General biochemistry - Prof. Sergio Oddi - a.a. 2025/2026
Section outline
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Associate Professor of Biochemistry. He has taught courses in “Biochemical Methods for Food Quality Control,” “Genetics and Molecular Biology Applied to Agri-Food,” “Biochemical Diagnostics,” “Methods Applied to the Study of Reproduction,” “Enzymology,” “Applied Biochemistry and Nutrition,” and “Elements of Chemistry and Biochemistry.” He currently teaches the course ‘Biochemistry’ for the Master's Degree in Veterinary Medicine and “Food Biochemistry” for the Bachelor's Degree in Food Science and Technology at the University of Teramo.
His main scientific interest concerns the signaling of endocannabinoids, a new class of bioactive lipids derived from arachidonic acid, capable of activating the same receptors recognized by the psychoactive principles of Cannabis indica. In particular, his study aims to clarify the biochemical mechanisms through which these lipids perform biosignaling functions in the central nervous system, proving to be relevant both in physiological processes and in the context of neurodegenerative and neuroinflammatory diseases. Through his research, which uses the most advanced molecular and microscopic techniques, he has contributed to clarifying important aspects in the field of (i) the mechanisms underlying the metabolism, transport, and intracellular accumulation of endocannabinoids; (ii) the spatiotemporal dynamics of cannabinoid receptors in their membrane environment; (iii) the neuroprotective role of (endo)cannabinoids in animal models of neurodegenerative diseases.
From an application perspective, he has contributed to the development and characterization of new molecules, covered by international patents, for which he has been registered as an inventor with the European Patent Office (https://register.epo.org/application?number=EP06754964&tab=main). With the authorization of the Universities of Rome “Tor Vergata” and Teramo, one of the patented molecules, biotinyl-anandamide (MM-22), is currently produced and marketed by Tocris Bioscience (http://www.tocris.com/dispprod.php?ItemId=280487#. UJQM2G9U-QB).
Prof. Oddi has published more than 70 full-length articles, mainly in international peer-reviewed biochemistry journals (ResearchGate score = 1250; h-index = 32; with more than 3000 total citations; https://www.researchgate.net/profile/Sergio_Oddi/scores).
COURSE OBJECTIVES AND PREREQUISITES
- Main objective of the course > This course introduces students to the foundational concepts of biochemistry essential for the biotechnology profession. It covers the structure and function of major organic molecules—such as lipids, carbohydrates, proteins, myoglobin, hemoglobin, connective proteins, and enzymes—with a particular focus on the structure-function relationships within different classes of biological macromolecules. The course also provides foundational knowledge in molecular biology relevant to future professional activities, including key principles of genetic information flow, the organization of prokaryotic and eukaryotic cells, and basic concepts of evolution. Additionally, it equips students with the necessary background to understand more advanced topics such as metabolism and physiology, which will be addressed in subsequent courses.
- Prerequisites > The “General Biochemistry” course requires basic logical and mathematical knowledge.
TEACHING UNIT 1 - "Biological Molecules"
THE LIPIDS
The structure, properties and functions of lipids, classification. Saturated and unsaturated fatty acids, their nomenclature, Eicosanoids. The physico-chemical properties of fatty acids. The relationship between pKa and pH. Reserve lipids: triglycerides, their localization. Fats and oils. The iodine test. The hydrogenation of vegetable oils. The biological functions of triglycerides. Membrane lipids: glycerophospholipids and sphingolipids. Steroids. Cholesterol, steroid hormones, adrenocorticoid hormones, bile salts. The amphipathic lipid aggregates in water: micelles, bilayers, liposomes.CARBOHYDRATES
The structure, properties and functions of carbohydrates. The classification of monosaccharides. The chirality of monosaccharides. The stereoisomers. Enantiomers and epimers. Cyclic sugars: hemiacetals and hemichetals. The furanosic and pyranosic structures of monosaccharides, the anomers. Conventions for writing the cyclic structures of monosaccharides: conformational formulas, Fischer's projections, Haworth's formulas. The redox of sugars. Acetals and ketals. The glycosidic bond. Disaccharides: maltose, cellobiose, lactose, sucrose. Animal polysaccharides: glycogen. Vegetable polysaccharides: starch and cellulose. The deoxysugars.AMINO ACIDS, PEPTIDES AND PROTEINS
The biological functions of proteins. The classification and common structural properties of amino acids present in proteins. The enantiomers. Stereochemistry and acid-base behavior of amino acids. The amphoteric molecules. The amino acid families. The structure and properties of the side chains of standard amino acids, the disulfide bond, non-standard amino acids. The peptides and the resonance of the peptide bond. The protein conformation. The primary structure. The secondary structures: the alpha helix and the beta sheet. Supersecondary structures. Domains and the tertiary structure. The quaternary structure and the control of biological activity. The oligomers. Macromolecular complexes. The size of the proteins. Simple proteins and conjugated proteins. The Ramachandran chart and its meaning. Fibrous and globular proteins. The common properties of globular proteins. Relationship between protein structure and function. Denaturation and denaturing agents, protein renaturation. Homologous proteins and invariant amino acids. Protein dissociation. Protein wrapping through discrete intermediates.THE CONNECTIVE PROTEINS
Collagen and its functions. The tropocollagen. The types of collagen. The proline and lysine in collagen. The collagen glycoprotein. The melting temperature of collagen. The maturation of collagen. The procollagen peptidase. Collagen under the electron microscope. The intra and intermolecular cross-links. The collagenases. Elastine: structure and function. The covalent transverse bonds.MYGLOBIN (Mb) AND HEMOGLOBIN (Hb)
The transport and storage of oxygen: the role of hemoglobin (Hb) and myoglobin (Mb). The structure of the two molecules; the globin winding. The heme group and its localization. The most important forms of myoglobin. Metamyoglobin and methemoglobin. The toxicity of carbon monoxide (CO). The Mb gene. The evolution of proteins: Mb and Hb as examples. The most important hemoglobins. The role of the globin winding. Oxy and deoxyhemoglobin. The binding of oxygen by Mb and Hb. Saturation curves of Mb and Hb with oxygen. Allosteric proteins. The allosteric behavior of Hb and its regulatory mechanism. The homotropic and heterotropic allosteric effectors. The role of pH, carbon dioxide and 2.3 bisphosphoglycerate on the oxygen bond. The Bohr effect. The Hill coefficient. The interactions between the subunits of Hb. From deoxy- to oxy Hb: the allosteric transition. The saline bonds. The Bohr effect. The transport functions of the Hb. Fetal hemoglobin. The abnormal and pathological Hbs. Sickle cell anemia: the characteristics of this molecular disease. The HbS. The role of the fingerprint in identifying the mutation. The sickle cell tract. Sickle cell anemia and malaria: the meaning of balanced polymorphism. The Hammersmith Hb. The α- and β-thalassemias.TEACHING UNIT 2 - "Enzymology and Elements of Molecular Biology"
ENZYMOLOGY
Introduction to enzymology. Classification of enzymes. The prosthetic groups. Structure-function relationship in enzymes. The enzyme-substrate complex and the transition state diagram. The general properties of enzymes and their dosage. The general characteristics of enzymes. Catalytic mechanisms and their efficiency. Experimental measurements and analysis of kinetic data. The enzyme kinetics. Methods for obtaining kinetic data of reactions to a substrate, calculation of kinetic parameters and their meaning (KM, VMAX, Michaelis Menten equation and Lineweaver-Burk Plot). Reversible and irreversible enzymatic inhibitions. Enzymatic methods of analysis. Factors that influence enzymatic activity: pH, temperature, etc. The macromolecule-ligand balance. Regulatory enzymes. Substrate level regulation. Feedback regulation. The allosteric regulation. Allosteric models and their applications. Examples of allosterically regulated enzymatic activities. Covalent bond regulation. Examples of covalently regulated enzymatic activities. The proteolytic enzymes. The four main classes of proteolytic enzymes. The serine proteases. Blood clotting. Recombinant DNA technology applied to enzymes.THE MOLECULAR BIOLOGY OF PROKARYOTS
The two types of nucleic acids: ribonucleic acid (RNA) and deoxyribonucleic acid (DNA). DNA as a carrier of genetic information. Experiments showing that genes are made up of DNA. The nitrogenous base composition of DNA and Chargaff's rules. The double helix theory. The chemical structure and physical properties of DNA and RNA. The melting temperature (Tm), denaturation, the size of the DNA molecules. The semi-conservative nature of DNA replication. The flow of genetic information. The gene-protein colinearity. DNA replication in prokaryotes. DNA polymerases in E. coli. Enzymes and protein factors involved in replication. The stages of replication: beginning, lengthening and termination. DNA transcription in prokaryotes. The RNA polymerase in E.coli. The beginning of transcription and its regulation. The promoting sites. The consensus sequence. The term of the transcription factor rho-independent and factor-dependent. The messenger RNA. Protein synthesis in prokaryotes. The RNA transfer. The unusual nitrogenous bases of transfer RNA. Activation of amino acids. The aminoacyl-t-RNA synthetases. The genetic code and its important characteristics. The oscillation hypothesis. The ribosome and its complex molecular machine. The polyribosomes. The stages of protein synthesis: beginning, lengthening and termination. The fidelity of protein synthesis. Post-translational modifications of polypeptide chains.THE MOLECULAR BIOLOGY OF THE EUKARYOTS
Genes and DNA of eukaryotes. The genome of eukaryotes. Definition of gene. Structural genes and regulatory sequences. The repetitive sequences. Discontinuous genes: introns and exons. The splicing. The physical and chemical structure of chromatin. Basic histone proteins, nucleosomes and higher order regular chromatin structures. DNA replication in eukaryotes. The assembly of nucleosomes. Eukaryotic DNA polymerases. Transcription in eukaryotes. Eukaryotic RNA polymerases. General characteristics of the promoters. The transcription factors. The stimulatory sequences (enhancers). The stages of transcription. The maturation of messenger RNA. The structure of ribosomes in eukaryotes. The stages of protein synthesis in eukaryotes.THE EVOLUTION
The evolutionary theory of the cell. Molecular evolution. The production of simple biological molecules under prebiotic conditions. Chemical evolution. Replication through complementarity. Cellular compartmentalization. The evolution of organisms.TEXTBOOK
Nelson and Cox, Lehninger Principles of Biochemistry. MacMillan learning Ed.
link: https://www.macmillanlearning.com/college/us/product/Lehninger-Principles-of-Biochemistry/p/1319228003