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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

SureCN43515     2-amino-3-cyclohexyl-propanoic acid

Synonyms: AG-A-35738, NSC-12794, AC1L3UEI, NSC12794, AR-1L8643, ...
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High impact information on Cyclohexylalanine

  • Para-aminophenylalanine 10 and O-ethyltyrosine 10 substitutions yielded antagonists potent in vitro, but His(10), 3,3'-diphenylalanine 10, 2-naphthylalanine 10, and cyclohexylalanine 10 modifications were detrimental [1].
  • A series of replacements for the C-terminal Leu established that residues containing a lipophilic side chain were most effective, with cyclohexylalanine having the greatest potency (3g, IC50 = 0.36 +/- 0.06 microM) [2].
  • These inhibitors, which are of the hydroxyethylene and statine types, respectively, possess a cyclohexylalanine side chain at P1 and have interesting functionalities at the P3 position which, until now, have not been subjected to crystallographic analysis [3].
  • Structure-activity relationships at the Leu10 side chain revealed that the LVR derived from L-cyclohexylalanine provided a 130-fold boost in potency over the LVR derived from L-leucine [4].
  • Furthermore, a shortening of the C-terminal part of our peptide analogues and the replacement of the leucine residue in P1 by a cyclohexylalanine leads to the tripeptide analogue 12 a potent renin inhibitor (IC50 = 3.5 x 10(-9) M) [5].

Associations of Cyclohexylalanine with other chemical compounds

  • We have selected three hydrophilic and charged residues--glutamic acid, histidine, and lysine--as well as three hydrophobic residues--cycloleucine, cyclohexylalanine, and naphthyl-(1)-alanine--to replace the A14 Tyr [6].


  1. Increased activity of antagonists of growth hormone-releasing hormone substituted at positions 8, 9, and 10. Varga, J.L., Schally, A.V., Horvath, J.E., Kovacs, M., Halmos, G., Groot, K., Toller, G.L., Rekasi, Z., Zarandi, M. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  2. Conformationally constrained [p-(omega-aminoalkyl)phenacetyl]-L-seryl-L-lysyl dipeptide amides as potent peptidomimetic inhibitors of Candida albicans and human myristoyl-CoA:protein N-myristoyl transferase. Nagarajan, S.R., Devadas, B., Zupec, M.E., Freeman, S.K., Brown, D.L., Lu, H.F., Mehta, P.P., Kishore, N.S., McWherter, C.A., Getman, D.P., Gordon, J.I., Sikorski, J.A. J. Med. Chem. (1997) [Pubmed]
  3. X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors. Cooper, J., Quail, W., Frazao, C., Foundling, S.I., Blundell, T.L., Humblet, C., Lunney, E.A., Lowther, W.T., Dunn, B.M. Biochemistry (1992) [Pubmed]
  4. New inhibitors of renin that contain novel phosphostatine Leu-Val replacements. Dellaria, J.F., Maki, R.G., Stein, H.H., Cohen, J., Whittern, D., Marsh, K., Hoffman, D.J., Plattner, J.J., Perun, T.J. J. Med. Chem. (1990) [Pubmed]
  5. New fluoroketones as human renin inhibitors. Tarnus, C., Jung, M.J., Rémy, J.M., Baltzer, S., Schirlin, D.G. FEBS Lett. (1989) [Pubmed]
  6. The A14 position of insulin tolerates considerable structural alterations with modest effects on the biological behavior of the hormone. Chu, Y.C., Zong, L., Burke, G.T., Katsoyannis, P.G. J. Protein Chem. (1992) [Pubmed]
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