The electronic structure of human erythropoietin as an aid in the design of oxidation-resistant therapeutic proteins

Fabio Pichierri

doi:10.1016/j.bmcl.2005.10.041

The electronic structure of human erythropoietin as an aid in the design of oxidation-resistant therapeutic proteins

Fabio Pichierri

ENG - Applied Chemistry

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

Abstract

The electronic structure of human erythropoietin (HuEPO) has been investigated with the aid of quantum mechanical calculations. The results indicate that the protein is highly polarized and its permanent dipole moment has a magnitude of 471 D. The HOMO of HuEPO is localized on Trp51, which stays in close proximity to Met54. Three oxidation-resistant mutants of HuEPO (W51F, M54V, and W51F-M54V) have been modeled and their electronic structures are compared to that of the native protein. Among them, the W51F mutation is predicted to be the most effective in increasing the oxidation potential of the protein.

Original language	English
Pages (from-to)	587-591
Number of pages	5
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	16
Issue number	3
DOIs	https://doi.org/10.1016/j.bmcl.2005.10.041
Publication status	Published - 2006 Feb 1

Keywords

Anemia
Computational chemistry
Erythropoietin
Protein-based therapeutics

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Pharmaceutical Science
Drug Discovery
Clinical Biochemistry
Organic Chemistry

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KW - Protein-based therapeutics

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