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Graduated in biochemistry, bio-organic chemistry and food chemistry; PhD on structure-function relationship of the enzyme; postdoctoral work in X-ray absorption spectroscopy. Bachelor and master teaching on the subjects of organic chemistry, (bio)-inorganic chemistry, instrumental analysis, advanced spectroscopy, and advanced molecular structure determination; master and advanced courses on biocatalysis, homogeneous catalysis, X-ray absorption spectroscopy, and chemistry of metals in biological systems.
Gemini surfactants are amphiphilic molecules containing two head groups and two aliphatic tails which are linked by a spacer between the head groups, or between the linker region connecting the heads and the tails.1 Because their critical aggregate concentration is 103-fold lower they are more effective surfactants than the corresponding monovalent compounds (i.e. classical surfactants with a single chain and a single head group), which makes them interesting for various biomedical applications. Cationic geminis have shown to be viable agents for transfection, the introduction of nucleotides into a eukaryotic cell, thereby providing an alternative to viruses and cationic polymers.2 Amphiphilic peptides consisting of a peptide spacer with the N- and C-termini appended with hydrophobic groups are asymmetric geminis and are called gemini-like or geminoids. Interestingly, the SPKR geminoid with unsaturated alkyl tails can achieve transfection without the lysogenic helper lipid that is required in other cases.3 The proteases involved in the maturation of the polyprotein of dengue virus to new virus particles have cationic peptide sequences as their preferred substrates. Saturated geminoids of the KGnK and KAnK series (n = 1 or 2) are inhibitors of dengue virus 2 protease and the host protease furin, with slight selectivity of one over the other.4,5 The inhibitors are also active against dengue virus 2 infection in a cellular context, at concentrations below which they are toxic