The course covers the physics of colloidal dispersions. In a first section, the course provides the basic definition of colloidal dispersion and stability. Particular emphasis is provided on the attraction forces (i.e. Van der Waals) and how they can be translated from small molecules up to complex systems. The understanding of the stabilization methods, including electrostatic and steric stabilization, is another goal of the course. These principles are referred first to polymer systems and then in the description of protein aggregation.

Lectures and exercise sessions will allow students to:

- know and discuss about interactions between colloidal particles

- know and discuss about kinetic of aggregations in colloidal systems

- know and discuss about manufacture and the formulation of therapeutic proteins

The frontal lessons are supported by a laboratory project, which gives the possibility to the students to deal with a real case study. In this way, the students can uderstand the practical criticalities in handling colloidal systems and the complex interactions with the macroscale environment.

The course covers the physics of colloidal dispersions and in particular the following aspects:

- Interactions between colloidal particles: van der Waals, electrostatic and hydrodynamic forces

- Colloidal stability

- Kinetic models for aggregation in colloidal systems (population balances)

- Structure, size and morphology of aggregates and their experimental characterization

- Definition of gel phase and gelation kinetics

- Role of fluid dynamics in colloid aggregation

- Aggregation kinetic models in laminar and turbulent flows

In the last part of the course, the stability of protein solutions is considered with reference to the following aspects: protein structure and unfolding processes; aggregation during the manufacture and the formulation of therapeutic proteins; aggregate characterization (from globular to fibrils); effect of the environmental physicochemical conditions on the protein propensity to aggregate; technologies for protein aggregate removal.

The lectures are supported with numerical exercises, where population balances to describe the colloid aggregation processes are solved with the use of Matlab.

A laboratory project, lasting the entire duration of the course, is assigned to the students, divided in work teams of maximum of 4 people each. In particular, they are asked to solve a practical case study combining the modelling of the process, the design of the experiments supported by an extensive literature research and finally the conduction of experiments in a chemical laboratory to produce a colloidal system and validate its functionality. At the end of the project, each work team is required to gather and discuss the results obtained with a presentation.

Students are required to know the basic principles of physical chemistry and to possess basic programming skills with Matlab.

The students will be evaluated based on the results of the project as well as on the knowledge acquired during the frontal lessons.

In particular, the students, organized in work teams of maximum 4 people, will work on a practical case study dealing with colloidal stability and colloid aggregation assigned at the beginning of the course. For the evaluation, each work team is required to produce and discuss a presentation of the work and the results obtained in the project. The students are required to have properly understood and master the case study they worked on, to master the knowledge (including kinetic scheme, mechanism of the process and role of the different compounds) of the processes the used and to critically analyse the results obtained. The discussion of the results of the project accounts for 50% of the final grade.

The remaining 50% can be acquired with an indivdual oral examination on the topics covered during the frontal lessons. The students should demonstrate to master:

• principles of colloidal stability
  
• role and extension of Van der Waals forces between colloids
• methods for colloid stabilization: electrostatic stabilization and steric stabilization
• controlled aggregation
• protein stability and aggregation