6403-17-4

Usage

Uses

Used in Biochemistry Research:
H-SER-ALA-OH is used as a building block for peptide synthesis, allowing researchers to create and study custom peptides with specific properties and functions. Its versatility in forming peptide bonds makes it an essential component in the development of novel bioactive peptides.
Used in Protein Modification:
H-SER-ALA-OH is used as a modifying agent for the alteration of protein structures and functions. The carboxylic acid group allows for the attachment of various functional groups or other molecules to proteins, enabling the exploration of protein-protein interactions, enzyme activity, and other biological processes.
Used in Drug Development:
H-SER-ALA-OH is used as a potential therapeutic agent in drug development. Its ability to form peptide bonds and interact with proteins makes it a promising candidate for the design of peptide-based drugs targeting specific biological pathways or receptors.
Used in Cosmetics and Personal Care Products:
H-SER-ALA-OH is used as an active ingredient in cosmetics and personal care products for its moisturizing and skin conditioning properties. The presence of serine and alanine, which are components of the natural moisturizing factor (NMF) in the skin, helps maintain skin hydration and elasticity.
Used in Food and Beverage Industry:
H-SER-ALA-OH is used as a flavor enhancer and taste modifier in the food and beverage industry. H-SER-ALA-OH's ability to interact with taste receptors and proteins can contribute to the overall taste and mouthfeel of various food products.

Upstream product

• 38428-20-5 methyl ((benzyloxy)carbonyl)-L-seryl-L-alaninate 
• 6402-95-5 Cbz-L-ser-L-ala-Cbz 
• 24787-87-9 N-Benzyloxycarbonyl-L-seryl-L-alanin 

Relevant academic research and scientific papers

Direct asymmetric intermolecular aldol reactions catalyzed by amino acids and small peptides

In nature there are at least nineteen different acyclic amino acids that act as the building blocks of poly-peptides and proteins with different functions. Here we report that α-amino acids, β-amino acids, and chiral amines containing primary amine functions catalyze direct asymmetric intermolecular aldol reactions with high enantio-selectivities. Moreover, the amino acids can be combined into highly modular natural and unusual small peptides that also catalyze direct asymmetric intermolecular aldol reactions with high stereoselectivities, to furnish the corre sponding aldol products with up to > 99% ee. Simple amino acids and small peptides can thus catalyze asymmetric aldol reactions with stereoselectivities matching those of natural enzymes that have evolved over billions of years. A small amount of water accelerates the asymmetric aldol reactions catalyzed by amino acids and small peptides, and also increases their stereoselectivities. Notably, small peptides and amino acid tetrazoles were able to catalyze direct asymmetric aldol reactions with high enantioselectivities in water, while the parent amino acids, in stark contrast, furnished nearly racemic products. These results suggest that the prebiotic oligomerization of amino acids to peptides may plausibly have been a link in the evolution of the homochirality of sugars. The mechanism and stereochemistry of the reactions are also discussed.

The small peptide-catalyzed direct asymmetric aldol reaction in water

The asymmetric aldol reaction is a powerful method for forming carbon-carbon bonds. Small peptides with a primary amine as the catalytic residue catalyze asymmetric aqueous aldol reactions between unmodified ketones and aldehydes to furnish the corresponding aldol products with high ees. The high momodularity of the small peptides should enable the construction of several novel catalysts by combinatorial techniques for the aqueous asymmetric aldol reaction. The remarkably high difference in stereoselectivity between the peptide bond-formation was an important step towards the evaluation of asymmetric catalysis and homochilarity.

Small peptides as modular catalysts for the direct asymmetric aldol reaction: Ancient peptides with aldolase enzyme activity

Simple peptides and their analogues having a primary amino group as the catalytic residue mediate the direct asymmetric intermolecular aldol reaction with high stereoselectivity and furnish the corresponding aldol products with up to 99% ee; this intrinsic ability of highly modular peptides may explain the initial molecular evolution of aldolase enzymes. The Royal Society of Chemistry 2005.