Related Experiment Video
Updated: Jun 12, 2026

08:00
Sample Preparation and Relative Quantitation using Reductive Methylation of Amines for Peptidomics Studies
Published on: November 4, 2021
Analysis of Endogenous D-Amino Acid-Containing Peptides in Metazoa
Lu Bai1, Sarah Sheeley, Jonathan V Sweedler
1Department of Molecular and Integrative Physiology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801.
Bioanalytical Reviews
|May 22, 2010
Summary
D-amino acid-containing peptides (DAACPs) are found in animals, with altered structures enhancing biological functions. These peptides, often overlooked, may be more common than previously believed.
Area of Science:
- Biochemistry
- Molecular Biology
- Animal Physiology
Background:
- Peptides are chiral molecules, with L-amino acids forming proteins.
- D-amino acid-containing peptides (DAACPs) are found in animals, differing from bacterial peptides.
- Enzyme-catalyzed isomerization of L-amino acids to D-forms can enhance peptide function.
Purpose of the Study:
- To review the history and discovery of DAACPs in animals.
- To discuss analytical methods for separating and detecting peptide diastereomers.
- To highlight the potential prevalence of DAACPs due to subtle post-translational modifications.
Main Methods:
- Review of existing literature on DAACPs.
- Discussion of analytical techniques for diastereomeric separation and detection.
- Analysis of discrepancies in bioassays and chromatography indicating DAACPs.
Main Results:
- DAACPs have been identified across various Metazoan groups.
- The L-to-D modification is subtle and often missed by standard sequencing.
- Existing diastereomer separation techniques have aided discovery, but more robust methods are needed.
Conclusions:
- DAACPs may be more widespread in animals than currently recognized.
- Improved analytical methods are crucial for identifying DAACPs in complex biological samples.
- Understanding DAACPs is vital for comprehending their enhanced biological roles.
Related Concept Videos
Amino Acid Catabolism
Microorganisms rely on proteins as an essential carbon and energy source, particularly in environments with limited polysaccharides or lipids. However, proteins are too large to cross the plasma membrane unaided, necessitating enzymatic degradation. Microbes secrete extracellular proteases and peptidases that hydrolyze proteins into peptides, which can then be transported across the membrane. Once inside the cell, intracellular proteases degrade these peptides into free amino acids, which...
Amino Acid Biosynthetic Pathways
Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which provide...
Protein Digestion
Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.
Overview of Protein Metabolism
Proteins are broken down into amino acids during digestion. Unlike fats and carbohydrates, which are stored for later use, proteins are not. Instead, amino acids are either used to produce ATP through oxidation or contribute to the creation of new proteins for the growth and repair of the body. Any surplus amino acids from the diet are converted into glucose or triglycerides rather than excreted.
Amino acids play various roles in the body once they are absorbed into cells. They are restructured...
Amino acids play various roles in the body once they are absorbed into cells. They are restructured...
