Objectives:

Understanding protein aggregation is important as this process is

implicated in many human diseases such as Alzheimer's, Parkinson's,

prions and Type II diabetes. Therefore, for designing therapeutics, the

exact mechanism of protein aggregation should be clear. Moreover,

protein aggregation is an important aspect for regulatory agencies and

the biopharmaceutical industry for developing protien/peptide drugs

for human welfare. Protein aggregation during drug formulation often

introduces adverse effect in the patients. For example, protein

aggregation not only leads to its loss-of-function but also leads to

gain of adverse functions such as toxicity and immunogenicity due to

aggregation. Hence, protein aggregation often causes roadblock for

the formulation of protein/peptides therapeutics.

This course will introduce mechanism and consequences of protein

aggregation associated with human diseases as well as the

formulation of biotherapeutics. The course will also discuss the

experimental strategies for predicting and quantifying protein

aggregation.

Contact: Prof. Samir K. Maji (samirmaji@iitb.ac.in),

Professor, Department of Biosciences and

Bioengineering, IIT Bombay, Powai,

Mumbai – 400076, Dial: (+91 22) 2576

7774/4741

REGISTRATION:

http://portal.iitb.ac.in/ceqipapp/

Note: No income tax is to be deducted at source from the

course fee, as IIT Bombay is exempt from the same. The course

fee includes course material, lunch and coffee/tea.

Protein aggregation:

Posing human diseases to formulation issues

Course coordinator: Prof. Samir K. Maji, IIT Bombay

Accommodation and boarding:

For outstation registrants, we might have a limited number of

accommodation (depending upon availability and preferably

twin share basis) available in the Institute Guest house, on the

basis of additional payment. Please send an advance request. If

you really need single room occupancy, please mention the same

in your request

Lunch and other refreshments will be provided at the venue

itself.

Program fee:

Industry Participants: 30000 (including 18% GST)

Academia: 20000 (including 18% GST)

Students: 15000 (including 18% GST)

International participants: 40000 (including 18% GST)

Course Content:

1. Principle of protein folding in vitro and in vivo

2. Protein structure and structure-function relationship

3. Principle involved in protein misfolding and aggregation

4. Techniques in studying protein folding, misfolding and aggregation

5. Analytical techniques for predicting and analyzing protein aggregates in solution

6. Case studies of protein aggregation associated with disease, function and drug formulation

7. Demonstration of structural and biophysical techniques for studying protein aggregation in

solution.

Course evaluation: All participants, who will complete the entire course, will be awarded with Course Participant Certificate.

Teaching faculty: Possible teaching faculty members include IIT Bombay and TIFR, Mumbai who are working on protein structure,

folding and aggregation. Intended audience:

1. Students/faculties who would like to start their research in protein chemistry and biophysical characterization of protein and protein

folding.

2. Students/faculties interested in studying protein aggregation associated with various human diseases and protein formulations

3. Scientists in academia and industries working with protein/peptide therapeutics and formulation.

Duration: 17-21 September 2019

Venue: Indian Institute of Technology-Bombay, Powai

Introduction:

Proteins are the workhorses in cellular machinery and

perform a wide array of functions in our body for our

survival. However, for proteins to function properly, they

must be folded correctly into a three-dimensional

conformation. During in-vivo protein folding, non-native

conformers of protein can also arise due to various reasons

such as alteration in primary structure (e.g., mutation),

altered post-translational modifications and environmental

conditions, which may lead to protein aggregation and

diseases. Furthermore, the partial unfolding of proteins can

also happen due to thermal and oxidative stress. All these

can induce non-native conformations of the protein, which

can oligomerize and form protein aggregates. Protein

aggregates can be either amorphous or can have ordered

structure like amyloid fibrils. The accumulation of such

stable and insoluble protein aggregates is often linked to

neuronal degeneration and other protein deposition.

.