(THE GIST OF PIB) Amyloidosis

(NOVEMBER-2023)

Recently, a 2D protein monolayer was fabricated by scientists by assembling lysozyme molecules–the model protein in studying diseases like Amyloidosis.

It is a rare disease that occurs when an abnormal protein, called amyloid, builds up in one’s organs, affecting their shape and functioning.
Amyloid deposits can build up in the heart, brain, kidneys, spleen, and other parts of the body, leading to life-threatening conditions like organ failure.
Some varieties of amyloidosis occur in association with other diseases.
These types may improve with treatment of the underlying disease. Some varieties of amyloidosis may lead to life-threatening organ failure.
The general signs or symptoms would include: Severe fatigue; Loss of weight; swelling in the belly, legs, ankles or feet; Numbness, pain, or tingling in hands or feet, and changes in skin colour.
Different amyloidosis that are prevalent
Light-chain (AL) amyloidosis: People with conditions such as multiple myeloma or a bone marrow illness are more likely to have AL amyloidosis.
AA amyloidosis: Previously known as secondary amyloidosis, this condition is the result of another chronic infectious or inflammatory disease, such as rheumatoid arthritis, Crohn’s disease, or ulcerative colitis.

It is a protein present in mucosal secretions and a principal component of airway fluid.

They have assembled lysozyme molecules as a 2D monolayer at the interface of pure aqueous subphase.
Researchers used the 2D protein monolayer to understand the behaviour of lysozyme molecules at air-water as well as at air-solid interface with the help of a technique called the Langmuir-Blodgett (LB) technique.
The physical properties of lysozyme molecules at the air-water interface were investigated under the variation of surface pressure and subphase pH conditions in the study.
The compressible behaviour of lysozyme monolayers was correlated to the stripe-like domains formed with an increase in surface pressure.
Lysozyme molecules at the air-water interface and their structural or conformational changes in variable pH conditions can be considered a model system to study Amyloidosis disease, which occurs because of the misfolding and agglomeration of lysozyme molecules.