Unit GENERAL APPLIED AND CLINICAL BIOCHEMISTRY
- Course
- Pharmaceutical chemistry and technology
- Study-unit Code
- A003594
- Curriculum
- In all curricula
- Teacher
- Carmela Conte
- Teachers
-
- Carmela Conte
- Michela Codini (Codocenza)
- Hours
- 40 ore - Carmela Conte
- 40 ore (Codocenza) - Michela Codini
- CFU
- 10
- Course Regulation
- Coorte 2025
- Offered
- 2026/27
- Learning activities
- Caratterizzante
- Area
- Discipline biologiche e farmacologiche
- Sector
- BIO/10
- Type of study-unit
- Obbligatorio (Required)
- Type of learning activities
- Attività formativa monodisciplinare
- Language of instruction
- Italian
- Contents
- Knowledge of the main biological macromolecules and the relationship between structure and function.
Metabolisms and related clinical aspects. Main biochemical methods for the study of macromolecules. - Reference texts
- - I principi di Biochimica di Lehninger Di
Nelson and Cox- Zanichelli Editore
- Biochimica Medica di Siliprandi e Tettamanti, Piccin editore. - Educational objectives
- At the end of the study the student will be able to acquire the basic knowledge of the fundamental principles of General, applied and clinical biochemistry.
- Prerequisites
- The teaching of general, applied and clinical biochemistry aims to address topics that the student will be able to learn if he has acquired the basic knowledge of inorganic and organic chemistry. In order to understand the contents of the course, it is essential that the student has acquired the fundamental notions on the structure of the main macromolecules and chemical bonds as well as their behavior during metabolic
- Teaching methods
- The teaching will be carried out through lectures in the classroom covering all the topics of the program.
- Other information
- none
- Learning verification modality
- The assessment includes an oral exam during which the student will have to answer questions regarding the topics covered during the lessons. During the interview the student will have to demonstrate coherence with the proposed question, clarity of presentation and adequate scientific terminology
- Extended program
- • Introduction to Biochemistry
• Water and weak interactions in aqueous systems. Ionization of water, weak acids, and weak bases. Biological buffers.
• Fundamental principles of thermodynamics
• Structure and function of the main biomolecules.
• Nucleic acids: Nucleotides. Main structures and functions of DNA and RNA.
• Cell membranes and transmembrane transport. Membrane phospholipids. Membrane proteins. Asymmetry of the plasma membrane. The erythrocyte membrane. Spectrin and glycophorin. Transmembrane transport: classification. Selective permeability. Passive transport and active transport. ATPases. Molecular model of the Na¿/K¿ ATPase.
• Carbohydrates: monosaccharides, disaccharides, and polysaccharides, and their implications in human biochemistry.
• Evaluation of carbohydrate metabolism. Diabetes. Glycated hemoglobin (HbA1c).
• Lipids: the main classes of lipids and their implications in human biochemistry. Fatty acids, acylglycerols, phospholipids, sphingolipids, glycolipids, and polyprenoids. Cholesterol. Lipids as signals and cofactors.
• Dyslipidemia. Plasma lipoproteins. Classification of lipoproteins based on density and electrophoretic migration. Apolipoproteins. Chylomicrons: structure, function, and fate. VLDL: structure, function, and fate. LDL: structure, function, and fate. HDL: structure and function. Atherosclerotic plaques.
• Amino acids. Classification and description of the twenty L-amino acids that make up proteins. Essential amino acids. Other amino acids of metabolic importance.
• Proteins. Functions performed by proteins in the human body. Protein structure. The peptide bond. Amino acid sequence. Secondary structure and description of alpha-helix, beta-sheet, and beta-turns. Structural motifs. Tertiary structure. Forces that stabilize the three-dimensional structure of proteins. Structural domains. Quaternary structure. Globular and fibrous proteins. alpha-keratins and silk fibroin. Methods for isolation of the proteins
• Protein folding. Factors determining the folding rate. Chaperonines. Protein misfolding. Protein aggregation, fibril formation.
• Amyloidosis and the molecular basis of human degenerative diseases.
• Post-translational modifications of proteins: glycosylation and phosphorylation. Lipid anchors. Signal peptides. Intracellular protein trafficking. Protein degradation. Ubiquitination system. The proteasome.
• Alterations in nitrogen compound metabolism: azotemia, uremia, uricemia.
• Connective tissue proteins. Collagen: triple helix, proline-hydroxyproline (role of vitamin C). Collagen diseases: rickets, scurvy. Elastin. Proteoglycans.
• Blood: complete blood count (hemogram). Wintrobe indices, hematocrit, white blood cell differential, ESR (erythrocyte sedimentation rate), iron, anemias.
• Globins. Structure of myoglobin and hemoglobin; structure-function relationships. Hemoglobinopathies.
• General principles of enzymes: Classification, catalytic activity, and structure; cofactors and prosthetic groups; holoenzyme and apoenzyme. Specificity of action. Chemical kinetics and thermodynamics. Formation of the enzyme-substrate complex. Characteristics of the active site. Enzyme kinetics. Michaelis-Menten model. Km and Vmax values.
• Units of measurement of enzyme activity.
Reversible enzymatic reactions. Effect of pH and temperature. Competitive, non-competitive, and irreversible inhibition. Drugs as enzyme inhibitors. Mechanisms of enzymatic catalysis. Acid-base catalysis. Covalent catalysis. Multienzyme complexes: pyruvate dehydrogenase.
• Enzyme regulation. Allosterism and cooperativity. Kinetics of allosteric enzymes. Cooperativity: concerted model and sequential model. Covalent regulation: reversible and irreversible. Signal amplification: blood coagulation. Compartmentalization. Control of the intracellular levels of enzymes.
• Clinical enzymology. Liver function indices.
• Biochemical action of vitamins. Vitamins utilized in metabolic pathways. Water-soluble and fat-soluble vitamins. Vitamin requirements and deficiencies. Coenzymes: structure and functions. Flavin and pyridine coenzymes. Folic acid. Thiamine. Lipoic acid. Biotin. Coenzyme A. Pyridoxine coenzymes. Vitamin B12 coenzymes.
• Signal transduction pathways. G-protein-coupled receptors (stimulatory and inhibitory G proteins). Tyrosine kinase receptors (insulin receptor) and signaling. The MAP kinase cascade. PI-3K pathway, receptors with guanylate cyclase activity. Biosignaling of steroid hormones.
• Methods for the isolation and study of proteins.
• Overview of Metabolism
• Carbohydrate Metabolism
• Citric Acid Cycle
• Electron Transport & Oxidative Phosphorylation
• Lipid Metabolism
• Ketone Body Metabolism
• Amino Acid Metabolism
• Nucleotide Metabolism - Obiettivi Agenda 2030 per lo sviluppo sostenibile
- Health and wellness.