (MSP2) from the human malaria parasite Plasmodium falciparum is expressed as a GPI-anchored protein on the merozoite surface. It has been implicated in the process of erythrocyte invasion and is a leading vaccine candidate. MSP2 is an intrinsically unstructured protein (IUP), and recombinant MSP2 forms amyloid-like fibrils upon storage. We have examined synthetic peptides corresponding to sequences in the conserved N-terminal region of MSP2 for the presence of local structure and the ability to form fibrils related to those formed by full-length MSP2. In a 25-residue peptide corresponding to the entire N-terminal region of mature MSP2, structures calculated from N..

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