PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2006 | 53 | 1 |

Tytuł artykułu

Chelating ability of proctolin tetrazole analogue

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
The aim of the investigation was to establish the chelating ability of a new proctolin analogue of the sequence Arg-Tyr-LeuΨ[CN4]Ala-Thr towards copper(II) ions. The insertion of the tetrazole moiety into the peptide sequence has considerably changed the coordination ability of the ligand. Potentiometric and spectroscopic (UV-Vis, CD, EPR) results indicate that the incorporation of 1,5-disubstituted tetrazole ring favours the formation of a stable complex form of CuH-1L. This 4N coordination type complex is the dominant species in the physiological pH range. The tetrazole moiety provides one of these nitrogens. The data indicate that Cu(II) ions are strongly trapped inside the peptide backbone. These findings suggest that Cu(II) can hold peptide chains in a bent conformation. This bent conformation may be essential for bioactivity of the tetrazole peptides.

Wydawca

-

Rocznik

Tom

53

Numer

1

Opis fizyczny

p.65-72,fig.,ref.

Twórcy

  • Technical University of Lodz, Lodz, Poland
autor
autor
autor
autor
autor

Bibliografia

  • Bal W, Kozłowski H, Kupryszewski G, Maćkiewicz Z, Petit LD, Robbins R (1993) Complexes of Cu(II) with Asn-Ser-Phe-Arg-Tyr-NH2; an example of metal ion-promoted conformational organization which results in exceptionally high complex stability. J Inorg Biochem 52: 79–87.
  • Bishop CA, O’Shea M, Miller RJ (1981) Neuropeptide proctolin (H-Arg-Tyr-Leu-Pro-Thr-OH): immunological detection and neuronal localization in insect central nervous system. Proc Natl Acad Sci USA 78: 5899–5902.
  • Brown BE, Starratt AN (1975) Isolation of proctolin, a myotropic peptide, from Periplaneta americana. J Insect Physiol 21: 1879–1881.
  • Chruscinska E, Dyba M, Micera G, Ambroziak W, Olczak J, Zabrocki J, Kozlowski H (1997) Binding ability of Cu2+ ions by opiate-like fragments of bovine casein. J Inorg Biochem 66: 19–22.
  • Chruscinska E, Olczak J, Zabrocki J, Dyba M, Micera G, Sanna D, Kozlowski H (1998) Specific interaction of bovine and human beta-casomorphin-7 with Cu(II) ions. J Inorg Biochem 69: 91–95.
  • Clarke ER, Martell AE (1970) Metal chelates of arginine and related ligands. J Inorg Nucl Chem 32: 911–926.
  • Eckert M, Agricola H, Penzlin H (1981) Immunocytochemical identification of proctolin-like immunoreactivity in the terminal ganglion and hindgut of the cockroach Periplaneta americana (L.). Cell Tissue Res 217: 633–645.
  • Gans P, Sabatini A, Vacca A (1985) SUPERQUAD: An improved general program for computation of formation constants from potentiometric data. J Chem Soc, Dalton Trans 1195–1200.
  • Irving H, Miles MG, Pettit LD (1967) A study of some problems in determining the stoichiometric proton dissociation constants of complexes by potentiometric titrations using a glass electrode. Anal Chim Acta 38: 475–488.
  • Konopińska D, Rosiński G, Lesicki A, Sujak P, Sobótka W, Bartosz-Bechowski H (1988a) New N-terminal modified proctolin analogs — synthesis and their cardio-excitatory effect on insects. Int J Pept Protein Res 31: 463.
  • Konopińska D, Rosiński G, Lesicki A, Sujak P, Sobótka W (1988b) [L-Dopa2]-Proctolin-synthesis and its high cardioexcitatory properties on cockroach Periplaneta americana. Bull Pol Acad Sci S Chem 36: 17.
  • Konopińska D, Rosiński G (1999) Proctolin an insect neuropeptide. J Pept Sci 5: 533–546.
  • Kowalik-Jankowska T, Rajewska A, Szeszel-Fedorowicz W, Konopińska D (2005) Bonding of copper(II) ions by proctolin analogues modified in fifth position of the peptide chain. Polyhedron 24: 443–450.
  • Kozlowski H, Micera G (1995) Biological fluids in bioinorganic chemistry. In Handbook of Metal-Ligand Interactions (Berthon G, ed) vol 1, pp 566–582, Marcel Dekker, New York.
  • Kozłowski H, Radomska B, Kupryszewski G, Lammek B, Livera C, Petit LD, Pyburn S (1989) The unusual co-ordination ability of vasopressin-like peptides; potentiometric and spectroscopic studies of some copper(II) and nickel(II) complexes. J Chem Soc Dalton Trans 173–177.
  • Kozlowski H, Bal W, Dyba M, Kowalik-Jankowska T (1999) Specific structure-stability relations in metallopeptides. Coord Chem Rev 184: 319–46.
  • Kuczer M, Rosiński G, Lisowski M, Picur B, Konopińska D (1996) New proctolin analogues modified by D-amino acids in the peptide chain and their high cardioexcitatory effect on tenebrio molitor. Int J Pept Protein Res 48: 289–291.
  • Linder MC, Goode CA (1991) Biochemistry of Copper. Pp 220–231, Plenum Press, New York.
  • Livera C, Pettit LD, Bataille M, Krembel J, Bal W, Kozlowski H (1988) Copper(II) complexes with some tetrapeptides containing the “break-point” prolyl residue in the third position. J Chem Soc Dalton Trans 1357–1360.
  • Lodyga-Chruscinska E, Micera G, Szajdzińska-Piętek E, Sanna D (1998) Copper(II) complexes of opiate-like food peptides. J Agric Food Chem 46: 115–118.
  • Lodyga-Chruscinska E, Micera G, Sanna D, Olczak J, Zabrocki J, Kozlowski H, Chruscinski L (1999) Effect of the tetrazole cis-amide bond surrogate on the complexing ability of some enkephalin analogues toward Cu(II) ions. J Inorg Biochem 76: 1–11.
  • Lodyga-Chruscinska E, Brzezinska-Blaszczyk E, Micera G, Sanna D, Kozlowski H, Olczak J, Zabrocki J, Olejnik AK (2000) Can the 1,5-disubstituted tetrazole ring modify the co-ordination ability and biological activity of opiate-like peptides. J Inorg Biochem 78: 283–291.
  • Łodyga-Chruścińska E, Ołdziej S, Micera G, Sanna D, Chruściński L, Olczak J, Zabrocki J (2004) Impact of 1,5-disubstituted tetrazole ring on chelating ability of δ-selective opioid peptide. J Inorg Biochem 98: 447–458.
  • Nachman RJ, Zabrocki J, Olczak J, Williams HJ, Moyna G, Ian Scott A, Coast GM (2002) cis-peptide bond mimetic tetrazole analogs of the insect kinins identify the active conformation. Peptides 23: 709–716.
  • Nachman RJ, Coast GM, Kaczmarek K, Williams HJ, Zabrocki J (2004) Stereochemistry of insect kinin tetrazole analogues and their diuretic activity in crickets. Acta Biochim Polon 51: 121–127.
  • Onindo CO, Sliva TYu, Kowalik-Jankowska T, Fritsky IO, Buglyo P, Petit LD, Kozłowski H, Kiss T (1995) Copper(II) co-ordination by oxime analogues of amino acids and peptides. J Chem Soc Dalton Trans 3911–3915.
  • Orchard I, Belanger JH, Lange AB (1989) Proctolin: a review with emphasis on insects. J Neurobiol 20: 470–496.
  • O’Shea M, Adams M (1986) Proctolin: from `gut factor’ to model neuropeptide. Adv Insect Physiol 19: 1–28.
  • Pettit LD, Gregor JG, Kozlowski H (1990) In Perspectives on Bioinorganic Chemistry (Hay RW, Dilworth JR, Nolan KB, eds) vol 1, pp 16–27, JAI Press, London.
  • Sovago I (1990) Metal complexes of peptides and their derivatives. In Biocoordination Chemistry: Coordination Equilibria in Biologically Active Systems (Burger K, ed) pp 135–184, Ellis Horwood.
  • Woźnica I, Szeszel-Fedorowicz W, Rosiński G, Konopińska D (2004) Biological evaluation of analogues of an insect neuropeptide proctolin. Acta Biochim Polon 51: 115–119.
  • Zabrocki J, Smith GD, Dunbar JB, Iijima H, Marshall GR (1988) Conformational mimicry. 1 1,5-Disubstituted tetrazole ring as a surrogate for the cis amide bond. J Am Chem Soc 110: 5875–5880.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-84484c68-0560-4157-80ee-72e8193739bd
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.