Steered Molecular Dynamic Simulations Reveal Critical Residues for (Un) Binding of Substrates, Inhibitors and a Product of the Malarial PFM1AAP

Daniel S. Moore; John P. Dalton; Irina G. Tikhonova

doi:10.1016/j.bpj.2016.11.1920

Steered Molecular Dynamic Simulations Reveal Critical Residues for (Un) Binding of Substrates, Inhibitors and a Product of the Malarial PFM1AAP

Daniel S. Moore, John P. Dalton, Irina G. Tikhonova

Research output: Contribution to journal › Meeting abstract › peer-review

Abstract

Malaria is one of the most prevalent and fatal infectious diseases of the world and is
compounded by wide spread drug resistance, with some strains developing resistance to current front-line anti-malarials. Plasmodium falciparum M1 alanyl aminopeptidase (PFM1AAP) is involved in the terminal stages of haemoglobin degradation and the generation of an amino acid pool to support parasitic growth and development. This represents a promising new anti-malarial target where inhibition of this enzyme is lethal to

Original language	English
Pages (from-to)	354a
Number of pages	1
Journal	Biophysical Journal
Volume	112
Issue number	3 (Supplement 1)
DOIs	https://doi.org/10.1016/j.bpj.2016.11.1920
Publication status	Published - 03 Feb 2017

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abstract = "Malaria is one of the most prevalent and fatal infectious diseases of the world and is compounded by wide spread drug resistance, with some strains developing resistance to current front-line anti-malarials. Plasmodium falciparum M1 alanyl aminopeptidase (PFM1AAP) is involved in the terminal stages of haemoglobin degradation and the generation of an amino acid pool to support parasitic growth and development. This represents a promising new anti-malarial target where inhibition of this enzyme is lethal to ",

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AB - Malaria is one of the most prevalent and fatal infectious diseases of the world and is compounded by wide spread drug resistance, with some strains developing resistance to current front-line anti-malarials. Plasmodium falciparum M1 alanyl aminopeptidase (PFM1AAP) is involved in the terminal stages of haemoglobin degradation and the generation of an amino acid pool to support parasitic growth and development. This represents a promising new anti-malarial target where inhibition of this enzyme is lethal to

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DO - 10.1016/j.bpj.2016.11.1920

M3 - Meeting abstract

SN - 0006-3495

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JO - Biophysical Journal

JF - Biophysical Journal

IS - 3 (Supplement 1)

ER -

Steered Molecular Dynamic Simulations Reveal Critical Residues for (Un) Binding of Substrates, Inhibitors and a Product of the Malarial PFM1AAP

Abstract

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