Featured Research

from universities, journals, and other organizations

Work with small peptide chains may revolutionize study of enzymes, diseases

Date:
April 4, 2014
Source:
Syracuse University
Summary:
Chemists, for the first time, have created enzyme-like activity using peptides that are only seven amino acids long. The breakthrough may revolutionize the study of modern-day enzymes, whose chains of amino acids usually number in the hundreds, and of neurological diseases, such as Alzheimer's, which are usually characterized by small clumps of misshapen proteins called amyloids.

A rendering of a catalytic amyloid-forming peptide, with zinc ions shown as gray spheres
Credit: Image courtesy of Syracuse University

Chemists in The College of Arts and Sciences have, for the first time, created enzyme-like activity using peptides that are only seven amino acids long.

A rendering of a catalytic amyloid-forming peptide, with zinc ions shown as gray spheres

Their breakthrough, which is the subject of a recent article in Nature Chemistry magazine (Macmillan Publishers, 2014), may revolutionize the study of modern-day enzymes, whose chains of amino acids usually number in the hundreds, and of neurological diseases, such as Alzheimer's, which are usually characterized by small clumps of misshapen proteins called amyloids.

Their finding also supports the theory that amyloid fibrils -- strong, highly organized fibers, formed by proteins and peptides -- may have predated enzymes and triggered reactions that led to some of the earliest forms of life.

"Enzymes fold into unique three-dimensional structures, which underlie their remarkable catalytic properties and contribute to their large size," says Ivan V. Korendovych, assistant professor of chemistry, who co-led the study with William DeGrado, SU professor of pharmaceutical chemistry at the University of California, San Francisco (UCSF). "Our goal was to prove that much shorter peptides can also achieve well-defined conformations through the formation of amyloid fibrils."

Korendovych and his team designed seven simple peptides, each containing seven amino acids. They then allowed the molecules of each peptide to self-assemble, or spontaneously clump together, to form amyloids. (Zinc, a metal with catalytic properties, was introduced to speed up the reaction.) What they found was that four of the seven peptides catalyzed the hydrolysis of molecules known as esters, compounds that react with water to produce water and acids -- a feat not uncommon among certain enzymes.

"It was the first time that a peptide this small self-assembled to produce an enzyme-like catalyst," says Korendovych, an expert in bioinorganic chemistry, biophysics and chemical biology. "Our finding suggests that amyloids, whose buildup leads to Alzheimer's in the brain, may also have served as the blueprint for larger, modern-day enzymes."

That's good news for researchers such as Korendovych, who thinks this finding may lead to the development of a new class of synthetic peptide-based catalysts. "The amyloid structures we've created may have a more complex biochemistry than we've realized," he says.

There are 20 naturally occurring amino acids, all of which serve as the building blocks of proteins and assist with metabolism.

An enzyme is a type of protein that is composed of at least 100 amino acids and speeds up reactions in a cell.

Korendovych says that, despite an astronomically large number of possible enzymes (each with a different amino acid sequence and three-dimensional shape), only a small number of them actually work.

"Each enzyme has to be an exact fit for its respective substrate," he says, referring to the molecule with which an enzyme reacts. "Even after millions of years, nature is still testing all the possible combinations of enzymes to determine which ones can catalyze metabolic reactions. Our results make an argument for the design of self-assembling nanostructured catalysts."


Story Source:

The above story is based on materials provided by Syracuse University. The original article was written by Rob Enslin. Note: Materials may be edited for content and length.


Journal Reference:

  1. Caroline M. Rufo, Yurii S. Moroz, Olesia V. Moroz, Jan Stφhr, Tyler A. Smith, Xiaozhen Hu, William F. DeGrado, Ivan V. Korendovych. Short peptides self-assemble to produce catalytic amyloids. Nature Chemistry, 2014; 6 (4): 303 DOI: 10.1038/nchem.1894

Cite This Page:

Syracuse University. "Work with small peptide chains may revolutionize study of enzymes, diseases." ScienceDaily. ScienceDaily, 4 April 2014. <www.sciencedaily.com/releases/2014/04/140404140401.htm>.
Syracuse University. (2014, April 4). Work with small peptide chains may revolutionize study of enzymes, diseases. ScienceDaily. Retrieved August 28, 2014 from www.sciencedaily.com/releases/2014/04/140404140401.htm
Syracuse University. "Work with small peptide chains may revolutionize study of enzymes, diseases." ScienceDaily. www.sciencedaily.com/releases/2014/04/140404140401.htm (accessed August 28, 2014).

Share This




More Health & Medicine News

Thursday, August 28, 2014

Featured Research

from universities, journals, and other organizations


Featured Videos

from AP, Reuters, AFP, and other news services

Mini Pacemaker Has No Wires

Mini Pacemaker Has No Wires

Ivanhoe (Aug. 27, 2014) — Cardiac experts are testing a new experimental device designed to eliminate major surgery and still keep the heart on track. Video provided by Ivanhoe
Powered by NewsLook.com
After Cancer: Rebuilding Breasts With Fat

After Cancer: Rebuilding Breasts With Fat

Ivanhoe (Aug. 27, 2014) — More than 269 million women are diagnosed with breast cancer each year. Many of them will need surgery and radiation, but there’s a new simple way to reconstruct tissue using a patient’s own fat. Video provided by Ivanhoe
Powered by NewsLook.com
Blood Clots in Kids

Blood Clots in Kids

Ivanhoe (Aug. 27, 2014) — Every year, up to 200,000 Americans die from a blood clot that travels to their lungs. You’ve heard about clots in adults, but new research shows kids can get them too. Video provided by Ivanhoe
Powered by NewsLook.com
Radio Waves Knock out Knee Pain

Radio Waves Knock out Knee Pain

Ivanhoe (Aug. 27, 2014) — Doctors have used radio frequency ablation or RFA to reduce neck and back pain for years. But now, that same technique is providing longer-term relief for patients with severe knee pain. Video provided by Ivanhoe
Powered by NewsLook.com

Search ScienceDaily

Number of stories in archives: 140,361

Find with keyword(s):
 
Enter a keyword or phrase to search ScienceDaily for related topics and research stories.

Save/Print:
Share:  

Breaking News:
from the past week

In Other News

... from NewsDaily.com

Science News

Health News

Environment News

Technology News



Save/Print:
Share:  

Free Subscriptions


Get the latest science news with ScienceDaily's free email newsletters, updated daily and weekly. Or view hourly updated newsfeeds in your RSS reader:

Get Social & Mobile


Keep up to date with the latest news from ScienceDaily via social networks and mobile apps:

Have Feedback?


Tell us what you think of ScienceDaily -- we welcome both positive and negative comments. Have any problems using the site? Questions?
Mobile iPhone Android Web
Follow Facebook Twitter Google+
Subscribe RSS Feeds Email Newsletters
Latest Headlines Health & Medicine Mind & Brain Space & Time Matter & Energy Computers & Math Plants & Animals Earth & Climate Fossils & Ruins