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Chemical Compound Review

Phe-Phe     (2R)-2-[[(2R)-2-amino-3- phenyl...

Synonyms: SureCN5065345, ANW-70612, CTK1E9331, KB-209662, AC1O52XA, ...
 
 
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Disease relevance of Phe-Phe

 

High impact information on Phe-Phe

  • Specificity was further shown by the finding that no significant interaction was observed in yeast expressing LexA-Abeta bait when the B42 transactivation domain was fused to an Abeta fragment with Phe-Phe at residues 19 and 20 replaced by Thr-Thr (AbetaTT), a finding that is consistent with in vitro observations made by others [3].
  • RMCP I was more prone than chymotrypsin to hydrolyze peptide bonds consisting of Leu-Xaa or two hydrophobic residues--e.g., Phe-Phe [4].
  • Patients with the Ile/Ile genotype had an increased risk for invasive disease (stage II-IV; OR = 2.13, 95% CI = 1.04-4.39) or metastatic disease (stage III and IV; OR = 2.31, 95% CI = 1.06-5.05) compared with those with the Phe/Phe genotype [5].
  • The importance of two Phe-Phe pairs in MBP to its interactions with lipids was investigated by separately mutating each pair to Ala-Ala [6].
  • We also show that mutation of residues Ser(338) to Ala or Tyr(340)-Tyr(341) to Phe-Phe immediately amino-terminal to the catalytic domain abrogates activation of both the wild type and zinc finger mutant Raf by both EGF/4beta-12-O-tetradecanoylphorbol-13-acetate and nocodazole [7].
 

Biological context of Phe-Phe

  • A study of the time course of the hydrolysis showed that the reaction was biphasic; nearly all of the protein was cleaved at Phe-Phe (88-89) before significant cleavages at other sites occurred [8].
  • Cerebral aspartic peptidases show identical substrate specificity, cleaving the Leu10-Leu bond in RSTP and Phe-Phe in SP and peptide I-III, and not splitting angiotensins I and II [9].
 

Anatomical context of Phe-Phe

  • Studies with guinea pig and rabbit myelin basic protein fragments showed that a region encompassing the central Phe-Phe (87-88) sequence is obligatory, but not sufficient, for reactivity with antibody 18.25 [10].
  • An intramolecularly quenched fluorogenic peptide containing o-aminobenzoyl (Abz) and ethylenediamine 2,4-dinitrophenyl (Eddnp) groups at amino- and carboxyl-terminal amino acid residues, Abz-Lys-Pro-Ile-Glu-Phe-Phe-Arg-Leu-Eddnp, was hydrolyzed by purified human pepsin, gastricsin, and gastric juice uniquely at the Phe-Phe bond [11].
  • These results provide evidence that in intestinal epithelium, hydrolysis of Phe-Phe and maltose does not occur on the cell surface with release of the hydrolyzed products to the medium [12].
  • We examined whether in-vivo expression of the variant compared to the wild-type Phe/Phe genotype at codon 124 of the 5-HT1B receptor in human temporal arteries modifies their agonist-induced contraction [13].
 

Associations of Phe-Phe with other chemical compounds

  • Design, structure-activity, and molecular modeling studies of potent renin inhibitory peptides having N-terminal Nin-For-Trp (Ftr): angiotensinogen congeners modified by P1-P1' Phe-Phe, Sta, Leu psi[CH(OH)CH2]Val or leu psi[CH2NH]Val substitutions [14].
  • Brain cathepsin D, purified by affinity chromatography on Sepharose pepstatin columns, was incubated with synthetic peptides corresponding to the susceptible regions of the myelin basic protein encompassing the two Phe-Phe bonds [15].
  • Kallistatin is a unique serine proteinase inhibitor (serpin) with Phe-Phe residues at the P2 and P1 positions [16].
  • N-Terminal sodium phosphonate derivatives Na3O3PCH2CONHR (R-Leu, Phe, or Tyr) and Na3O3PCH2CONHR-R (R-R = Leu-Phe, Phe-Leu, Phe-Phe, and Phe-Tyr) were synthesized [17].
 

Gene context of Phe-Phe

 

Analytical, diagnostic and therapeutic context of Phe-Phe

References

  1. Deimination of myelin basic protein. 1. Effect of deimination of arginyl residues of myelin basic protein on its structure and susceptibility to digestion by cathepsin D. Pritzker, L.B., Joshi, S., Gowan, J.J., Harauz, G., Moscarello, M.A. Biochemistry (2000) [Pubmed]
  2. HIV-1 protease inhibitors: synthesis and biological evaluation of glycopeptidemimetics. Ghosh, A.K., McKee, S.P., Sanders, W.M., Darke, P.L., Zugay, J.A., Emini, E.A., Schleif, W.A., Quintero, J.C., Huff, J.R., Anderson, P.S. Drug design and discovery. (1993) [Pubmed]
  3. Two-hybrid system as a model to study the interaction of beta-amyloid peptide monomers. Hughes, S.R., Goyal, S., Sun, J.E., Gonzalez-DeWhitt, P., Fortes, M.A., Riedel, N.G., Sahasrabudhe, S.R. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  4. Substrate specificity of the chymotrypsin-like protease in secretory granules isolated from rat mast cells. Le Trong, H., Neurath, H., Woodbury, R.G. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  5. Functional STK15 Phe31Ile polymorphism is associated with the occurrence and advanced disease status of esophageal squamous cell carcinoma. Miao, X., Sun, T., Wang, Y., Zhang, X., Tan, W., Lin, D. Cancer Res. (2004) [Pubmed]
  6. Membrane-anchoring and charge effects in the interaction of myelin basic protein with lipid bilayers studied by site-directed spin labeling. Bates, I.R., Boggs, J.M., Feix, J.B., Harauz, G. J. Biol. Chem. (2003) [Pubmed]
  7. Microtubule integrity regulates Pak leading to Ras-independent activation of Raf-1. insights into mechanisms of Raf-1 activation. Zang, M., Waelde, C.A., Xiang, X., Rana, A., Wen, R., Luo, Z. J. Biol. Chem. (2001) [Pubmed]
  8. Large peptides of bovine and guinea pig myelin basic proteins produced by limited peptic hydrolysis. Martenson, R.E., Kramer, A.J., Deibler, G.E. Biochemistry (1975) [Pubmed]
  9. Substrate specificity of cerebral cathepsin D and high-Mr aspartic endopeptidase. Azaryan, A.V., Galoyan, A.A. J. Neurosci. Res. (1988) [Pubmed]
  10. Evidence for specific polypeptide chain folding in myelin basic protein from reactions between fragments of the protein and monoclonal antibodies. Alvord, E.C., Hruby, S., Martenson, R.E., Deibler, G.E., Law, M.J. J. Neurochem. (1986) [Pubmed]
  11. A fluorimetric method for the determination of pepsin activity. da Silva Gomes, R.A., Batista, R.P., Costa de Almeida, A., da Fonseca, D.N., Juliano, L., Hial, V. Anal. Biochem. (2003) [Pubmed]
  12. Uptake of the components of phenylalanylphenylalanine and maltose by intestinal epithelium. Shoaf, C.R., Heizer, W.D., Caplow, M. Biochim. Biophys. Acta (1980) [Pubmed]
  13. 5-Hydroxytryptamine-induced contraction of human temporal arteries coexpressing 5-HT2A receptors and wild-type or variant (Phe124Cys) 5-HT1B receptors: increased contribution of 5-HT1B receptors to the total contractile amplitude in arteries from Phe124Cys heterozygous individuals. Verheggen, R., Werner, I., Lücker, A., Brüss, M., Göthert, M., Kaumann, A.J. Pharmacogenet. Genomics (2006) [Pubmed]
  14. Design, structure-activity, and molecular modeling studies of potent renin inhibitory peptides having N-terminal Nin-For-Trp (Ftr): angiotensinogen congeners modified by P1-P1' Phe-Phe, Sta, Leu psi[CH(OH)CH2]Val or leu psi[CH2NH]Val substitutions. Sawyer, T.K., Pals, D.T., Mao, B., Staples, D.J., de Vaux, A.E., Maggiora, L.L., Affholter, J.A., Kati, W., Duchamp, D., Hester, J.B. J. Med. Chem. (1988) [Pubmed]
  15. Specificity of brain cathepsin D: cleavage of model peptides containing the susceptible Phe-Phe regions of myelin basic protein. Marks, N., Benuck, M., Hashim, G. J. Neurosci. Res. (1980) [Pubmed]
  16. Novel roles of kallistatin, a specific tissue kallikrein inhibitor, in vascular remodeling. Chao, J., Miao, R.Q., Chen, V., Chen, L.M., Chao, L. Biol. Chem. (2001) [Pubmed]
  17. Effect of several amino acid phosphonates and related compounds on rat brain aminopeptidases. Weiss, B., Hui, K.S., Hui, M., Lajtha, A. Res. Commun. Chem. Pathol. Pharmacol. (1987) [Pubmed]
  18. Specificity of human tissue kallikrein towards substrates containing Phe-Phe pair of amino acids. Pimenta, D.C., Chao, J., Chao, L., Juliano, M.A., Juliano, L. Biochem. J. (1999) [Pubmed]
  19. Cleavage of rabbit myelin basic protein by pepsin. Martenson, R.E., Lüthy, V., Deibler, G.E. J. Neurochem. (1981) [Pubmed]
  20. Functional Phe31Ile polymorphism in Aurora A and risk of breast carcinoma. Sun, T., Miao, X., Wang, J., Tan, W., Zhou, Y., Yu, C., Lin, D. Carcinogenesis (2004) [Pubmed]
  21. Cloning and sequencing of a complementary deoxyribonucleic acid coding for a bovine alpha s1-casein A from mammary tissue of a homozygous B variant cow. McKnight, R.A., Jimenez-Flores, R., Kang, Y., Creamer, L.K., Richardson, T. J. Dairy Sci. (1989) [Pubmed]
 
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