Unraveling the Mysteries of Amyloidosis: Scientists Create 2D Lysozyme Protein Monolayer

In a significant breakthrough, scientists from the Institute of Advanced Study in Science and Technology, Guwahati (IASST), an autonomous institute under the Department of Science and Technology (DST) in North-East India, have successfully fabricated a 2D protein monolayer using lysozyme molecules. Lysozyme, a crucial protein found in mucosal secretions and a principal component of airway fluid, serves as a model protein for understanding diseases like Amyloidosis.

Understanding Amyloidosis: A Rare Disease with Multi-Organ Impact

Amyloidosis is a rare condition characterized by the accumulation of a protein called amyloid in various organs. This buildup can adversely affect the functioning of vital organs such as the heart, kidneys, liver, spleen, nervous system, and digestive tract, ultimately leading to multi-organ dysfunction.

Lysozyme as a Model Protein in Disease Study

Lysozyme’s significance lies in its role as a model protein for studying Amyloidosis. The misfolding and agglomeration of lysozyme molecules are implicated in the development of Amyloidosis, making it a valuable subject for scientific inquiry.

Innovative Fabrication of 2D Protein Monolayer

Led by Dr. Sarathi Kundu, Associate Professor at IASST, the research team, in collaboration with junior Research Fellow Himadri Nath, achieved the fabrication of a 2D protein monolayer by assembling lysozyme molecules at the interface of a pure aqueous subphase. The technique employed for this innovative creation is known as the Langmuir-Blodgett (LB) technique, offering a unique platform to study the behavior of lysozyme molecules at both air-water and air-solid interfaces.

Insights into Lysozyme Behavior

The study, recently published in the esteemed RSC Advances under the RSC publishers, delved into the physical properties of lysozyme molecules at the air-water interface. The research explored the compressible behavior of lysozyme monolayers, revealing the formation of stripe-like domains with increasing surface pressure. The investigation, conducted under varying subphase pH conditions, provided valuable insights into the structural and conformational changes of lysozyme molecules.

Applications and Future Implications

The closely packed lysozyme monolayers generated through the LB method present an exciting avenue for studying diverse chemical and physical properties in a 2D protein environment. Additionally, the deposited LB films of lysozyme hold potential as protein nanotemplates, offering opportunities for the crystallization of proteins of interest.



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