PhD in Pharmaceutical Sciences, King’s College London, 2009
Area of scientific activity
The area of scientific activity is Biochemistry and Chemical Biology with a strong commitment to applications in Health Sciences. I have been dedicated tothe 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.
Domain of specialization
Biochemistry and Chemical Biology
Inorganic Biochemistry of Iron
Present research interest
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 cancer;
5 – Development of a glycomics based glycoproteomics approach for the discovery of glycoprotein epitopes in cancer;
6 – Analysis of the functional and structural impact of protein post-translational modifications.
Silva AMN, Rangel M (2022) The (Bio)Chemistry of Non-Transferrin-Bound Iron. Molecules. 27, 1784. DOI: 10.3390/molecules27061784
Silva AMN, Moniz T, de Castro B, Rangel M (2021) Human transferrin: a bioinorganic chemistry perspective. Coord. Chem. Rev. 449, 214186. DOI: 10.1016/j.ccr.2021.214186
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. 41(28), 2681–2695.
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
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