所有图片(1)
别名:
Pro-Phe, N-L-Prolyl-L-phenylalanine, N-Prolylphenylalanine, L-Prolyl-L-phenylalanine, Proline phenylalanine dipeptide, Proline-phenylalanine dipeptide, Prolyl-phenylalanine
经验公式（希尔记法）:
C14H18N2O3
推荐产品
质量水平
检测方案
≥95% (HPLC)
形式
solid
颜色
white to beige
mp
250—251 °C
储存温度
2-8°C
SMILES字符串
OC(=O)C(Cc1ccccc1)NC(=O)C2CCCN2
一般描述
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.
应用
Prolylphenylalanine can be used in biochemical and metabolomics research applications
特点和优势
- Suitable for Metabolomics and Biochemical research
- High-quality compound suitable for multiple research applications
其他说明
For additional information on our range of Biochemicals, please complete this form.
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
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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