- Docente: Concettina Cappadone
- Credits: 9
- SSD: BIO/10
- Language: Italian
- Moduli: Concettina Cappadone (Modulo 1) Cecilia Prata (Modulo 2)
- Teaching Mode: Traditional lectures (Modulo 1) Traditional lectures (Modulo 2)
- Campus: Bologna
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Corso:
First cycle degree programme (L) in
Applied Pharmaceutical Sciences (cod. 8518)
Also valid for First cycle degree programme (L) in Applied Pharmaceutical Sciences (cod. 8518)
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from Oct 03, 2025 to Nov 21, 2025
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from Nov 24, 2025 to Jan 16, 2026
Learning outcomes
At the conclusion of the course, the student will have acquired fundamental knowledge of the structure and functions of the major biological macromolecules, including carbohydrates, lipids, proteins, and nucleic acids. The student will also understand the principal metabolic pathways, such as glycolysis, the citric acid cycle, and oxidative phosphorylation, and their regulatory mechanisms. Additionally, the student will comprehend the molecular processes by which genetic information is transmitted from DNA to proteins, encompassing transcription and translation. Furthermore, the student will gain expertise in the roles of macro- and micronutrients, as well as nutraceutical components, in maintaining health, and will be knowledgeable about the rational use of dietary supplements.
Course contents
MODULE I – GENERAL BIOCHEMISTRY – Concettina Cappadone
INTRODUCTION: Biological macromolecules; principles of thermodynamics; water as a solvent and its properties; weak molecular interactions.
PROTEINS: Amino acid classification. Primary structure: peptide bond. Secondary structure: α-helix and β‑sheet; fibrous proteins: α- and β‑keratins, collagen.Tertiary structure: protein folding, molecular chaperones, brief mention of misfolding and prion proteins. Quaternary structure
MYOGLOBIN AND HEMOGLOBIN: Structure of the heme group. Role of the proximal and distal histidine.Physiological functions of hemoglobin and myoglobin. Myoglobin–O₂ binding: hyperbolic curve and its functional significance. Hemoglobin–O₂ binding: sigmoidal curve and its functional significance. Homotropic and heterotropic modulators. Binding cooperativit. Effects of pH and CO₂ (Bohr effect). Effect of 2,3‑bisphosphoglycerate (2,3‑BPG). Abnormal hemoglobin variants.
CARBOHYDRATES: Structures of maltose, cellobiose, lactose, and sucrose. Classification of polysaccharides. Structure and function of starch, glycogen, and cellulose.
NUCLEOTIDES: Nucleoside mono‑, di‑ and triphosphates. ATP and nucleotide functions. Cyclic nucleotides: cAMP and cGMP
LIPIDS: Structures and functions of fatty acids, triacylglycerols, glycerophospholipids, sphingophospholipids, cholesterol
MEMBRANES: Phospholipid bilayer. Fluid mosaic model. Membrane asymmetry. Membrane proteins and their relative composition. Fluidity and the role of cholesterol. Lipid rafts. Selective permeability. Membrane transport: passive and active mechanisms.
ENZYMES: Endoergonic vs exoergonic reactions. Concepts of equilibrium and reaction rate. Activation energy. Active site and enzyme–substrate complex (ES). Enzyme mechanisms. Specificity; effects of pH and temperature. Classification of enzymes. Definitions of enzyme velocity and activity. Michaelis–Menten kinetics; significance of Vₘₐₓ and Kₘ . Irreversible and reversible enzyme inhibition. Allosteric enzymes: sigmoidal kinetics, T and R states, modulators. Covalent regulation: phosphorylation/dephosphorylation, zymogen activation
HEMOSTASIS: Coagulation cascade and blood clot formation
SIGNAL TRANSDUCTION: Signaling molecules, receptors, specificity, and amplification; cellular responses. Mechanisms of action of hydrophilic and lipophilic hormones. G‑protein–coupled receptor signaling. Tyrosine kinase receptors. Brief mention of defective receptor tyrosine kinase signaling and apoptosis
METABOLISM: Definitions of catabolism and anabolism. ATP hydrolysis and coupled reactions. High‑energy phosphate transfer compounds. Redox reactions. Structure and function of pyridine (NAD⁺/NADP⁺) and flavin (FAD/FMN) coenzymes.
GLYCOLYSIS: The ten glycolytic reactions. Anaerobic pyruvate fate: lactic acid and alcoholic fermentation. Regulation of glycolysis at the three irreversible steps. Aerobic pyruvate fate. Mitochondrial structure. Pyruvate dehydrogenase complex: TPP, lipoate, CoA‑SH, thioesters; reaction mechanism; allosteric and covalent regulation
KREBS CYCLE (TRICARBOXYLIC ACID CYCLE): Overview of reactions and fates of reduced coenzymes. Regulation of the cycle. Energy yield from complete glucose oxidation. Amphibolic roles of the cycle.
MITOCHONDRIAL ELECTRON TRANSPORT CHAIN & OXIDATIVE PHOSPHORYLATION: Overview; flavoproteins; iron–sulfur centers; coenzyme Q; cytochromes; descriptions of complexes I–IV. Chemiosmotic hypothesis. Structure of Fo–F₁ ATP synthase and oxidative phosphorylation mechanism. Brief mention of shuttle systems
GLUCOSE HOMEOSTASIS: Definition of blood glucose concentration. Gluconeogenesis: localization, precursors, reactions, and reciprocal regulation with glycolysis via tandem enzymes. Hormonal regulation of glycemia. Ketone body formation and utilization. Hepatic glycogen synthesis and glycogenolysis. Adrenaline and muscle glycogen metabolism.
FATTY ACID CATABOLISM: Adipose tissue triglyceride lipolysis. Fatty acid transport in blood (albumin). Activation in the cytosol and mitochondrial import. β‑oxidation of palmitic acid and its energetic yield. Brief mention of unsaturated and odd‑chain fatty acid β‑oxidation. Regulation of fatty acid oxidation
FATTY ACID BIOSYNTHESIS: Malonyl‑CoA formation. E. coli fatty acid synthase and butyryl‑ACP synthesis. Allosteric and hormonal regulation of acetyl‑CoA carboxylase. Brief reference to fatty acid elongation, desaturation, and essential fatty acids.
CHOLESTEROL: Functions of cholesterol and its biosynthesis
AMINO ACID CATABOLISM: Nitrogen excretion pathways. Transamination reactions; glutamate dehydrogenase reaction. Brief mention of carbamoyl phosphate formation and the urea cycle. Ammonia transport from extrahepatic tissues to the liver. Carbon skeleton catabolism and metabolic fates
NUCLEIC AC ACID STRUCTURE: Phosphodiester bond; enzymatic and non‑enzymatic hydrolysis of DNA and RNA. Restriction endonucleases; denaturation. Supercoiling in prokaryotes and eukaryotes. RNA: modified bases; structures and functions of different RNA types.
DNA REPLICATION: Central dogma. DNA replication in E. coli; DNA polymerase III and I characteristics. Replication fidelity and proofreading. DNA damage and mutations
TRANSCRIPTION: Transcription in E. coli; RNA polymerase characteristics and fidelity; promoters; constitutive vs regulated genes. Expanded central dogma; prokaryotic ribosome structure; tRNA aminoacylation.
GENETIC CODE: Definition; reading frames; start and stop codons; degeneracy; mutation types; Codon–anticodon interactions
TRANSLATION: Translation in E. coli: Shine–Dalgarno sequence; initiation, elongation, and termination.
RECOMBINANT DNA TECHNOLOGY: Overview of steps for constructing recombinant DNA and potential applications
MODULE II – NUTRITIONAL BIOCHEMISTRY – Cecilia Prata
FOOD AND NUTRITION, NUTRITIONAL STANDARDS, DIETARY GUIDELINES, INTRODUCTION TO CALORIMETRY: Fundamental concepts and definitions.
AVAILABLE AND NON-AVAILABLE CARBOHYDRATES: Nutritional sources; caloric value. Role of digestible carbohydrates; minimum and recommended intake. Glycemic index of foods. Lactose intolerance. Soluble and insoluble dietary fibers: solubility, viscosity, fermentability. Beneficial and adverse effects of fiber. Recommended intake levels
PROTEINS: Nutritional significance and caloric value. Nitrogen balance; protein turnover. Nutritional and functional roles of amino acids. Transamination reactions. Requirements for proteins and essential amino acids. Age-based recommended daily protein intake. Protein–energy malnutrition; celiac disease
LIPIDS: Nutritional sources; caloric value. Nutritionally relevant fatty acids: saturated, monounsaturated, polyunsaturated, trans fats; omega‑6 and omega‑3 families. Lipid requirements; dietary vs endogenous cholesterol; functions of cholesterol. Plasma lipoproteins
WATER, ALCOHOLIC & CAFFEINATED BEVERAGES: Nutritional characteristics; caloric content; ethanol metabolism; effects of caffeine and other stimulants.
VITAMINES: Nutritional importance and classification; deficiencies; stability; toxicity. Water-soluble vitamins (B‑complex and C): structure, function, requirements, sources, deficiency. Fat-soluble vitamins (A, D, E, K): structure, function, requirements, sources, deficiency, and toxicity
MINERALS: Function, food sources, bioavailability, recommended intakes, deficiency, and toxicity.
ROS AND ANTIOXIDANTS: Reactive oxygen species and definition of oxidative stress. Role of ROS in signaling and cellular damage. Cellular antioxidant defenses. Involvement of vitamins and minerals in antioxidant protection.
FUNCTIONAL FOODS AND NUTRACEUTICAL COMPONENTS: Phenols and polyphenols, especially flavonoids. Phytochemicals and their proposed mechanisms of action. Considerations on efficacy. Traditional functional foods
DIETETIC PRODUCTS AND DIETARY SUPPLEMENTS: Sports nutrition products: energy formulas, electrolyte‑vitamin supplements, protein and amino acid supplementation.
Readings/Bibliography
D.L. Nelson, M.M. Cox "Introduzione alla Biochimica di Lehninger", VI edizione, Zanichelli, 2018.
M.K. Campbell, S.O. Farrell, O.M. McDougal "Biochimica", EdiSES, V edizione
G. Arienti "Le basi molecolari della nutrizione", V edizione, Piccin, 2021
U. Leuzzi, E. Bellocco, D. Barreca "Biochimica della nutrizione", Zanichelli, 2013
C. Pignatti "Biochimica della nutrizione", Società Editrice Esculapio, 2022
Teaching methods
The course consists of two instructional modules: one worth 6 ECTS credits (General Biochemistry) and one worth 3 ECTS credits (Nutritional Biochemistry). The General Biochemistry module is delivered before the Nutritional Biochemistry module, as it provides essential foundational knowledge required for the subsequent nutrition topics. Instruction is conducted through traditional lectures, with instructors utilizing PowerPoint presentations and brief educational videos. No laboratory sessions are included in the curriculum.
Assessment methods
Learning assessment consists of a final examination delivered as an oral interview covering both instructional modules. For each exam session published on AlmaEsami, the student may register either for the General Biochemistry module alone or for both modules.
If a student decides not to attend an exam session for which they have registered, it is recommended that they withdraw from the registry list and/or inform the instructor via email.
Access to the Nutritional Biochemistry oral exam is permitted only upon successful completion of the General Biochemistry exam.
The final grade will be calculated with a weight of two‑thirds based on the General Biochemistry score and one‑third based on the Nutritional Biochemistry score.
Teaching tools
The textbook recommended by the instructor is the primary instrument through which the student must acquire their preparation.
All additional teaching materials—namely the PowerPoint presentations shown during lectures and any supplementary resources the instructor deems useful—serve as guides to facilitate the optimal understanding of the topics to be studied.
Students with learning disorders and\or temporary or permanent disabilities: please, contact the office responsible (https://site.unibo.it/studenti-con-disabilita-e-dsa/en/for-students ) as soon as possible so that they can propose acceptable adjustments. The request for adaptation must be submitted in advance (15 days before the exam date) to the lecturer, who will assess the appropriateness of the adjustments, taking into account the teaching objectives.
Office hours
See the website of Concettina Cappadone
See the website of Cecilia Prata
SDGs


This teaching activity contributes to the achievement of the Sustainable Development Goals of the UN 2030 Agenda.