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Robert Charles Hider (born 1943, London) is a Professor of Medicinal Chemistry at King's College London. He is a specialist in therapeutic iron chelators.
Education
After education at Winslade School, Exeter, Hider attended King's College London as a BSc chemistry and physics undergraduate (1961–64), and then obtained a Ph.D. there in synthetic chemistry (1967).
Academic career
Holder began a career in biological chemistry in the endocrinology department of St Thomas's Hospital Medical School under the supervision of David London. He studied the influence of insulin on muscle protein synthesis. In 1970 he was appointed as the first lecturer in biological chemistry at Essex University and initiated the biological chemistry degree. During this period his research was directed towards the study of membranes,[1] the mechanisms of penetration of such structures[2][3][4] and their mode of interaction with animal toxins.[5][6][7][8] In 1977 he was awarded sabbatical leave and worked with Joe Neilands, in the Department of Biochemistry, the University of California, Berkeley. This laboratory was centred on siderophore chemistry and biochemistry [9]
On return to the UK, Hider in collaboration with Ernest Huehns, developed the first orally active iron chelator, deferiprone,[10][11][12] which was introduced into clinical trials by Victor Hoffbrand in 1987.[13] During this decade he was promoted to senior lecturer and then to reader. Deferiprone is currently used worldwide for the treatment of transfusion – induced iron overload, which is associated with β-thalassaemia and sickle cell anaemia.
In 1987 Hider was appointed professor of medicinal chemistry in the pharmacy department of King's College London, where he continued his studies on iron biochemistry. Over the period 1987–2008 he introduced several analytical methods for "non-transferrin bound iron"[14] and continued to develop new iron chelators[15] and particularly those targeted to mitochondria.[16][17] He collaborated with Ciba Geigy (now Novartis), Apotex, Shire Pharmaceuticals, Vifor, and Renapharma.
During the 1992–2008 period at King's College Hider was, at various times, head of the health science division (1992–1994), head of the School of Life, Basic Medicinal and Health Sciences (1994–2000); head of the department of pharmacy (2000–2003), and head of the School of Biomedical and Health Sciences (2003–2007). In 2008, he retired from teaching and administration duties but continued to maintain an active research laboratory.[citation needed]
Selected publications
His most cited articles are:
Hider RC, Kong X. Chemistry and biology of siderophores. Natural product reports. 2010;27(5):637-57
Shayeghi M, Latunde-Dada GO, Oakhill JS, Laftah AH, Takeuchi K, Halliday N, Khan Y, Warley A, McCann FE, Hider RC, Frazer DM. Identification of an intestinal heme transporter. Cell. 2005 Sep 9;122(5):789-801.
Hider RC. Siderophore mediated absorption of iron. InSiderophores from Microorganisms and Plants 1984 (pp. 25–87). Springer, Berlin, Heidelberg.
Hider married Shirley Nickels in 1967. They have two children and six grandchildren.
References
^Bunce AS and Hider RC. The composition of black lipid membranes formed from egg-yolk lecithin, cholesterol and n-decane. Biochimica Biophysica Acta., 1974;363, 423-427.
^Ash PS, Bunce AS, Dawson CR and Hider RC. The effect of synthetic polymers on the electrical and permeability properties of lipid membranes. Biochim. Biophys. Acta., 1978; 510, 216-229.
^Dawson CR, Drake AF, Helliwell J and Hider RC. The interaction of bee melittin with lipid bilayer membranes. Biochim. Biophys. Acta., 1978; 510, 75-86.
^Drake AF and Hider RC. The structure of melittin in lipid bilayers. Biochim. Biophys. Acta., 1979; 555, 371-373.
^Dufton MJ and Hider RC. Snake toxin secondary structure predictions – structure activity relationships. J. Mol. Biol., 1977; 115, 177-193.
^Hider RC and Ragnarsson U. A proposal for the structure of apamin. FEBS Letts., 1980; 111, 189-193.
^Hider RC, Drake AF, Inagaki F, Williams RJP, Endo T and Miyatawa T. The molecular conformation of α-cobratoxin as studied by nuclear magnetic resonance and circular dichroism. J. Mol. Biol, 1982; 158, 275-291.
^Inagaki F, Hider RC, Hodges SJ and Drake AF. Molecular conformation of α- bungarotoxin as studied by nuclear magnetic resonance and circular dichroism. J. Mol. Biol., 1985; 183, 575-590.
^Hider RC, Silver J, Neilands JB, Morrison IEG, Rees LVC. Identification of iron(II) enterobactin and its possible role in Escherichia coli iron transport. FEBS Letters, 1979; 102: 325-328.
^Huehns ER, Porter JB and Hider RC. Selection of hydroxypyridin-4-ones for the treatment of iron overload using in vitro and in vivo models. Haemoglobin, 1988; 12, 593-600.
^Porter JB, Gyparaki M, Burke LC, Huehns ER, Sarpong P, Saez V and Hider RC. Iron mobilization from hepacyte monolayer cultures by chelators: The importance of membrane permeability and iron binding constant. Blood, 1988; 72, 1497-1505.
^Porter JB, Huehns ER and Hider RC. The development of iron chelating drugs. Ballieres Clinical Haematology, (ed. C Hershco), 1989; 257-292.
^Hider RC, Hoffbrand AV. The role of deferiprone in iron chelation. New England J. Medicine, 2018; 379: 2140-50.
^Singh S, Hider RC and Porter JB. A direct method for quantification of non-transferrin bound iron. Anal. Biochem., 1990; 186, 320-323.
^Dobbin PS, Hider RC, Hall AD, Taylor PD, Sarpong P, Porter JB, Xiao G and van der Helm D. Synthesis, physicochemical properties, and biological evaluation of N-substituted 2-alkyl-3-hydroxy-4(1H)-pyridinones:orally active iron chelators with clinical potential. J. Med. Chem., 1993; 36, 2448-2458.
^Abbate V, Reelfs O, Hider RC, Pourzand C., Design of novel fluorescent mitochondria-targeted peptides with iron-selective sensing activity. Biochemical Journal. 2015, 469, 357-366.
^Ward RJ, Dexter D, Florence A, Aouad F, Hider RC, Jenner P and Crichton RP. Brain iron in the ferrocene-loaded rat: Its chelation and influence on dopamine metabolism. Biochem. Pharmacol., 1995; 49, 1821-1826.
