16875-28-8

Usage

Uses

Used in Pharmaceutical Industry:
SER-PHE is used as a therapeutic agent for its potential role in treating various neurological disorders and enhancing cognitive function due to its involvement in neurotransmitter synthesis and protein regulation.
Used in Nutritional Supplements:
SER-PHE is used as a dietary supplement to support protein synthesis, promote muscle growth, and maintain overall health, given its contribution to amino acid and neurotransmitter production.
Used in Cosmetics Industry:
SER-PHE is used as an active ingredient in skincare products for its potential anti-aging and skin-repairing properties, leveraging its role in cellular metabolism and protein synthesis.
Used in Food and Beverage Industry:
SER-PHE is used as a functional ingredient to enhance the nutritional profile of foods and beverages, capitalizing on its essential amino acid composition and its role in protein synthesis and cellular functions.

Upstream product

• 17896-38-7 N--O-<α,α,α-trifluor-1-benzyloxycarbonylamino-aethyl>-Ser-Phe 
• 35661-40-6 N-Fmoc L-Phe 
• 71989-33-8 Fmoc-Ser(tBu)-OH 
• 87494-17-5 Gly-Ser-Phe 
• 17896-36-5 N--O-<α,α,α-trifluor-1-benzyloxycarbonylamino-aethyl>-Ser-Phe-methylester 
• 5564-45-4 Z-Ser-Phe-O-benzyl 

Downstream Products

• 56-45-1 L-serin 
• 63-91-2 L-phenylalanine 
• 1415888-09-3 C₁₉H₁₉N₇O₆ 

Relevant academic research and scientific papers

γ-Valerolactone (GVL): An eco-friendly anchoring solvent for solid-phase peptide synthesis

Due to the hazardous nature of CH2Cl2, regulatory authorities have imposed restrictions to minimize or even stop its use. It has therefore become imperative to identify environmentally benign solvents to replace it. Here we report on a bio derived solvent, γ-valerolactone, for the incorporation of the first amino acid onto p-alkoxybenzyl alcohol resin in solid-phase peptide synthesis. Satisfactory loading values (by a spectrophotometric method) were achieved. Furthermore, racemization and dipeptide formation were also checked and found to be acceptable.

Comparative study of the reactivity of zirconium(IV)-substituted polyoxometalates towards the hydrolysis of oligopeptides

The hydrolytic activity of the ZrIV-substituted Keggin-type (Et2NH2)8[{α-PW11O39Zr-(μ-OH)(H2O)}2]·7H2O (1), Lindqvist-type (Me4N)2[W5O18Zr(H2O)3] (2), and Wells-Dawson-type Na14[Zr4(P2W16O59)2(μ3-O)2(OH)2(H2O)4]·57H2O (3) polyoxometalates (POMs) towards the peptide bonds in the oligopeptides triglycine, tetraglycine, glycylglycylhistidine, and glycylserylphenylalanine was investigated by kinetic methods and multinuclear NMR spectroscopy. 31P NMR and UV/Vis spectroscopy showed that 1-3 were stable under the conditions used to study peptide bond hydrolysis. The reactivity of 1-3 towards oligopeptides was compared on the basis of the amount of free glycine produced at a certain time increment. In the presence of 1-3, rate constants in the range 6.25×10-7 to 10.14×10-7 s-1 were obtained, whereas no hydrolysis was observed after one month in the absence of these POMs. The results showed that the Keggin-type complex 1 was the most active towards peptide bond hydrolysis in tri- and tetrapeptides. 1H and 13C NMR spectroscopy showed that triglycine, tetraglycine, and glycylserylphenylalanine interact with 1 and 2 preferentially through the amine nitrogen atom and the N-terminal amide oxygen atom to activate the peptide bond towards hydrolysis. The coordination of glycylglycylhistidine resulted in multiple complexes with 1-3 as a result of additional imidazole coordination to the ZrIV centers.

Compositions and Methods for Binding Lysophosphatidic Acid

Compositions and methods for making and using anti-LPA agents, for example, monoclonal antibodies, are described.

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.