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SMB01352

Sigma-Aldrich

Prolylphenylalanine

≥95% (HPLC)

Synonyme(s) :

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

Formule empirique (notation de Hill):
C14H18N2O3
Numéro CAS:
Poids moléculaire :
262.30
Numéro MDL:
Code UNSPSC :
12352209

Niveau de qualité

Pureté

≥95% (HPLC)

Forme

solid

Couleur

white to beige

Pf

250—251 °C

Température de stockage

2-8°C

Chaîne SMILES 

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

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Description générale

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

Caractéristiques et avantages

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

Autres remarques

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Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

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)
Prolinase and non-specific dipeptidase of human kidney.
Priestman DA, et al.
The Biochemical Journal, 231, 689-694 (1985)
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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