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2009 | 1-4 |

Tytuł artykułu

Effects of arginine substitutions on the cardioinhibitory activity of the Led-NPF-I neuropeptide

Treść / Zawartość

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Effects of structural changes on the cardioinhibitory activity of the Led-NPF-I peptide (Ala-Arg-Gly-Pro-Gln-Leu-Arg-Leu-Arg-Phe-amide) were examined by replacing Arg residues in positions 2, 7 and 9. Replacement of L-Arg2 with another basic amino acid, such as Lys, His or D-Arg, did not abolish but rather promoted cardioinhibitory activity in giant mealworm beetle Zophobas atratus Fab. Agonistic peptides were also obtained by substitution of Arg residue in position 7 with Lys or D-Arg, and Arg in position 9 with His or D-Arg, respectively. All these analogues showed stronger cardioinhibitory effects than the native peptide at low concentration (10-9 M), and [Lys7]-, [D-Arg7]- and [D-Arg9]-Led-NPF-I also at the higher concentration (10-6 M). However, substitutions of the Arg residues in position 7 with His or in position 9 with Lys caused a loss of the cardioinhibitory activity. In addition, the replacement of Arg residues in all three positions with Lys or Orn caused a reduction of cardioinhibitory activity, although a single substitution of Arg in positions 2 or 7 with Lys yielded agonistic peptides. We conclude that the Arg2 position in the N-terminal region is more tolerant to structural modification than the other two Arg positions located in the C-terminal region.

Wydawca

-

Czasopismo

Rocznik

Numer

1-4

Opis fizyczny

p.71-78,fig.,ref.

Twórcy

autor
  • Adam Mickiewicz University, 89 Umultowska St., 61-614 Poznan, Poland
autor
autor
autor
autor

Bibliografia

  • [1] Matsumoto S., Brown M.R., Crim J.W., Vigna S.P., Lea A.O., Insect Biochem., 1989, 19, 277-283.
  • [2] Spittaels K., Verhaert P., Shaw C., Johnston R.N., Devresse B., Van Beeumen J., De Loof A., Insect Biochem. Mol. Biol., 1996, 26, 375-382.
  • [3] Schoofs L., Clynen E., Cerstiaens A., Baggerman G., Wei Z., Vercammen T., Nachman R., De Loof A., Tanaka S., Peptides, 2001, 22, 219-227.
  • [4] Hewes S.R., Taghert P.H., Genome Res., 2001, 11, 1126-1142.
  • [5] Huang Y., Brown M.R., Lee T.D., Crim J.W., Insect Biochem. Mol. Biol., 1998, 28, 345-356.
  • [6] Veenstra J.A., Lambrou G., Biochem. Biophys. Res. Commun., 1995, 213, 519-524.
  • [7] R iehle M.A., Garczynski S.F., Crim J.W., Hill C.A., Brown M.R., Science, 2002, 298, 172-175.
  • [8] Li B., Predel R., Neupert S., Hauser F., Tanaka Y., Cazzamali G., Williamson M., Arakane Y., Verleyen P., Schoofs L., Schachtner J., Grimmelikhuijzen C.J.P., Park Y., Genome Res., 2008, 18, 113-122.
  • [9] C erstiaens A., Benfekih L., Zouiten H., Verhaert P., De Loof A., Schoofs L., Peptides, 1999, 20, 39-44.
  • [10] Huybrechts J., De Loof A., Schoofs L., Biochem. Biophys. Res. Commun., 2004, 317, 909-916.
  • [11] Lee K.S., You K.H., Choo J.K., Han Y.M., Yu K., J. Biol. Chem., 2004, 279, 50781-50789.
  • [12] Skonieczna M., Rosiński G., Pestycydy/Pesticides, 2004, (3-4), 33-39.
  • [13] Skonieczna M., Grodecki S., Konopińska D., Rosiński G., ibid., 2005, (4), 91-98.
  • [14] Marciniak P., Grodecki S., Konopińska D., Rosiński G., J. Pept. Sci., 2008, 14, 329-334.
  • [15] Quennedey A., Aribi N., Everaerts C., Delbecque J.P., J. Insect Physiol., 1995, 41, 143-152.
  • [16] R osiński G., Gade G., ibid., 1988, 34, 1035-1042.
  • [17] Martens I., Meeusen T., Huybrechts R., De Loof A., Schoofs L., Biochem. Biophys. Res. Commun., 2002, 297, 1140-1148.
  • [18] Garczynski S.F., Brown M.R., Crim J.W., Peptides, 2006, 27, 575-582.
  • [19] Garczynski S.F., Crim J.W., Brown M.R., ibid, 2007, 28, 109-118.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

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