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Merck

SMB01352

Sigma-Aldrich

Prolylphenylalanine

≥95% (HPLC)

Sinónimos:

Pro-Phe, N-L-Prolyl-L-phenylalanine, N-Prolylphenylalanine, L-Prolyl-L-phenylalanine, Proline phenylalanine dipeptide, Proline-phenylalanine dipeptide, Prolyl-phenylalanine

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About This Item

Fórmula empírica (notación de Hill):
C14H18N2O3
Número de CAS:
Peso molecular:
262.30
MDL number:
UNSPSC Code:
12352209

Quality Level

assay

≥95% (HPLC)

form

solid

color

white to beige

mp

250—251 °C

storage temp.

2-8°C

SMILES string

OC(=O)C(Cc1ccccc1)NC(=O)C2CCCN2

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General description

Prolylphenylalanine, a dipeptide composed of proline and phenylalanine, exhibits considerable potential for diverse applications in both biochemical and biomedical research. It is an incomplete breakdown product of protein digestion or protein catabolism, found in urine. In biochemical studies, it serves as a substrate for various enzymes, including dipeptidyl peptidase-4 (DPP-4) and prolylcarboxypeptidase (PCP), shedding light on essential biochemical pathways related to protein digestion and metabolism. Moreover, prolylphenylalanine functions as a versatile tool for exploring protein interactions with other molecules, probing enzyme active sites, and identifying potential drug targets. Furthermore, it can also be used for polypeptide synthesis, where phenylalanine is an aromatic amino acid that can inhibit the activity of Angiotensin-converting enzyme (ACE, HY-P2983). Within biomedical research, prolylphenylalanine is the focus of extensive exploration as a potential therapeutic agent for a range of conditions, including hypertension, cardiovascular disease, and Alzheimer′s disease.

Application

Prolylphenylalanine can be used in biochemical and metabolomics research applications

Features and Benefits

  • Suitable for Metabolomics and Biochemical research
  • High-quality compound suitable for multiple research applications

Other Notes

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Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Prolinase and non-specific dipeptidase of human kidney.
Priestman DA, et al.
The Biochemical Journal, 231, 689-694 (1985)
Angiotensin I converting enzyme inhibitory peptides from simulated in vitro gastrointestinal digestion of cooked eggs
Majumder K, et al
Journal of Agricultural and Food Chemistry, 57, 471-477 (2009)
J Jandke et al.
Journal of chromatography, 382, 39-45 (1986-10-31)
Fractions of dipeptides, obtained from human urine by a combination of cation-exchange chromatography, ligand-exchange chromatography and reversed-phase chromatography, were transformed into their N-heptafluorobutyryl methyl ester derivatives and then subjected to capillary gas chromatography. The profiles obtained indicate the presence of

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