The aim of this course is for students acquire the fundamental concepts of structural and metabolic biochemistry. The main purpose of the course is to instill a fundamental understanding of the biochemical and molecular mechanisms of cellular metabolism in order to provide students the information needed to face the subsequent subjects.

In particular, the chemical reactions that allow living organisms to obtain energy via the oxidation of organic molecules absorbed through diet intake and transformed into their constituents will be analysed. Moreover, the regulatory mechanisms of these metabolic pathways in different pathophysiological conditions will be discussed.

Introduction to Biochemistry.

Amino acids, peptides and proteins. 

General structure, properties and classification of the amino acids that make up proteins.

Levels of Protein Organization: primary, secondary, tertiary and quaternary structures.

Native conformation of proteins and factors contributing to the protein conformation stability.

Structure and features of the peptide bond.

Secondary structures of proteins: a-helix, β-sheet, folds and loops.

Fibrous proteins (α-keratin and collagen) and globular proteins. 

Protein motifs and domains.

Protein denaturation and folding.

Diseases caused by defects in protein folding: amyloidosis and prion diseases.

Myoglobin and hemoglobin.

Heme: structure and properties.

Myoglobin: structure and function. Oxygen binding curve to myoglobin.

Hemoglobin: structure and function. Oxygen binding curve to hemoglobin. Cooperative bond. Bohr effect. Role of 2,3-bisphosphoglycerate (BPG). Sickle cell anemia.

Introduction to enzymes. International classification of enzymes.

How enzymes work.

Basic aspects of enzymatic kinetics. Michaelis-Menten kinetics. Km and Vmax. Factors affecting enzyme activity.

Reversible and irreversible enzyme inhibition.

Allosteric enzymes.

Structure and function of carbohydrates. Monosaccharides and disaccharides. Derivatives of hexoses. Glycated hemoglobin. Reducing sugars. Polysaccharides. Homopolysaccharides: Starch, Glycogen and cellulose. Heteropolysaccharides: peptidoglycan, glycosaminoglycans. Glycoconjugates: proteoglycans, glycoproteins and glycolipids.

Structure and function of lipids.

Lipid storage: fatty acids and triacylglycerols. Nomenclature of the most common fatty acids. ω-3 and ω-6 fatty acids. Hydrogenated fats. Structural membrane lipids, glycerophospholipids, sphingolipids, glycolipids and sterols.

The signal transduction pathways. Basic aspects of signal transduction. G protein-coupled receptors and second messengers. Receptors with tyrosine kinase activity. Controlled ion channel.

Introduction to metabolism.

Mentions of digestive processes: conversion of a meal into molecules usable by the cell.

Basic knowledge of metabolism: The regulation of metabolic processes. The free energy. The transfer of phosphoric groups. Structure and function of ATP. The biological reactions of redox. The electron carriers (NADH, NADPH and FADH2).

Glycolysis, gluconeogenesis and the pentose phosphate pathway.

Reactions of glycolysis and gluconeogenesis.

Metabolic fate of pyruvate: lactic and alcoholic fermentation and oxidation to acetyl-CoA.

Coordinated regulation of glycolysis and gluconeogenesis.

Oxidation of glucose via the pentose phosphate pathway.

Citric acid cycle. Production of acetylCoA. Pyruvate dehydrogenase complex. Reactions of the citric acid cycle. Functions, energy balance and regulation of the citric acid cycle.

Fatty acid catabolism.

Digestion, mobilisation and transport of fatty acids. Fatty acid oxidation. The ketone bodies.

Oxidation of amino acids and urea production.

Metabolic fate of amino groups. Nitrogen excretion and the urea cycle. Pathways of degradation of amino acids.

Oxidative phosphorylation.

The mitochondrial respiratory chain. The proton motive force. ATP synthase. The synthesis of ATP. Shuttle systems (shuttle) of malate-aspartate and glycerol 3-phosphate. Regulation of oxidative phosphorylation.

Glycogenolysis and glycogen synthesis.

Lipid synthesis.

Fatty acid biosynthesis: stages and regulation. Biosynthesis of triacylglycerols and phospholipids. Cholesterol: biosynthesis (main steps), regulation and transport. Plasma lipoproteins.

Biosynthesis of amino acids. Nitrogen fixation. Incorporation of ammonia into biomolecules. Mention to the biosynthesis of amino acids.

Metabolism integration.

Metabolic interrelationships between the various organs. Fasting-eating cycle. Hormonal regulation.

As reported in the teaching regulations for the master's degree in Pharmacy, students are strongly advised to follow the sequence of the courses laid out in the study plan. Furthermore, in order to allow an adequate learning process, students must  pass the exam of "Animal Biology"  before taking the "General an Molecular Biochemistry" exam.

Knowledge and understanding: students will have to demonstrate that they have acquired a thorough knowledge of the structure and function of biological macromolecules and the basic principles of the metabolism. Furthermore, they will have to be familiar with the regulation strategies of the metabolism itself, of the specific biochemical processes of the various tissues and organs, in addition to their integration and hormonal regulation.

Applied knowledge and understanding: students must demonstrate their ability to establish correlations between structure and function of biomolecules and links between the different topics covered.

Autonomy of judgement: students will have to demonstrate their ability to critically analyse and discuss the information acquired.

Communication skills: students will have to communicate the skills acquired in a clear and effective way, by using the appropriate terminology relating to the topics covered.

Ability to learn: students will have to demonstrate good learning skills which will allow them to use the knowledge acquired during the biochemistry course and in subsequent courses.

The teaching material prepared by the lecturer in addition to recommended textbooks (such as for instance slides, lecture notes, exercises, bibliography) and communications from the lecturer specific to the course can be found inside the Moodle platform › blended.uniurb.it

No activities to support teaching are  planned

Teaching

Frontal Lessons

Attendance

Attendance is recommended, but not mandatory.

Course books

David L Nelson Michael M Cox. Fondamenti di biochimica di Lehninger. I Ed. italiana condotta sulla VII ed.americana. A cura di Edon Melloni (2021)

Jeremy M Berg, John L Tymoczko, Gregory J. Gatto, Lubert Stryer. BIOCHIMICA. VIII ed. italiana condotta sulla IX ed. americana (2020)

Assessment

The exam consists of a written test with questions covering the entire course program.

There are 2 ongoing written tests which replace the final written test. The dates of the ongoing tests will be posted during the course. In this case, the final mark will be calculated on the average of the two marks obtained  on both tests, but only if both results are ≥ 18/30. Those who do not obtain a passing mark on both partial tests must take the full exam.

The written test consists of a series of multiple-choice questions (you must indicate the only correct answer among the choices) and open questions. For multiple choice questions, each correct answer is worth 1 point, each answer left blank 0 points, and each incorrect answer is worth -0.25 points. For the open-ended questions, scores will range from -0.25 to 1 depending on the appropriateness of the answer.

Disability and Specific Learning Disorders (SLD)

Students who have registered their disability certification or SLD certification with the Inclusion and Right to Study Office can request to use conceptual maps (for keywords) during exams.

To this end, it is necessary to send the maps, two weeks before the exam date, to the course instructor, who will verify their compliance with the university guidelines and may request modifications.

Assessment

The exam consists of a written test with questions covering the entire course program.

The written test consists of a series of multiple-choice questions (you must indicate the only correct answer among the choices) and open questions. For multiple choice questions, each correct answer is worth 1 point, each answer left blank 0 points, and each incorrect answer is worth -0.25 points. For the open-ended questions, scores will range from -0.25 to 1 depending on the appropriateness of the answer.

Disability and Specific Learning Disorders (SLD)

Students who have registered their disability certification or SLD certification with the Inclusion and Right to Study Office can request to use conceptual maps (for keywords) during exams.

To this end, it is necessary to send the maps, two weeks before the exam date, to the course instructor, who will verify their compliance with the university guidelines and may request modifications.