PROTEIN SCIENCE AND BIOTECHNOLOGY

Menico Rizzi (10 h – 1.66 ECTS)

He received a PhD in Molecular Biotechnologies at University Cattolica “Sacro Cuore”. He was visiting scientist/professor at the University of York (UK), University of Kyoto (JP) and at the Japanese National Institute for infectious disease (Tokyo, JP). He is currently full professor of Biochemistry at UPO. He is member of the scientific committee of several National and International Congresses including FEBS and FASEB meetings and lecturer in International PhD Schools supported by UNESCO. Past President of the “Protein Chemistry” division of the Italian Society of Biochemistry and expert member for biological sciences of the Italian National Agency for the evaluation of University and research (ANVUR). Prof. Rizzi joined the International non-proprietary names program of the World Health Organization at the beginning of 2016. He is an expert in structural biology and enzymology and coordinates a group investigating proteins of medical interest, with a particular focus on poverty-linked diseases.

Academic lecturers: 4

Guest lecturers: 6

Laboratory: 0

Davide Ferraris (2 h – 0.33 ECTS)

After graduating in Chemistry at the University of Turin (Italy), he received in 2008 a PhD in Infection Biology at the Medical School of Hannover (Germany) with an experimental thesis in Structural Biology at the Helmholtz Centre for Infection Research (HZI, Braunschweig, Germany). He is researcher at the Department of Pharmaceutical Science at the University of Eastern Piedmont (Novara, Italy) in the research group directed by Prof. Menico Rizzi. His research interests include the structural and functional elucidation of virulence factors of M. tuberculosis and the development of protein technologies for biotechnological applications.

Academic lecturers: 2

Guest lecturers: 0

Laboratory: 0

Franca Rossi (2 h – 0.33 ECTS)

Upon graduation in Biological Sciences at the University of Pavia (Italy) in 1992, she worked for several years as research fellow first at the Italian CNR (IGBE-CNR, Pavia; Italy) and then abroad (INSERM, Nice; France), acquiring a broad knowledge of technologies for the functional characterization of proteins of medical and biotechnological relevance. Skilled in recombinant protein production and protein-protein interactions analysis, she was involved in multi-disciplinary projects, as the reference team member for macromolecular interactions investigations. In 2001, she joined the Biochemistry Unit of the Department of Pharmaceutical Sciences of the University of Eastern Piedmont (DSF-UPO, Novara; Italy), where she contributed her expertise to the pre-existing high-standard know-how in structural biology, thus creating a new blend of complementary skills that resulted in the establishment of new research lines. In 2002, she obtained a permanent position as Researcher of DSF-UPO, where she teaches the “Applied Biochemistry” and “Molecular Biology” courses. Her current projects are mainly focused on studying the structure-function relationship of single proteins and macromolecular complexes from different sources, including Mycobacterium tuberculosis, the causative agent of tuberculosis in humans and the malaria vector Anopheles gambiae, as well as human enzymes involved in tryptophan degradation.

Academic lecturers: 2

Guest lecturers: 0

Laboratory: 0

Riccardo Miggiano (4 h – 0.66 ECTS)

He is a Researcher of the Biochemistry group at the Department of Pharmaceutical Sciences of the University of Piemonte Orientale. He received the master degree in Pharmaceutical Chemistry and Technology at the University of Parma and then the PhD in Pharmaceutical and Food Biotechnologies at the University of Piemonte Orientale. Dr. Miggiano was visiting PhD student at the Institute of Biosciences and BioResources of CNR in Naples and at Luis Serrano’s group at the Centre for Genomic Regulation in Barcellona where he get familiar with innovative biochemical assays for testing enzyme activity and for protein/protein interaction analysis. In 2018, he conducted part of his research at the City University of New York (CUNY). During the experience at CUNY he performed cryo-EM studies on protein complexes involved in DNA repair. His activity resulted in 15 published papers and 17 protein structures deposited in the Protein Data Bank. Moreover, Dr. Miggiano is a co-founder of the IXTAL spin-off (www.ixtal.it), a biotech company that operates in the field of protein science. His research activity mainly focus on i) the biochemical and structural characterization of individual enzymes involved in alkylated-DNA repair in Mycobacterium tuberculosis (Mtb); ii) the identification and characterization of macromolecular complexes participating to the maintenance of Mtb genome stability; iii) protein engineering studies for the design of self-labeling fluorescent protein-tag.

Academic lecturers: 4

Guest lecturers: 0

Laboratory: 0

Title Protein Science and biotechnology (3 ECTS)
Program

 

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.

Rizzi M. – 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

The beauty of vitamins – The biochemistry of vitamins in physiology with a special focus on aging. Vitamins in cosmetics: example of their use and effects.

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

Dynamics of genome integrity: from DNA damage response to cellular senescence and death – The chemistry of different DNA-damaging agents; the molecular biology of DNA damage response and its correlation with aging and cell death.

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

Nomenclature for Medicines: the case of the International Nonproprietary Name (INN) system. The lecture will focus on the INN nomenclature scheme for chemical and biological medicines as implemented by the World Health Organization. The topics covered by the School of INN, a recently launched WHO global initiative, will discussed.

Rizzi M. – 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 held by Prof. Rizzi.
Teaching methods 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.

– Each student has to select one paper amongst the four that we will be communicated and will be asked 1-2 questions related to the selected paper the same day he/she takes the exam (after the written part defined above). Total grade for this part is a maximum of 6 points.

The overall grade will be the sum of the two parts.

 

TITLE

Protein Science and biotechnology (3 ECTS)

 

PROGRAM

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.

Rizzi M. – 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

The beauty of vitamins – The biochemistry of vitamins in physiology with a special focus on aging. Vitamins in cosmetics: example of their use and effects.

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

Dynamics of genome integrity: from DNA damage response to cellular senescence and death – The chemistry of different DNA-damaging agents; the molecular biology of DNA damage response and its correlation with aging and cell death.

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

Nomenclature for Medicines: the case of the International Nonproprietary Name (INN) system. The lecture will focus on the INN nomenclature scheme for chemical and biological medicines as implemented by the World Health Organization. The topics covered by the School of INN, a recently launched WHO global initiative, will discussed.

Rizzi M. – 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 held by Prof. Rizzi.

TEACHING METHODS

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.

– Each student has to select one paper amongst the four that we will be communicated and will be asked 1-2 questions related to the selected paper the same day he/she takes the exam (after the written part defined above). Total grade for this part is a maximum of 6 points.

The overall grade will be the sum of the two parts.

Last modified: November 06, 2019