Protein Therapeutics Exam

Study Notes

Proteins can be developed and produced to serve specific therapeutic functions, such as treating metabolic disorders, resisting infections, and arresting the spread of cancer.
Protein-based drugs can be grouped into four categories based on their pharmacological activity:
- Group 1: therapeutics with enzymatic or regulatory activity
- Group 2: therapeutics with special targeting activity
- Group 3: vaccines
- Group 4: diagnostic agents
Protein therapeutics have several advantages over small-molecule drugs, including:
- highly specific and complex functions that cannot be mimicked by simple chemical compounds
- less potential for interference with normal biological processes and adverse effects
- well-tolerated and less likely to elicit immune responses
- effective replacement treatment for diseases with mutated or deleted genes
- faster clinical development and FDA approval time
- unique form and function, allowing for far-reaching patent protection
The first recombinant protein used in therapy was insulin, which was purified from bovine pancreas in 1922 and later produced through genetic engineering in E. coli bacteria in 1978.

Storage, distribution, and understanding of protein properties (solubility, ability to enter the body, stability)
Degradation of proteins through lysosome, proteosome, or protease action
Immune response, which can neutralize the effect of the introduced protein or cause severe effects
Administration of active protein/enzyme in active conformation, considering post-translational modifications
Cost and time-consuming process of producing recombinant proteins
Ethical issues in investing in research for rare diseases versus widely distributed diseases

Enzymes are biological catalysts made of proteins that accelerate chemical reactions without heating.
Enzymes are:
- efficient, with acceleration rates of up to 17 orders of magnitude
- substrate-specific, with active sites that complement the substrate geometrically and electrostatically
- reaction-specific, catalyzing a single reaction
There are six classes of enzymes:
- Oxidation-reduction class (catalyzes oxidoreduction reaction)
- Group transfer class (catalyzes transfer of a chemical group from one molecule to another)
- Hydrolysis class (catalyzes reaction in which a molecule is broken down using a water molecule)
- Water-independent lysis class (catalyzes reaction hydrolysis of a molecule without a water molecule)
- Isomerisation class (catalyzes isomerization of a chemical group or double bond)
- Ligation class (catalyzes binding of two molecules, often coupled with energy consumption by hydrolysing ATP)
Enzymes can be classified using the Enzyme Classification (E.C) system, which assigns a 4-digit number indicating the class, reaction, and specific information.
Enzymes can:
- couple energy-demanding reactions to ATP hydrolysis
- be regulated through means such as small molecules, phosphorylation, degradation, synthesis, and post-translational modifications
- create large molecular machines for carrying out complex tasks