Industrial pharmacy

The chemistry of carbon: functional groups. Cell architecture: organization, structure, and composition of prokaryotic and eukaryotic cells; functional role of subcellular organelles. Physicochemical properties of water: structure, solvation, hydrogen bonding, hydrophobic interactions, van der Waals forces, ionic bonds, colligative properties, osmosis, diffusion, ionization, acid-base chemistry, pH, pKa, buffer systems, biological buffers based on phosphate and carbonate. Nucleotides: structure and function of nucleotides, modified nucleotides, cyclic nucleotides. Amino acids: structure and function of standard and some non-standard amino acids, ionization and acid-base properties of amino acids. Proteins: peptide bond, primary, secondary, tertiary, and quaternary structure, supersecondary structures, intrinsically disordered domains. Biologically relevant peptides such as glutathione. Protein folding process, denaturation and refolding, Levinthal’s paradox. Structure and function of keratin, fibroin, and collagen. Structure and function of myoglobin and hemoglobin, heme group structure, oxygen-binding curves of myoglobin and hemoglobin, allosterism, cooperativity, Bohr effect, carbon dioxide transport, pathological hemoglobins. Enzymatic catalysis: general properties of enzymes, activation energy, catalytic mechanisms, steady-state kinetics, Michaelis-Menten equation, Lineweaver-Burk plot. Enzyme inhibition. Mechanisms of enzymatic activity regulation. Coenzymes and vitamins: structure and function of NAD and NADP, FMN, FAD (oxidized and reduced forms), vitamins A, C, D, E, K, lipoic acid, pyridoxal phosphate, thiamine pyrophosphate, biotin, pantothenic acid, folates, S-adenosyl methionine. Carbohydrates: structure and function of monosaccharides, disaccharides, polysaccharides, and glycoconjugates; the role of oligosaccharides in cellular recognition and adhesion; antigenic determinants of blood groups, lectins, glycoproteins. Lipids: structure and function of fatty acids, triacylglycerols, glycerophospholipids, sphingolipids, prostaglandins, and sterols. Lipoproteins. Cell membranes: structure and organization, micelles and lipid bilayers, lipid rafts, caveolae, general mechanisms of membrane fusion, membrane proteins. Transport mechanisms across membranes: ionophores, channels, pumps, glucose transporters. Cell signaling: major cellular signal transduction pathways, G protein–coupled receptors and second messengers, cyclic AMP, Ca²⁺, diacylglycerol, and inositol triphosphate, enzyme-linked receptors, ion channels. Mechanisms of action of adrenaline and glucagon, vision mechanism, action of insulin and steroid hormones. Introduction to metabolism: laws of thermodynamics, free energy, role of triphosphate nucleotides and high-energy phosphorylated compounds, redox reactions. Carbohydrate metabolism: reactions of glycolysis, alcoholic and lactic fermentation, pentose phosphate pathway, glycogen synthesis and degradation, glycogenin, gluconeogenesis. Overview of the Calvin cycle. Citric acid cycle: reactions of the cycle, structure and function of coenzyme A, pyruvate dehydrogenase complex, role of the cycle in anabolism. Electron transport, photosynthesis, and oxidative phosphorylation: mitochondrial electron transport chain, mitochondrial ATP synthesis, thermogenesis. Introduction to electron transport in chloroplasts. Lipid metabolism: lipid absorption (chylomicrons and lipoproteins), oxidation of saturated fatty acids, general principles of unsaturated and odd-chain fatty acid oxidation, ketone bodies and their metabolism, biosynthesis of fatty acids and cholesterol, overview of the biosynthesis of triacylglycerols and membrane phospholipids. Amino acid and protein metabolism: protein digestion and amino acid absorption, catabolism of amino groups, nitrogen excretion and the urea cycle. Overview of amino acid catabolism and biosynthesis. Tumor cell metabolism and the Warburg effect.

In order to successfully complete the Biochemistry course, students should have a solid foundation in the following areas: General and inorganic chemistry: Atomic structure, electronic configuration, chemical bonds Chemical equilibria, acid-base, oxidation-reduction Chemical thermodynamics (free energy, enthalpy, entropy) Properties of solutions and fundamental concepts of solubility, pH and buffers Organic chemistry: Structure and reactivity of the main functional groups (alcohols, amines, carboxylic acids, aldehydes, ketones, esters, amides) Basic concepts of stereochemistry and isomerism Fundamental reactions (nucleophilic, electrophilic, condensation, hydrolysis) Understanding of peptide bonds and the characteristics of organic biomolecules Cell biology: Structure and function of eukaryotic and prokaryotic cells Organization of cell organelles and their roles This knowledge is fundamental to understanding: Molecular interactions in biomolecules The principles of enzymatic catalysis and metabolic pathways The mechanisms of transport, regulation and signal transduction The energy concepts underlying biochemical reactions

Biochemistry by Thomas M. Devlin Edition VI/2023 Edises ISBN 9788836231300 Fundamentals of Biochemistry Donald Voet, Judith G Voet, Charlotte W Pratt Zanichelli

Not compulsory but highly recommended, with signatures taken three times during the course at random.

The oral examination consists of a 30-40 minute interview with the lecturer. Theoretical knowledge of the main topics covered in the programme (biomolecules, metabolism, enzymes, biosignalling, etc.) with related biomolecule structures and metabolic cycles. Ability to link biochemical concepts to cellular, physiological and pathological functions. Interpretation and analysis of experimental data such as enzyme curves and buffer systems. Clarity of expression and ability to summarise. Assessment is based on accuracy, completeness of answers and critical thinking skills.

Frontal Teaching Involves: Lessons delivered in person or online by the instructor Verbal explanation of concepts, supported by slides, diagrams, and visual materials Active student engagement through questions, examples, short quizzes Use of whiteboard, PowerPoint, educational videos, molecular models, etc. Example of Learning Objectives Example: Understand the structure of amino acids, their classification, protein structure, and protein folding. Content: General structure of amino acids Classification (polar/non-polar, charged, aromatic...) Protein structural levels (primary → quaternary) Myoglobin vs hemoglobin, Bohr effect Materials: PowerPoint slides with clear images (formulas, diagrams, 3D structures) Classification tables Oxygen saturation curves Intermediate Assessment: 3 oral questions or Multiple-choice quiz Tools and Materials: PowerPoint slides with clear visuals (formulas, diagrams, 3D protein structures) Short videos (e.g. protein folding, signal transduction, mitochondria) Concept maps and summary tables Interactive quizzes on Kahoot, Quizizz, Google Forms Printable or PDF handouts for review Assessment of Learning: Oral questions during the lesson Mini multiple-choice tests (5–10 questions) Short written exercises (e.g., fill-in-the-blank, true/false, definitions) Group discussion of a clinical or metabolic case (e.g., Warburg effect) Example of Weekly Schedule (Extract): Week Module Topics Activity 1 Chemistry of Water and Functional Groups Water structure, bonding, colligative properties Lecture + quiz 2 Cells and Organelles Prokaryotes vs. eukaryotes, mitochondria, ER Lecture + exercises 3 Amino Acids and Proteins Structure, folding, hemoglobin Lecture + oral questions 4 Enzymes Catalysis, Michaelis-Menten, inhibition Lecture + graph + quiz 5 Coenzymes and Vitamins NAD⁺, FAD, Vitamins A–D Slides + written test

The chemistry of carbon: functional groups. Cell architecture: organization, structure, and composition of prokaryotic and eukaryotic cells; functional role of subcellular organelles. Physicochemical properties of water: structure, solvation, hydrogen bonding, hydrophobic interactions, van der Waals forces, ionic bonds, colligative properties, osmosis, diffusion, ionization, acid-base chemistry, pH, pKa, buffer systems, biological buffers based on phosphate and carbonate. Nucleotides: structure and function of nucleotides, modified nucleotides, cyclic nucleotides. Amino acids: structure and function of standard and some non-standard amino acids, ionization and acid-base properties of amino acids. Proteins: peptide bond, primary, secondary, tertiary, and quaternary structure, supersecondary structures, intrinsically disordered domains. Biologically relevant peptides such as glutathione. Protein folding process, denaturation and refolding, Levinthal’s paradox. Structure and function of keratin, fibroin, and collagen. Structure and function of myoglobin and hemoglobin, heme group structure, oxygen-binding curves of myoglobin and hemoglobin, allosterism, cooperativity, Bohr effect, carbon dioxide transport, pathological hemoglobins. Enzymatic catalysis: general properties of enzymes, activation energy, catalytic mechanisms, steady-state kinetics, Michaelis-Menten equation, Lineweaver-Burk plot. Enzyme inhibition. Mechanisms of enzymatic activity regulation. Coenzymes and vitamins: structure and function of NAD and NADP, FMN, FAD (oxidized and reduced forms), vitamins A, C, D, E, K, lipoic acid, pyridoxal phosphate, thiamine pyrophosphate, biotin, pantothenic acid, folates, S-adenosyl methionine. Carbohydrates: structure and function of monosaccharides, disaccharides, polysaccharides, and glycoconjugates; the role of oligosaccharides in cellular recognition and adhesion; antigenic determinants of blood groups, lectins, glycoproteins. Lipids: structure and function of fatty acids, triacylglycerols, glycerophospholipids, sphingolipids, prostaglandins, and sterols. Lipoproteins. Cell membranes: structure and organization, micelles and lipid bilayers, lipid rafts, caveolae, general mechanisms of membrane fusion, membrane proteins. Transport mechanisms across membranes: ionophores, channels, pumps, glucose transporters. Cell signaling: major cellular signal transduction pathways, G protein–coupled receptors and second messengers, cyclic AMP, Ca²⁺, diacylglycerol, and inositol triphosphate, enzyme-linked receptors, ion channels. Mechanisms of action of adrenaline and glucagon, vision mechanism, action of insulin and steroid hormones. Introduction to metabolism: laws of thermodynamics, free energy, role of triphosphate nucleotides and high-energy phosphorylated compounds, redox reactions. Carbohydrate metabolism: reactions of glycolysis, alcoholic and lactic fermentation, pentose phosphate pathway, glycogen synthesis and degradation, glycogenin, gluconeogenesis. Overview of the Calvin cycle. Citric acid cycle: reactions of the cycle, structure and function of coenzyme A, pyruvate dehydrogenase complex, role of the cycle in anabolism. Electron transport, photosynthesis, and oxidative phosphorylation: mitochondrial electron transport chain, mitochondrial ATP synthesis, thermogenesis. Introduction to electron transport in chloroplasts. Lipid metabolism: lipid absorption (chylomicrons and lipoproteins), oxidation of saturated fatty acids, general principles of unsaturated and odd-chain fatty acid oxidation, ketone bodies and their metabolism, biosynthesis of fatty acids and cholesterol, overview of the biosynthesis of triacylglycerols and membrane phospholipids. Amino acid and protein metabolism: protein digestion and amino acid absorption, catabolism of amino groups, nitrogen excretion and the urea cycle. Overview of amino acid catabolism and biosynthesis. Tumor cell metabolism and the Warburg effect.

In order to successfully complete the Biochemistry course, students should have a solid foundation in the following areas: General and inorganic chemistry: Atomic structure, electronic configuration, chemical bonds Chemical equilibria, acid-base, oxidation-reduction Chemical thermodynamics (free energy, enthalpy, entropy) Properties of solutions and fundamental concepts of solubility, pH and buffers Organic chemistry: Structure and reactivity of the main functional groups (alcohols, amines, carboxylic acids, aldehydes, ketones, esters, amides) Basic concepts of stereochemistry and isomerism Fundamental reactions (nucleophilic, electrophilic, condensation, hydrolysis) Understanding of peptide bonds and the characteristics of organic biomolecules Cell biology: Structure and function of eukaryotic and prokaryotic cells Organization of cell organelles and their roles This knowledge is fundamental to understanding: Molecular interactions in biomolecules The principles of enzymatic catalysis and metabolic pathways The mechanisms of transport, regulation and signal transduction The energy concepts underlying biochemical reactions

Biochemistry by Thomas M. Devlin Edition VI/2023 Edises ISBN 9788836231300 Fundamentals of Biochemistry Donald Voet, Judith G Voet, Charlotte W Pratt Zanichelli

Not compulsory but highly recommended, with signatures taken three times during the course at random.

The oral examination consists of a 30-40 minute interview with the lecturer. Theoretical knowledge of the main topics covered in the programme (biomolecules, metabolism, enzymes, biosignalling, etc.) with related biomolecule structures and metabolic cycles. Ability to link biochemical concepts to cellular, physiological and pathological functions. Interpretation and analysis of experimental data such as enzyme curves and buffer systems. Clarity of expression and ability to summarise. Assessment is based on accuracy, completeness of answers and critical thinking skills.

Frontal Teaching Involves: Lessons delivered in person or online by the instructor Verbal explanation of concepts, supported by slides, diagrams, and visual materials Active student engagement through questions, examples, short quizzes Use of whiteboard, PowerPoint, educational videos, molecular models, etc. Example of Learning Objectives Example: Understand the structure of amino acids, their classification, protein structure, and protein folding. Content: General structure of amino acids Classification (polar/non-polar, charged, aromatic...) Protein structural levels (primary → quaternary) Myoglobin vs hemoglobin, Bohr effect Materials: PowerPoint slides with clear images (formulas, diagrams, 3D structures) Classification tables Oxygen saturation curves Intermediate Assessment: 3 oral questions or Multiple-choice quiz Tools and Materials: PowerPoint slides with clear visuals (formulas, diagrams, 3D protein structures) Short videos (e.g. protein folding, signal transduction, mitochondria) Concept maps and summary tables Interactive quizzes on Kahoot, Quizizz, Google Forms Printable or PDF handouts for review Assessment of Learning: Oral questions during the lesson Mini multiple-choice tests (5–10 questions) Short written exercises (e.g., fill-in-the-blank, true/false, definitions) Group discussion of a clinical or metabolic case (e.g., Warburg effect) Example of Weekly Schedule (Extract): Week Module Topics Activity 1 Chemistry of Water and Functional Groups Water structure, bonding, colligative properties Lecture + quiz 2 Cells and Organelles Prokaryotes vs. eukaryotes, mitochondria, ER Lecture + exercises 3 Amino Acids and Proteins Structure, folding, hemoglobin Lecture + oral questions 4 Enzymes Catalysis, Michaelis-Menten, inhibition Lecture + graph + quiz 5 Coenzymes and Vitamins NAD⁺, FAD, Vitamins A–D Slides + written test