Chemistry

Imaging research on monoclonal antibodies shines the protein dynamics for the development of biopharmaceuticals.

A diagram showing the results of the Tandem-TimS device. The X axis shows the cross section or the size of the ions. The Y -axis represents the abundance of ions with a specific cross section. The black line indicates the result of NIST monoclonal antibodies. The illustration of the NIST monoclonal antibody is displayed on the right. Credit: Fanny Rue

Monoclonal antibodies or Mabs are important tools for medicine. Proteins made in these laboratorys are widely used to treat diseases such as cancer, Alzheimer’s disease, autoimmune disease, and infectious diseases. A recent study of the Florida State University of Chemistry and Birthday, indicates that a specific type of monoclonal antibody known as Nistmab has been changed to the sugar subjugation.

This study, published in chemical communication, is an extremely important step to understand Nistmab protein dynamics and develop new treatments using monoclonal antibodies.

“Understanding how sugar molecules will affect the behavior of monoclonal antibodies have been a long -standing issue in biological therapy,” said Associate Professor Christian Briholder, a research leader. “Changing the sugar part of the antibody does not seem to affect its overall structure or its movements. This is important when developing antibodies as a treatment.”

Monoclonal antibodies are the largest groups of biological drugs, are made from living things and provided in various forms. These molecules need to maintain a specific structure to properly function, as important changes in shape can destroy the ability to bind to the target.

To study the MAB structure, Bleiholder cooperates with BRUKER DALTONICS’s Melvin A. Park to measure the tandem trap ion mobility spectroscope (has developed a breakthrough method called tandem TIM. By this method, scientists We were able to study proteins and other molecules in a way to maintain the structure so that researchers can research how they change under different conditions.

This patented technology has been 10 years since then. Bleiholder learned how to perform iontophoresizing as a postdoc researcher at the California University of Santa Barbara, and observed molecular changes during the onset of Alzheimer’s disease. When he started a lab at Florida State University in 2013, he started a process to develop new measurement technology. The result was a breakthrough that allows scientists to investigate complex protein structures and stability in an unprecedented detail.

“It was rewarding to see that we could finally apply it to solve the problem after working for more than 10 years to create this method,” says Bleiholder. I did it.

In this study, Tandem-Tim was used to separate and analyze NIST monoclonal antibodies, which are standard antibodies in biological therapy research. Bleiholder’s team has confirmed that structural fluctuations between antibody groups have not been affected by glycosylation. This is a process in which the sugar molecules adhere to other molecules. This study shows an extremely important step in understanding protein dynamics and providing clarity to biopharmaceutical developers.

“Our research shows a new light on the relationship between the various structures of the antibodies after protein translation and their characteristics,” said Fanny C. Rue, FSU teacher. 。 “This study has exciting possibilities to accelerate new biological engineering in patients.”

This study can easily design monoclonal antibodies by examining how the sugar molecules adhered to the shape and stability. This breakthrough can accelerate the timeline of pharmaceutical development, improve the quality of biological therapy, and benefit patients around the world.

The study was collaborating with industry leaders such as Johnson End Johnson, exploring the application of this technology when strengthening biological medicine development.

Bleiholder’s Lab has expanded the application of tandem TIM and includes other structural analysis of other important proteins, such as SARS-COV-2 spike proteins and HIV capsapsyidore semi-brain, for biological medicine research. This lab is also a pioneering method for imaging the protein of the tissue sample, and has opened the path to the progress of individualized medicine.

The co -author of this research was JUSUNG LEE and THAIS PEDRETE. BRUKER DALTONICS’s collaborators were Erin M. PANCZYK and STUART PENGELLEY.

Details: Fanny C. Liu et al, differential glycosylation does not adjust the uniform of three -dimensional distribution of IgGK NIST monoclonal antibodies and chemical and communication (2024). Doi: 10.1039/D4cc02125H

Provided by Florida State University

Quotation: Monoclonal antibody imaging research was collected on January 30, 2025 https://phys.org/news/2025-01-imaging-monoclonal-pROTIN-Dynamics on January 30, 2025. Lights the protein dynamics for the development of biopharmaceuticals. Html

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