24046-71-7

Usage

Uses

Used in Pharmaceutical Industry:
H-TRP-ALA-OH is used as a potential therapeutic agent for its involvement in the synthesis of important neurotransmitters and hormones. The presence of tryptophan, a precursor to serotonin and melatonin, suggests its use in treating conditions related to mood regulation and sleep disorders.
Used in Nutraceutical Industry:
H-TRP-ALA-OH is used as a dietary supplement to support the body's natural production of serotonin and melatonin, potentially aiding in the maintenance of mental health and sleep patterns.
Used in Research Applications:
H-TRP-ALA-OH serves as a subject of study in scientific research to explore its effects on neurotransmitter synthesis and its potential role in various physiological processes, including mood regulation, sleep, and energy metabolism.

InChI:InChI=1/C14H17N3O3/c1-8(14(19)20)17-13(18)11(15)6-9-7-16-12-5-3-2-4-10(9)12/h2-5,7-8,11,16H,6,15H2,1H3,(H,17,18)(H,19,20)

Upstream product

• 35661-39-3 N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine 
• 143824-78-6 3-[(S)-2-carboxy-2-(9H-fluoren-9-ylmethoxycarbonylamino)ethyl]indole-1-carboxylic acid tert-butyl ester 

Relevant academic research and scientific papers

Heavy atom induced phosphorescence study on the influence of internal structural factors on the photophysics of tryptophan in aqueous solutions

In this study the effect of alanyl residue insertion into tryptophan and to some extent the effect of peptide bond on the photophysics of tryptophan chromophore has been studied. The photophysical parameters crucial in triplet state decay mechanism of aqueous AW, WA and AWA peptides have been determined applying our previously proposed methodology based on the heavy atom effect and compared with the previously reported values for tryptophan (Kowalska-Baron et al., 2012). The obtained results clearly indicated that the presence of alanyl residue and the peptide bond results in the changes in the fluorescence and phosphorescence decay kinetics of tryptophan. The fluorescence decays of the oligopeptides studied at pH 7 were biexponential. The longer lifetime component of WA arises from anionic form of this dipeptide, while the shorter one may be assigned to the zwitterionic form of WA. The observed invariance of the lifetimes of anionic and zwitterionic forms of WA throughout the pH studied supports the idea that these two components of WA fluorescence decay correspond to nearly independent species, possibly interconverting but at a rate slower than the fluorescence decay rates. Comparing the determined phosphorescence spectra of the oligopeptides studied with that of tryptophan, a slight blue-shift and more evident red-shift was observed in the spectrum of AW and WA, respectively. On the basis of the results of the phosphorescence measurements performed at pH 10, the 170 μs lifetime of WA, observed even at pH 7, may be assigned to the anionic form of the compound. It may be suggested that at pH 7 during the excited triplet state lifetime of WA there is a shift in the equilibrium towards the anionic form of this dipeptide. In the case of AW and AWA at pH 7 the obtained monoexponential decay kinetics, most probably, arise from zwitterionic forms of these peptides. The determined triplet quantum yield of AWA is slightly lower than that of tryptophan, while the quantum yield of AW is twofold lower than that of tryptophan. The highest value of the determined triplet quantum yield of WA confirms the presence of anionic form of this dipeptide at pH 7.

Process for the preparation of an α-amino acid amide

An α-amino acid amide is prepared by reaction of an Nα -aryloxycarbonylamino acid with a compound containing a free amino group. This process makes it possible readily to prepare peptides, by direct reaction between the carboxyl group of the N