>André Silva

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PhD in Pharmaceutical Sciences, King’s College London, 2009

 

Area of scientific activity

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The area of scientific activity is Biochemistry and Chemical Biology with a strongcommitment to application in Health Sciences. I have been dedicated are the study of protein post-translational modifications (PTMs) both at the structural and functional levels. I become proficient in proteomics methodologies for the identification and characterization of PTMs.

Particular interests are the study of protein glycosylation, glycation and oxidation in cancer, diabetes mellitus, iron overload and ageing.

Having a background in the biochemistry of iron, I have been focusing on the impact of serum protein modifications in the physiology of systemic iron transport in the context of hyperglycaemia (diabetes) and iron overload (hereditary hemochromatosis). I have also been collaborating on the development of iron chelators and iron chelates for several applications: from tuberculosis therapy to treating plant iron deficiency and the study of iron complexes used in medieval inks.

Recently, I have established a mass spectrometry based analytical platform for the prospection of glycoprotein biomarkers in bladder cancer, collaborating with researchers at IPO-Porto, the largest oncological hospital in Portugal.

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Domain of specialization

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Biochemistry and Chemical Biology

Mass Spectrometry

Proteomics

Glycoproteomics

Inorganic Biochemistry of Iron

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Present research interest

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My main research interest is the development of new analytical biochemistry methods for disease prognosis thought the identification of biomarkers. Current research focuses in:

1 – study of serum protein biochemistry, especially the occurrence of non-enzymatic post-translational modifications (such as glycation and oxidation) which are bound to play a major role in the disruption of normal serum iron transport;

2 – speciation of iron species in biological fluids;

3 - study of protein oxidation in age related pathologies;

4 – Discovery of protein biomarkers in bladder cancer;

5 – Development of a glycomics based glycoproteomics approach for the discovery of glycoprotein epitopes in cancer;

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6 – Analysis of the functional and structural impact of protein post-translational modifications.

     >selected publications

 

Vinchi F, Porto G, Simmelbauer A, Altamura S, Passos ST, Garbowski M, Silva AMN, Spaich S, Seida SE, Sparla R, Hentze MW, Muckenthaler M (2019) Atherosclerosis is aggravated by iron overload and ameliorated by dietary and pharmacological iron restriction. Eur. Heart J. Advanced publication

DOI: 10.1093/eurheartj/ehz112

 

Zhang H, Freitas D, Sang Kim H, Fabijanic K, Li Z, Chen H, Mark MT, Molina H, Martin AB, Bojmar L, Fang J, Rampersaud S, Hoshino A, Matei I, Kenific C, Nakajima M, Mutvei A, Sansone P, Buehring W, Wang H, Jimenez JP, Cohen-Gould L, Paknejad N, Brendel M, Manova-Todorova K, Magalhães A, Ferreira JA, Osório H, Silva AM, Massey H, Cubillos-Ruiz JR, Galletti G, Giannakakou P, Cuervo AM, Blenis J, Schwartz R, Brady MS, Peinado H, Bromberg J, Matsui H, Reis CA, Lyden D (2018) Identification of distinct nanoparticles and subsets of extracellular vesicles by asymmetric flow field-flow fractionation. Nat. Cell Biol. 20(3), 332-343, DOI: 10.1038/s41556-018-0040-4

 

Cotton S, Azevedo R, Gaiteiro C, Ferreira D, Lima L, Peixoto A, Fernandes E, Neves M, Neves D, Amaro T, Cruz R, Tavares A, Rangel M, Silva AMN, Santos LL, Ferreira JA (2017) Targeted O-glycoproteomics explored increased sialylation and identified MUC16 as a poor prognosis biomarker in advanced stage bladder tumours. Mol. Oncol. 11(8), 895-912 DOI: 10.1002/1878-0261.12035

 

Silva AMN*, Sousa PRH, Coimbra JTS, Brás NF, Vitorino R, Fernandes PA, Ramos MJ, Rangel M, Domingues P* (2014) The glycation site specificity of human serum transferrin is determinant for the protein functional impairment under elevated glycemic conditions. Biochem. J. 461(1), 33-42. DOI: 10.1042/BJ20140133

 

Silva AMN, Hider RC (2009) Influence of non-enzymatic post-translation modifications on the ability of human serum albumin to bind iron. Implications for non-transferrin-bound iron speciation. Biochim. Biophys. Acta - Proteins and Proteomics 1794(10), 1449-1458, DOI: 10.1016/j.bbapap.2009.06.003

 

Silva AMN, Kong XL, Parkin MC, Cammack R, Hider RC (2009) Iron(III) citrate speciation in aqueous solution. Dalton Transactions 40, 8616-8625. doi: 10.1039/B910970F