H-Phe-Phe-OH
H-Phe-Phe-OH structure
|
Common Name | H-Phe-Phe-OH | ||
|---|---|---|---|---|
| CAS Number | 2577-40-4 | Molecular Weight | 312.363 | |
| Density | 1.2±0.1 g/cm3 | Boiling Point | 582.8±50.0 °C at 760 mmHg | |
| Molecular Formula | C18H20N2O3 | Melting Point | N/A | |
| MSDS | USA | Flash Point | 306.2±30.1 °C | |
|
Metabolomic profiling of serum in the progression of Alzheimer's disease by capillary electrophoresis-mass spectrometry.
Electrophoresis 35(23) , 3321-30, (2014) There is high interest in the discovery of early diagnostic biomarkers of Alzheimer's disease, for which metabolomics exhibits a great potential. In this work, a metabolomic approach based on ultrafiltration and analysis by CE-MS has been used to obtain repre... |
|
|
Possible mechanism of uptake for several compounds in ionized form through human erythrocyte membrane.
Life Sci. 34(5) , 427-36, (1984) The mechanism underlying uptake of certain compounds in ionized form across human red blood cell membrane was examined. The ionized forms of salicylate, 5-methoxy-salicylate and phenylalanylphenylalanine were significantly taken up into the interior space of ... |
|
|
pH-dependence of complexion constants and complex mobility in capillary electrophoresis separations of dipeptide enantiomers.
Electrophoresis 22(15) , 3163-70, (2001) The chiral separation of the LL- and DD-enantiomers of the dipeptides Ala-Tyr, Phe-Phe, and Asp-PheOMe has been investigated at pH 2.5 and pH 3.5 using beta-cyclodextrin (beta-CD), heptakis-(2,6-di-O-methyl)-beta-cyclodextrin, and heptakis-(2,3,6-tri-O-methyl... |
|
|
Enzymatic digestibility of peptides cross-linked by ionizing radiation.
Int. J. Radiat. Biol. Relat. Stud. Phys. Chem. Med. 45(3) , 283-95, (1984) p6gestibility by proteolytic enzymes of peptides cross-linked by ionizing radiation was investigated. Small peptides of alanine and phenylalanine were chosen as model compounds and aminopeptidases and carboxypeptidases were used as proteolytic enzymes. Peptid... |
|
|
A symmetric inhibitor binds HIV-1 protease asymmetrically.
Biochemistry 32(3) , 937-47, (1993) Potential advantages of C2-symmetric inhibitors designed for the symmetric HIV-1 protease include high selectivity, potency, stability, and bioavailability. Pseudo-C2-symmetric monools and C2-symmetric diols, containing central hydroxymethylene and (R,R)-dihy... |
|
|
Carbohydrate binding sites in Candida albicans exo-β-1,3-glucanase and the role of the Phe-Phe 'clamp' at the active site entrance.
FEBS J. 277(21) , 4549-61, (2010) Candida albicans exo-β-1,3-glucanase (Exg; EC 3.2.1.58) is implicated in cell wall β-D-glucan remodelling through its glucosyl hydrolase and/or transglucosylase activities. A pair of antiparallel phenylalanyl residues (F144 and F258) flank the entrance to the... |
|
|
Renin inhibitors based on dipeptide analogues. Incorporation of the hydroxyethylene isostere at the P2/P3 sites.
J. Med. Chem. 33(1) , 371-4, (1990) The synthesis of a series of renin inhibitors in which the P2 and P3 amino acids are replaced with the hydroxyethylene dipeptide isostere is reported. In vitro evaluation of the inhibitors has revealed that this isostere is an acceptable amide-bond replacemen... |
|
|
Uptake of the components of phenylalanylphenylalanine and maltose by intestinal epithelium.
Biochim. Biophys. Acta 600(3) , 939-49, (1980) The observed rate of phenylalanine absorption into rat intestinal rings with 0.5 or 5.0 mM phenylalanine is greater than that for absorption of phenylalanine from 0.25 or 2.5 mM Phe-Phe, respectively. With the amino acid phenylalanine, V for absorption is the... |
|
|
A possible primordial peptide cycle.
Science 301(5635) , 938-40, (2003) alpha-Amino acids can undergo peptide formation by activation with carbon monoxide (CO) under hot aqueous conditions in the presence of freshly coprecipitated colloidal (Fe,Ni)S. We now show that CO-driven peptide formation proceeds concomitantly with CO-driv... |
|
|
The yeast kinase Yck2 has a tripartite palmitoylation signal.
Mol. Biol. Cell 22(15) , 2702-15, (2011) The yeast kinase Yck2 tethers to the cytoplasmic surface of the plasma membrane through dual palmitoylation of its C-terminal Cys-Cys dipeptide, mediated by the Golgi-localized palmitoyl-transferase Akr1. Here, the Yck2 palmitoylation signal is found to consi... |