Biochemistry

This course presents the essentials of Biochemistry. It covers the structures, functions, and interactions of biomacromolecules, including proteins, lipids, carbohydrates, DNA, and RNA, which perform many of the activities associated with life. The course provides insight in the specificity and action of enzymes, the bio catalysts of the cell. Further, it explains metabolic pathways that result in the generation of ATP, the major energy currency of the cell. Finally recent biochemical understandings on genome editing are presented that revolutionize treatment of diseases at the level of correcting mutated genes (gene therapy). Prerequisites for this course are an introduction to biology or chemistry.

This course covers the basic principles of biochemistry. Topics include amino acids, primary structures of proteins, properties of enzymes, carbohydrates, and lipids and membranes. 

This class covers the main routes of metabolism of sugars, lipids, and amino acids. Subjects include glycolysis, fermentation, oxidative decarboxylation; Krebs cycle, gluconeogenesis, and the biosynthesis and degradation of fatty acids and triglycerides; roles of coenzymes, coupled with enzyme catalysts, and how they work; and enzymology and kinetics, focusing on rates of reaction for enzymes in metabolic reactions.

In this course, students consider the ways of identifying novel compounds for development and the processes which take place before such compounds are released onto the market following its introduction into clinical practice. The course includes an opportunity for group project work on the development of a specific drug and series of case studies looking at the criteria which contributes to successful outcome in a drug development program. 

The course has four main focuses. It begins with an overview of the biotechnology and pharmaceutical industry with introduction on the biotech-pharmaceutical industry, market overview, and aspects of drug development. Second, the course offers an introduction of drug development focusing on small-molecule drug/anticancer drug, drug development and translational research, antibody and plant drug development, and immunotherapy. The third section is on research and development: preclinical, focusing on animal application, pharmacokinetics, pre-formulation and formulation development of new drugs, clinical trials, small molecule drug development. The final section covers industry business outline focusing on the biotech industry, biomedical research, development of patent protection, biotech economy.

This course is part of the Laurea Magistrale degree program and is intended for advanced level students. Enrollment is by permission of the instructor. The course is aimed at the comprehension of the main biological process at a molecular level: structures, properties and function of biomolecules, molecular mechanism, route and law of bio- transformations, the base of microbiological physiology and genetics, enzymatic catalysis, and fermentation. The course is also aimed at the comprehension and application of the knowledge and acquired skills in the biochemical interaction among organisms and environment.

The course content is divided into two parts:

Part 1: Biochemistry

• 1. Macromolecules: Amino Acids, Carbohydrates, Lipids
• 2. Protein structure: Primary, secondary, tertiary, quaternary
• 3. Plant biochemistry: Photosynthesis: light reactions, carbon fixation, synthesis of sugars, bacterial photosynthesis.
• 4. Catabolism of sugars: Glycolysis, Krebs cycle, respiration, chemiosmosis.
• 5. Enzyme catalysis: Substrate specificity, catalytic mechanisms, and enzyme kinetics

Part 2: Biochemical Methodologies

This part consists of experimental laboratory course, which introduces the students to the basic approaches for the determination of proteins amount, separation, and identification. During the practical laboratory, the following experimental activities are foreseen:

1. Determination of protein content by using a colorimetric assay;

2. Separation of a mixture of known proteins by using a chromatographic analysis;

3. Identification of purified proteins using spectrophotometric and electrophoretic techniques.