PROTEIN SCIENCE AND BIOTECHNOLOGY
Riccardo Miggiano (14 h – 2.34 ECTS)
Guest lecturers: 6
Laboratory: 0
Davide Ferraris (2 h – 0.33 ECTS)
Guest lecturers: 0
Laboratory: 0
Franca Rossi (2 h – 0.33 ECTS)
Guest lecturers: 0
Laboratory: 0
Title | Protein Science and biotechnology (3 ECTS) |
Program
|
Basic principles of protein structure: relevance in drug discovery Miggiano R. – 4 hours Biophysical methods for the analysis of protein-protein and protein-ligand ineraction Miggiano R. – 2 hours Collagen in cosmetics: sources, uses and modifications Ferraris D. M. – 2 hours Dynamics of genome integrity: from DNA damage response to cellular senescence and death Rossi F. – 2 hours Dysregulated antioxidant systems and anti-oxidative therapeutic strategies in dermatology Miggiano R. – 2 hours Proteostasis, aging proteome and key-targets for innovative dermo-cosmetics Guest lecturer – 4 hours The sustainable beauty: bioplastic in the cosmetic industry Guest lecturer – 2 hours |
Textbooks |
– Molecular biology of the Cell (Alberts et al.); ISBN 9780815344322 – Lehninger Principles of Biochemistry (Nelson & Cox); ISBN 1464109621 (or 9781464109621) – Textbook of Structural Biology (Anders Liljas et al.); ISBN: 978-981-277-208-4) (or 978-981-4365-40-6, ebook) |
Objectives | The course aims to provide the rudimental of protein science and biotechnology and elaborate around the central concept of protein structure-function relationship. Selected biotechnological techniques used in protein science will be reviewed and examples of proteins of pharmaceutical interest for translational cosmetic and dermatological science will be presented. |
Prerequisites | Basic knowledge of molecular biology (the central dogma in biology; basics of DNA replication, transcription an mRNA translation into proteins) and protein biochemistry. Further information and reading materials will be suggested at the introductory lecture. |
Teaching methods | Ex-cathedra lectures and seminars held by guest lecturers. |
Expected Results |
Knowledge and understanding: On completion of the course, the student should be able to: – describe the chemical composition, the main post-translational modifications and the different levels of protein structure. – explain the proteins structure-function relationship; – describe how enzymes work and how the enzyme activity could be affected by the presence of enzyme co-factors; – explain how enzymes can be used for biotechnological purposes; – describe how the DNA repair systems control gene expression quality; – describe the main cellular anti-oxidant systems; Skills and abilities: On completion of the course, the student should be able to Communication and general learning skills: On completion of the course, the student should be able to: – communicate appropriately about subjects in the field, by giving short talks and/or in the form of written assays. – work in a group, and organize collaborative literature research and data mining. – analyse new problems, also by retrieving additional information. – acquire further knowledge about subjects in the field, by scheduling his/her study activities independently. – apply critical and independent thinking in further studies and work. |
Exam modality |
The exam consists of: – A set of 24 questions (multiple choice) related to the different topics covered in the lectures. Each correct answer gives 1 point. All other possibilities is 0 point, i.e. there will be no negative grades. – 1 open-ended question (7 points). |
TITLE
Protein Science and biotechnology (3 ECTS)
Basic principles of protein structure: relevance in drug discovery
The basic principles behind protein folding and structure-function relationship that are relevant in drug discovery for both chemical and biological medicines.
Miggiano R. – 4 hours
Biophysical methods for the analysis of protein-protein and protein-ligand ineraction
Protein crosstalks as well as protein-ligand interactions play essential roles in many biological processes including signaling pathways, transcriptional regulation and numerous other metabolic reactions. In order to understand the role of such protein interactions in biological processes it is important to investigate the interaction dynamics describing the stoichiometry of the complexes, the binding free energy and their binding cooperativity as inter-molecular communication.
Miggiano R. – 2 hours
Collagen in cosmetics: sources, uses and modifications
The structure and function of collagen and its natural sources, and how collagen can be modified for the use in different cosmetic and surgical applications.
Ferraris D. M. – 2 hours
Dynamics of genome integrity: from DNA damage response to cellular senescence and death
Rossi F. – 2 hours
Dysregulated antioxidant systems and anti-oxidative therapeutic strategies in dermatology
The oxidative stress and anti-oxidative strategy in dermatology, with examples of various cutaneous disorder related to oxidative stress and aberrant antioxidant system.
Miggiano R. – 2 hours
Proteostasis, aging proteome and key-targets for innovative dermo-cosmetics
The role of proteostasis in longevity; the functional decline of proteostasis machinery as hallmark of aging; the innovative biomarkers for a development of new therapeutic or dermo-cosmetic solutions.
Guest lecturer – 4 hours
The sustainable beauty: bioplastic in the cosmetic industry
Description of the most recent research results on bio-economy sector for the development of high performance micro-beads for the cosmetic sector and biodegradable in water and soil for the protection of the environment, in compliance with the most recent regulations.
Guest lecturer – 2 hours
TEXTBOOKS
– Molecular biology of the Cell (Alberts et al.); ISBN 9780815344322
– Lehninger Principles of Biochemistry (Nelson & Cox); ISBN 1464109621
(or 9781464109621)
– Textbook of Structural Biology (Anders Liljas et al.); ISBN: 978-981-277-208-4) (or 978-981-4365-40-6, ebook)
OBJECTIVES
The course aims to provide the rudimental of protein science and biotechnology and elaborate around the central concept of protein structure-function relationship. Selected biotechnological techniques used in protein science will be reviewed and examples of proteins of pharmaceutical interest for translational cosmetic and dermatological science will be presented.
PREREQUISITES
Basic knowledge of molecular biology (the central dogma in biology; basics of DNA replication, transcription an mRNA translation into proteins) and protein biochemistry. Further information and reading materials will be suggested at the introductory lecture.
TEACHING METHODS
Ex-cathedra lectures and seminars held by guest lecturers.
EXPECTED RESULTS
Knowledge and understanding:
On completion of the course, the student should be able to:
– describe the chemical composition, the main post-translational modifications and the different levels of protein structure.
– explain the proteins structure-function relationship;
– describe how enzymes work and how the enzyme activity could be affected by the presence of enzyme co-factors;
– explain how enzymes can be used for biotechnological purposes;
– describe how the DNA repair systems control gene expression quality;
– describe the main cellular anti-oxidant systems;
– describe how proteins are turned over in living cells and how the processes are regulated normally and upon exposure to physical and chemical stress (e.g. UV, oxidation).
Skills and abilities:
On completion of the course, the student should be able to
use the acquired theoretical knowledge to explain the biochemical background of different biological phenomena or processes.
Communication and general learning skills:
On completion of the course, the student should be able to:
– communicate appropriately about subjects in the field, by giving short talks and/or in the form of written assays.
– work in a group, and organize collaborative literature research and data mining.
– analyse new problems, also by retrieving additional information.
– acquire further knowledge about subjects in the field, by scheduling his/her study activities independently.
– apply critical and independent thinking in further studies and work.
EXAM MODALITY
The exam consists of:
– A set of 24 questions (multiple choice) related to the different topics covered in the lectures. Each correct answer gives 1 point. All other possibilities is 0 point, i.e. there will be no negative grades.
– 1 open-ended question (7 points).
Last modified: September 13, 2023