• HOME
  • NEWS
  • EXPLORE
    • CAREER
      • Companies
      • Jobs
    • EVENTS
    • iGEM
      • News
      • Team
    • PHOTOS
    • VIDEO
    • WIKI
  • BLOG
  • COMMUNITY
    • FACEBOOK
    • INSTAGRAM
    • TWITTER
Friday, October 3, 2025
BIOENGINEER.ORG
No Result
View All Result
  • Login
  • HOME
  • NEWS
  • EXPLORE
    • CAREER
      • Companies
      • Jobs
        • Lecturer
        • PhD Studentship
        • Postdoc
        • Research Assistant
    • EVENTS
    • iGEM
      • News
      • Team
    • PHOTOS
    • VIDEO
    • WIKI
  • BLOG
  • COMMUNITY
    • FACEBOOK
    • INSTAGRAM
    • TWITTER
  • HOME
  • NEWS
  • EXPLORE
    • CAREER
      • Companies
      • Jobs
        • Lecturer
        • PhD Studentship
        • Postdoc
        • Research Assistant
    • EVENTS
    • iGEM
      • News
      • Team
    • PHOTOS
    • VIDEO
    • WIKI
  • BLOG
  • COMMUNITY
    • FACEBOOK
    • INSTAGRAM
    • TWITTER
No Result
View All Result
Bioengineer.org
No Result
View All Result
Home NEWS Science News Biology

Fast folding for synthetic peptides and microproteins

Bioengineer by Bioengineer
March 22, 2024
in Biology
Reading Time: 3 mins read
0
Disulfide bond common in protein structures
Share on FacebookShare on TwitterShare on LinkedinShare on RedditShare on Telegram

Chemists can now produce an important class of small proteins called cysteine-rich peptides in their naturally folded 3D structure more reliably and much faster, thanks to methods that mimic what happens inside cells. The advance, achieved by researchers at Xi’an Jiaotong-Liverpool University (XJTLU) in China and Nanyang Technological University (NTU) in Singapore, is published in the journal Angewandte Chemie.

Cysteine is one of the many different amino acid molecules that can become linked together to form protein chains. Peptides are chains that are shorter than many natural proteins. Cysteine molecules each contain a sulfur atom that can become bonded to the sulfur of another cysteine elsewhere in a protein, holding different parts of the chain together.

“Re-creating the 3D shapes of cysteine-rich peptides has always been a big problem in their manufacturing,” says Dr Shining Loo of the XJTLU team. Many bioactive proteins and peptides have multiple disulfide bonds between cysteine amino acids, which are crucial for maintaining their precise 3D folded structure. Drugs like linaclotide for constipation and ziconotide for chronic pain are examples of cysteine-rich peptide drugs on the market.

“Our procedure should unlock new opportunities for drug discovery and cost-effective manufacturing of cysteine-rich microproteins and peptides as therapeutic agents,” adds researcher Dr Antony Kam of the XJTLU team.

Nature’s influence 

Disulfide bond common in protein structures

Credit: A7Davis

Chemists can now produce an important class of small proteins called cysteine-rich peptides in their naturally folded 3D structure more reliably and much faster, thanks to methods that mimic what happens inside cells. The advance, achieved by researchers at Xi’an Jiaotong-Liverpool University (XJTLU) in China and Nanyang Technological University (NTU) in Singapore, is published in the journal Angewandte Chemie.

Cysteine is one of the many different amino acid molecules that can become linked together to form protein chains. Peptides are chains that are shorter than many natural proteins. Cysteine molecules each contain a sulfur atom that can become bonded to the sulfur of another cysteine elsewhere in a protein, holding different parts of the chain together.

“Re-creating the 3D shapes of cysteine-rich peptides has always been a big problem in their manufacturing,” says Dr Shining Loo of the XJTLU team. Many bioactive proteins and peptides have multiple disulfide bonds between cysteine amino acids, which are crucial for maintaining their precise 3D folded structure. Drugs like linaclotide for constipation and ziconotide for chronic pain are examples of cysteine-rich peptide drugs on the market.

“Our procedure should unlock new opportunities for drug discovery and cost-effective manufacturing of cysteine-rich microproteins and peptides as therapeutic agents,” adds researcher Dr Antony Kam of the XJTLU team.

Nature’s influence 

Inspired by how nature quickly folds proteins inside cells, the researchers tried a different approach for the ‘oxidative’ folding reactions that form the disulfide bonds. Instead of using water-based (aqueous) solutions  they used a mixture of organic solvents. This method imitates the natural enzyme that mediates the disulfide bond formation, by creating a highly reactive environment to greatly speed up the formation and rearrangement of these bonds.

By learning from nature in this way, the team was able to make 15 different peptides and microproteins, between 14 to 58 amino acids long with two to five disulfide bonds, at rates more than 100,000 times faster than could be achieved in aqueous solvents.

“The folding was efficiently completed within one second,” Dr Loo remarks, “And the range of microproteins we produced demonstrates that our method should be effective with a much larger range of peptides and microproteins in future investigations.”

This discovery is the latest advance from the XPad (XJTLU Peptide and Drug) research group, jointly established by Dr Loo and Dr Kam. This group is committed to using tools from chemical biology, synthetic biology, and molecular pharmacology to advance the application of peptides for developing therapeutic agents.

“The future of peptide research holds great promise, and we are committed to delivering even more valuable advancements in this field,” Dr Kam concludes.



Journal

Angewandte Chemie

DOI

10.1002/anie.202317789

Method of Research

Experimental study

Subject of Research

Not applicable

Article Title

Ultrafast Biomimetic Oxidative Folding of Cysteine-rich Peptides and Microproteins in Organic Solvents

Article Publication Date

11-Feb-2024

COI Statement

The authors declare no conflict of interest.

Share12Tweet8Share2ShareShareShare2

Related Posts

Encapsulated Pseudomonas Controls Pistachio Gummosis Effectively

Encapsulated Pseudomonas Controls Pistachio Gummosis Effectively

October 3, 2025
Scientists Uncover New Intracellular Trafficking Pathway in Plant Cells

Scientists Uncover New Intracellular Trafficking Pathway in Plant Cells

October 3, 2025

Microscopic Sugars in the Brain Alter Emotional Pathways, Driving Depression

October 3, 2025

Plant Mobile Domain Proteins Resist Polycomb Gene Silencing

October 3, 2025

POPULAR NEWS

  • New Study Reveals the Science Behind Exercise and Weight Loss

    New Study Reveals the Science Behind Exercise and Weight Loss

    93 shares
    Share 37 Tweet 23
  • New Study Indicates Children’s Risk of Long COVID Could Double Following a Second Infection – The Lancet Infectious Diseases

    88 shares
    Share 35 Tweet 22
  • Physicists Develop Visible Time Crystal for the First Time

    75 shares
    Share 30 Tweet 19
  • New Insights Suggest ALS May Be an Autoimmune Disease

    67 shares
    Share 27 Tweet 17

About

We bring you the latest biotechnology news from best research centers and universities around the world. Check our website.

Follow us

Recent News

California Partnership Boosted COVID-19 Response and Advanced Health Equity, Report Reveals

Unlocking City Health: The Crucial Role of the Urban Tree Microbiome

University of Oklahoma Wins $19.9 Million Grant to Advance Groundbreaking Radar Technology

Subscribe to Blog via Email

Enter your email address to subscribe to this blog and receive notifications of new posts by email.

Join 62 other subscribers
  • Contact Us

Bioengineer.org © Copyright 2023 All Rights Reserved.

Welcome Back!

Login to your account below

Forgotten Password?

Retrieve your password

Please enter your username or email address to reset your password.

Log In
No Result
View All Result
  • Homepages
    • Home Page 1
    • Home Page 2
  • News
  • National
  • Business
  • Health
  • Lifestyle
  • Science

Bioengineer.org © Copyright 2023 All Rights Reserved.