Vanadium Complexes as Prospective Therapeutics: Structural Characterization of a V-IV Lysozyme Adduct

Marino F. A. Santos; Isabel Lopes Correia; Ana Isabel Nobre Martins Aguiar de Oliveira Ricardo; Eugenio Garribba; Joao Costa Pessoa; Teresa Santos-Silva

doi:10.1002/ejic.201402408

Vanadium Complexes as Prospective Therapeutics: Structural Characterization of a V-IV Lysozyme Adduct

Marino F. A. Santos, Isabel Lopes Correia, Ana Isabel Nobre Martins Aguiar de Oliveira Ricardo, Eugenio Garribba, Joao Costa Pessoa, Teresa Santos-Silva

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

55 Citations (Scopus)

Abstract

The biological activity of vanadium complexes, namely, as insulin enhancers, is well known. We report a combined X-ray crystallography, electron paramagnetic resonance, and density functional theory study of the interaction of vanadium picolinate complexes with hen egg white lysozyme (HEWL). We show that the (VO)-O-IV(pic)(2) complex covalently binds to the COO- group of the side chain of Asp52 of HEWL. The long V-IV=O bond obtained in the X-ray study is explained to be due to reduction of V-IV to V-III during exposure of the crystals to the intense X-ray beam.

Original language	English
Pages (from-to)	3293-3297
Number of pages	5
Journal	European Journal of Inorganic Chemistry
Issue number	21
DOIs	https://doi.org/10.1002/ejic.201402408
Publication status	Published - Jul 2014

Keywords

Vanadium
Protein adducts
Medicinal chemistry
EPR spectroscopy
Density functional calculations
HYPERFINE COUPLING-CONSTANTS
BLOOD-SERUM
(VO)-O-IV COMPLEXES
CRYSTAL-STRUCTURE
AQUEOUS-SOLUTION
AMINO-ACIDS
SOLID-STATE
TRANSFERRIN
OXOVANADIUM(IV)
PREDICTION

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10.1002/ejic.201402408

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title = "Vanadium Complexes as Prospective Therapeutics: Structural Characterization of a V-IV Lysozyme Adduct",

abstract = "The biological activity of vanadium complexes, namely, as insulin enhancers, is well known. We report a combined X-ray crystallography, electron paramagnetic resonance, and density functional theory study of the interaction of vanadium picolinate complexes with hen egg white lysozyme (HEWL). We show that the (VO)-O-IV(pic)(2) complex covalently binds to the COO- group of the side chain of Asp52 of HEWL. The long V-IV=O bond obtained in the X-ray study is explained to be due to reduction of V-IV to V-III during exposure of the crystals to the intense X-ray beam.",

keywords = "Vanadium, Protein adducts, Medicinal chemistry, EPR spectroscopy, Density functional calculations, HYPERFINE COUPLING-CONSTANTS, BLOOD-SERUM, (VO)-O-IV COMPLEXES, CRYSTAL-STRUCTURE, AQUEOUS-SOLUTION, AMINO-ACIDS, SOLID-STATE, TRANSFERRIN, OXOVANADIUM(IV), PREDICTION",

author = "Santos, {Marino F. A.} and Correia, {Isabel Lopes} and Ricardo, {Ana Isabel Nobre Martins Aguiar de Oliveira} and Eugenio Garribba and Pessoa, {Joao Costa} and Teresa Santos-Silva",

year = "2014",

month = jul,

doi = "10.1002/ejic.201402408",

language = "English",

pages = "3293--3297",

journal = "European Journal of Inorganic Chemistry",

issn = "1434-1948",

publisher = "Wiley-VCH Verlag Berlin",

number = "21",

}

TY - JOUR

T1 - Vanadium Complexes as Prospective Therapeutics

T2 - Structural Characterization of a V-IV Lysozyme Adduct

AU - Santos, Marino F. A.

AU - Correia, Isabel Lopes

AU - Ricardo, Ana Isabel Nobre Martins Aguiar de Oliveira

AU - Garribba, Eugenio

AU - Pessoa, Joao Costa

AU - Santos-Silva, Teresa

PY - 2014/7

Y1 - 2014/7

N2 - The biological activity of vanadium complexes, namely, as insulin enhancers, is well known. We report a combined X-ray crystallography, electron paramagnetic resonance, and density functional theory study of the interaction of vanadium picolinate complexes with hen egg white lysozyme (HEWL). We show that the (VO)-O-IV(pic)(2) complex covalently binds to the COO- group of the side chain of Asp52 of HEWL. The long V-IV=O bond obtained in the X-ray study is explained to be due to reduction of V-IV to V-III during exposure of the crystals to the intense X-ray beam.

AB - The biological activity of vanadium complexes, namely, as insulin enhancers, is well known. We report a combined X-ray crystallography, electron paramagnetic resonance, and density functional theory study of the interaction of vanadium picolinate complexes with hen egg white lysozyme (HEWL). We show that the (VO)-O-IV(pic)(2) complex covalently binds to the COO- group of the side chain of Asp52 of HEWL. The long V-IV=O bond obtained in the X-ray study is explained to be due to reduction of V-IV to V-III during exposure of the crystals to the intense X-ray beam.

KW - Vanadium

KW - Protein adducts

KW - Medicinal chemistry

KW - EPR spectroscopy

KW - Density functional calculations

KW - HYPERFINE COUPLING-CONSTANTS

KW - BLOOD-SERUM

KW - (VO)-O-IV COMPLEXES

KW - CRYSTAL-STRUCTURE

KW - AQUEOUS-SOLUTION

KW - AMINO-ACIDS

KW - SOLID-STATE

KW - TRANSFERRIN

KW - OXOVANADIUM(IV)

KW - PREDICTION

U2 - 10.1002/ejic.201402408

DO - 10.1002/ejic.201402408

M3 - Article

SN - 1434-1948

SP - 3293

EP - 3297

JO - European Journal of Inorganic Chemistry

JF - European Journal of Inorganic Chemistry

IS - 21

ER -

Vanadium Complexes as Prospective Therapeutics: Structural Characterization of a V-IV Lysozyme Adduct

Abstract

Keywords

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