NOV 23, 2020 12:27 AM PST

Therapeutically Active Ion-Channels

WRITTEN BY: Nouran Amin

Therapeutically relevant ion channels have inspired researchers to look into drugs that can regulate their activity. Ion channels are a well-documented form of cell-to-cell communication and holds relevance in health and disease due to the possibility of ion channel defects. Research in the University of Leeds is proving that drug-like small molecules can regulate the activity ion channels – particularly TRPC5 ion channels that allow positive charged ions, like sodium and potassium flow throughout the cell’s plasma membrane.

Dr Muench said: "It amazes me that you think you understand how a small molecule may influence the activity of a protein -- and then you find something unexpected.

"The displacement of a lipid opens up some interesting new directions of research into how this important family of proteins functions at a fundamental level and how we may develop new therapies in the future."

Targeting TRPC5 channels can be considered therapeutic for treating kidney disease, cardiac issues, and even anxiety to name a few.

Learn more about ion channels:

 

 

Dr Bon said: "The opening and closing of TRPC channels is regulated by many factors, including dietary components such as lipids, minerals and antioxidants, as well as environmental toxins. Overactivity of TRPC channels is linked to a range of diseases. Therefore, small molecules that can stop TRPC channels from opening are increasingly considered as potential therapeutic agents.

Findings were published in Communications Biology and reveals that the drug, Pico145, can bind to TRPC5 channels preventing the channel from opening and as such imposing its therapeutic effects.

Dr David Wright, first author of the study, said: "Using cryo-electron microscopy performed in the Astbury BioStructure Laboratory, we determined high-resolution structures of the TRPC5 channel in the presence and absence of Pico145. These structures show, for the first time, how Pico145 can displace a lipid bound to each of the four TRPC5 proteins. Further studies revealed the importance of individual amino acid residues in the Pico145 binding site of TRPC5."

Source: Science Daily

About the Author
  • Nouran is a scientist, educator, and life-long learner with a passion for making science more communicable. When not busy in the lab isolating blood macrophages, she enjoys writing on various STEM topics.
You May Also Like
APR 07, 2021
Drug Discovery & Development
Therapeutics Enhance The Body's Natural Killers
APR 07, 2021
Therapeutics Enhance The Body's Natural Killers
Most people who have been prescribed pain killers are familiar with fentanyl, oxycodone, and morphine. These substances ...
MAY 04, 2021
Immunology
One Vaccine to Rule Them All
MAY 04, 2021
One Vaccine to Rule Them All
There are currently five variants of concern in the U.S., genetically distinct forms of the COVID-causing coronavirus th ...
JUN 01, 2021
Immunology
Nanoparticles Designed to Enhance Seasonal Flu Vaccines
JUN 01, 2021
Nanoparticles Designed to Enhance Seasonal Flu Vaccines
Seasonal flu vaccines only work around 40 to 60 percent of the time, says the U.S. Centers for Disease Control and Preve ...
JUN 18, 2021
Drug Discovery & Development
FDA Approves First New Drug Since 2014 for Weight-loss
JUN 18, 2021
FDA Approves First New Drug Since 2014 for Weight-loss
A new medication called ‘Wegovy’ produced by Novo Nordisk has been approved by the Food and Drug Administrat ...
JUL 11, 2021
Drug Discovery & Development
Antibiotic Resistance May Be Passed Between Dogs and Owners
JUL 11, 2021
Antibiotic Resistance May Be Passed Between Dogs and Owners
Household pets may act as a reservoir for mcr-1, a gene that is resistant to a last-resort antibiotic, colistin. The fin ...
JUL 16, 2021
Drug Discovery & Development
Machine Learning Ranks Cancer Drugs by Efficacy
JUL 16, 2021
Machine Learning Ranks Cancer Drugs by Efficacy
A machine learning algorithm developed by researchers at the Queen Mary University of London in the UK can rank cancer d ...
Loading Comments...