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001-es BibID:BIBFORM023664
Első szerző:Fehér Krisztina (vegyész)
Cím:Modified glycopeptides related to cell wall peptidoglycan : conformational studies by NMR and molecular modelling / Krisztina Fehér, Primož Pristovšek, László Szilágyi, Đurdica Ljevaković, Jelka Tomašić
Dátum:2003
ISSN:0968-0896
Megjegyzések:Polymeric peptidoglycans of bacterial cell walls, and smaller glycopeptides derived from them, exhibit versatile biological activities including immunomodulating properties. Peptidoglycan monomer (PGM) was isolated from Brevibacterium divaricatum and novel lipophilic derivatives of PGM bearing either (adamantyl-1-yl)-acetyl or Boc-Tyr substituents (Ad-PGM and BocTyr-PGM respectively) have recently been synthesized. We have obtained full assignments of the 1H and 13C spectra, using 2D NMR techniques, for all three compounds in DMSO solutions. NOESY/ROESY experiments have provided interproton distance restraints that were used in distance geometry modelling calculations to derive conformational preferences for each of these molecules. These data were supplemented with information available from chemical shifts, temperature dependence of amide proton shifts and proton?proton scalar couplings. Analysis of the results suggest that the lipophilic substituents attached to the Dap3-e amino group of the parent PGM molecule introduce changes to the conformational preferences of the peptide moiety. In PGM electrostatic interactions between charged end groups apparently promote folded conformations with participation of the long Dap side chain. Derivatives wherein such interactions are suppressed by acylation of the Dap3-e amino group are characterized by more extended conformations of the peptide chain. The new synthetic derivatives exhibit biological properties similar to those of the parent PGM. This may indicate that peripheral parts of the peptide chain such as the C-terminal and end groups of the long Dap side chain do not significantly contribute to the binding to receptors or enzymes participating in the biochemical interactions referred to above.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Bioorganic & Medicinal Chemistry. - 11 : 14 (2003), p. 3133-3140. -
További szerzők:Pristovšek, Primož Szilágyi László (1941-) (vegyész) Ljevaković, Đurdica Tomašić, Jelka
Pályázati támogatás:T034515
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001-es BibID:BIBFORM085390
Első szerző:Pristovšek, Primož
Cím:Structure of a synthetic fragment of the LALF protein when bound to lipopolysaccharide / Primoz Pristovsek, Krisztina Fehér, László Szilágyi, Jurka Kidric
Dátum:2005
ISSN:0022-2623 1520-4804
Megjegyzések:Peptidic lipopolysaccharide (LPS) antagonists are the subject of intensive research. We report an NMR and modeling study of LALF-14 (GCKPTFRRLKWKYKCG), a synthetic cyclized fragment of the limulus anti-LPS factor (LALF) comprising residues 36-47. In a mixture with LPS we observed the transferred NOE effect and derived the LPS-bound structure of LALF-14. Neither the free nor the LPS-bound peptide displays NOEs indicative of a beta-sheet-like structure that is adopted by the fragment in the full-size protein. However, docking calculations show that the former structure is not a prerequisite for binding of LALF-14 to LPS.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Journal of Medicinal Chemistry. - 48 : 5 (2005), p. 1666-1670. -
További szerzők:Fehér Krisztina (1974-) (vegyész) Szilágyi László (1941-) (vegyész) Kidric, Jurka
Pályázati támogatás:OTKA T 34515
OTKA
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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