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1.

001-es BibID:BIBFORM038449
Első szerző:Batista, Cesar V. F.
Cím:Two novel toxins from the Amazonian scorpion Tityus cambridgei that block Kv1.3 and Shaker B K(+)-channels with distinctly different affinities / Cesar V. F. Batista, Froylan Gómez-Lagunas, Ricardo C. Rodriguez de la Vega, Péter Hajdu, György Panyi, Rezső Gáspár, Lourival D. Possani
Dátum:2002
ISSN:1570-9639
Megjegyzések:Two novel toxic peptides (Tc30 and Tc32) were isolated and characterized from the venom of the Brazilian scorpion Tityus cambridgei. The first have 37 and the second 35 amino acid residues, with molecular masses of 3,871.8 and 3,521.5, respectively. Both contain three disulfide bridges but share only 27% identity. They are relatively potent inhibitors of K(+)-currents in human T lymphocytes with K(d) values of 10 nM for Tc32 and 16 nM for Tc30, but they are less potent or quite poor blockers of Shaker B K(+)-channels, with respective K(d) values of 74 nM and 4.7 microM. Tc30 has a lysine in position 27 and a tyrosine at position 36 identical to those of charybdotoxin. These two positions conform the dyad considered essential for activity. On the contrary, Tc32 has a serine in the position equivalent to lysine 27 of charybdotoxin and does not contain any aromatic amino acid. Due to its unique primary sequence and to its distinctive preference for K(+)-channels of T lymphocytes, it was classified as the first example of a new subfamily of K(+)-channel-specific peptides (alpha-KT x 18.1). Tc30 is a member of the Tityus toxin II-9 subfamily and was given the number alpha-KT x 4.4.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochimica et Biophysica Acta (BBA). Proteins and Proteomics. - 1601 : 2 (2002), p. 123-131. -
További szerzők:Gómez-Lagunas, Froylan Rodriguez de la Vega, Ricardo C. Hajdu Péter (1975-) (biofizikus) Panyi György (1966-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Possani, Lourival Domingos
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2.

001-es BibID:BIBFORM114859
035-os BibID:(cikkazonosító)140952 (scopus)85170288156
Első szerző:Elnahriry, Khaled A.
Cím:Structural and functional characterisation of Tst2, a novel TRPV1 inhibitory peptide from the Australian sea anemone Telmatactis stephensoni / Elnahriry Khaled A., Wai Dorothy C. C., Ashwood Lauren M., Naseem Muhammad Umair, Szanto Tibor G., Guo Shaodong, Panyi Gyorgy, Prentis Peter J., Norton Raymond S.
Dátum:2024
ISSN:1570-9639
Megjegyzések:Sea anemone venoms are complex mixtures of biologically active compounds, including disulfide-rich peptides, some of which have found applications as research tools, and others as therapeutic leads. Our recent transcriptomic and proteomic studies of the Australian sea anemone Telmatactis stephensoni identified a transcript for a peptide designated Tst2. Tst2 is a 38-residue peptide showing sequence similarity to peptide toxins known to interact with a range of ion channels (NaV, TRPV1, KV and CaV). Recombinant Tst2 (rTst2, which contains an additional Gly at the N-terminus) was produced by periplasmic expression in Escherichia coli, enabling the production of both unlabelled and uniformly 13C,15N?labelled peptide for functional assays and structural studies. The LC-MS profile of the recombinant Tst2 showed a pure peak with molecular mass 6 Da less than that of the reduced form of the peptide, indicating the successful formation of three disulfide bonds from its six cysteine residues. The solution structure of rTst2 was determined using multidimensional NMR spectroscopy and revealed that rTst2 adopts an inhibitor cystine knot (ICK) structure. rTst2 was screened using various functional assays, including patch?clamp electrophysiological and cytotoxicity assays. rTst2 was inactive against voltagegated sodium channels (NaV) and the human voltage-gated proton (hHv1) channel. rTst2 also did not possess cytotoxic activity when assessed against Drosophila melanogaster flies. However, the recombinant peptide at 100 nM showed >50% inhibition of the transient receptor potential subfamily V member 1 (TRPV1) and slight (~10%) inhibition of transient receptor potential subfamily A member 1 (TRPA1). Tst2 is thus a novel ICK inhibitor of the TRPV1 channel.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Sea anemone
Disulfide-rich peptides
Recombinant expression
NMR spectroscopy
ICK scaffold
TRPV1 channel
Megjelenés:Biochimica et Biophysica Acta (BBA). Proteins and Proteomics. - 1872 : 1 (2024), p. 1-13. -
További szerzők:Wai, Dorothy C. C. Ashwood, Lauren M. Naseem, Muhammad Umair (1993-) (biofizikus, molekuláris biológus) Szántó Gábor Tibor (1980-) (vegyész) Guo, Shaodong Panyi György (1966-) (biofizikus) Prentis, Peter Norton, Raymond S.
Pályázati támogatás:K143071
OTKA
Stipendium Hungaricum Scholarship from the Tempus Public Foundation
Egyéb
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3.

001-es BibID:BIBFORM003891
Első szerző:Gyémánt Gyöngyi (vegyész)
Cím:Evidence for pentagalloyl glucose binding to human salivary α-amylase through aromatic amino acid residues / Gyöngyi Gyémánt, Ágnes Zajácz, Bálint Bécsi, Chandran Ragunath, Narayanan Ramasubbu, Ferenc Erdődi, Gyula Batta, Lili Kandra
Dátum:2009
ISSN:1570-9639
Megjegyzések:We demonstrate here that pentagalloyl glucose (PGG), a main component of gallotannins, was an effective inhibitor of HSA and it exerted similar inhibitory potency to Aleppo tannin used in this study. The inhibition of HSA by PGG was found to be non-competitive and inhibitory constants of KEI = 2.6 ?M and KESI = 3.9 ?M were determined from Lineweaver-Burk secondary plots. PGG as a model compound for gallotannins was selected to study the inhibitory mechanism and to characterize the interaction of HSA with this type of molecules. Surface plasmon resonance (SPR) binding experiments confirmed the direct interaction of HSA and PGG, and it also established similar binding of Aleppo tannin to HSA. Saturation transfer difference (STD) experiment by NMR clearly demonstrated the aromatic rings of PGG may be involved in the interaction suggesting a possible stacking with the aromatic side chains of HSA. The role of aromatic amino acids of HSA in PGG binding was reinforced by kinetic studies with the W58L and Y151M mutants of HSA: the replacement of the active site aromatic amino acids with aliphatic ones decreased the PGG inhibition dramatically, which justified the importance of these residues in the interaction.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Molekulatudomány
pentagalloyl glucose
human salivary alpha-amylase inhibition
surface plasmon resonance
saturation transfer difference
NMR
Megjelenés:Biochimica et Biophysica Acta (BBA). Proteins and Proteomics. - 1794 : 2 (2009), p. 291-296. -
További szerzők:Zajácz Ágnes Bécsi Bálint (1981-) (vegyészmérnök) Ragunath, Chandran Ramasubbu, Narayanan Erdődi Ferenc (1953-) (biokémikus) Batta Gyula (1953-) (molekula-szerkezet kutató) Kandra Lili (1943-) (biokémikus)
Pályázati támogatás:TÁMOP-4.2.2-08/1-2008-0019
TÁMOP
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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4.

001-es BibID:BIBFORM003913
Első szerző:Mádi András (biológus)
Cím:Mass spectrometric proteome analysis suggests anaerobic shift in metabolism of Dauer larvae of Caenorhabditis elegans / András Mádi, Stefan Mikkat, Cornelia Koy, Bruno Ringel, Hans-Jürgen Thiesen, Michael O. Glocker
Dátum:2008
ISSN:1570-9639
Megjegyzések:The Dauer larva is a non-feeding alternative larval stage of some nematodes specialized for long-term survival and dispersal. In this study we compared proteome maps obtained from Dauer larvae with those from the corresponding third larval stage (L3) of the feeding life cycle of C. elegans wild-type strain N2. We demonstrate at the protein level that altered metabolism may participate in longevity determination of Dauers. We detected huge amounts of alcohol dehydrogenase (CE12212) and aldehyde dehydrogenase (CE29809) in Dauer animals, indicating highly active fermentative pathways. Inorganic pyrophosphatase (CE05448) that enables to metabolize pyrophosphate as a high-energy source was over-expressed in Dauers. An interesting differentially expressed protein was phosphatidylethanolamine-binding protein (CE38516) that was found in high abundance in samples from Dauer larvae. Protein synthesis may be lowered in Dauer animals by the reduced expression of splicing factor rsp-3 (CE31089) and methionyl-tRNA synthase (CE34219). We observed significantly lower amounts of the pepsin-like aspartyl protease 1 (CE21681) in non-feeding Dauers, which is in agreement with reduced nutrient digestion. Finally, the hypothetical protein R08E5.2 (CE33294) was present in high abundance in L3 animals.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Metabolism
Fractionated protein extraction
Proteomics
MALDI ToF MS
C. elegans
Megjelenés:Biochimica et Biophysica Acta (BBA). Proteins and Proteomics. - 1784 : 11 (2008), p. 1763-1770. -
További szerzők:Mikkat, Stefan Koy, Cornelia Ringel, Bruno Thiesen, Hans-Jürgen Glocker, Michael O.
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5.

001-es BibID:BIBFORM012809
Első szerző:Shemirani, Amir-Houshang (kutató orvos, laboratórium szakorvos)
Cím:The combined effect of fibrin formation and factor XIII A subunit Val34Leu polymorphism on the activation of factor XIII in whole plasma / Amir H. Shemirani, Gizella Haramura, Zsuzsa Bagoly, László Muszbek
Dátum:2006
ISSN:1570-9639
Megjegyzések:The first step in the activation of blood coagulation factor XIII (FXIII) is the proteolytic cleavage of the potentially active A subunit (FXIII-A) by thrombin at Arg37-Gly38. Both fibrin formation and FXIII-AVal34Leu polymorphism influence the rate of proteolytic activation of purified factor XIII, however their relative importance and interaction in determining the time of onset and the rate of FXIII activation in whole plasma have not yet been explored. In the present study it was shown that in plasma, fibrin formation preceded the truncation of FXIII-A by thrombin, the activation process took place exclusively on the surface of newly formed fibrin and activated FXIII remained associated with the fibrin clot. The time of fibrin formation closely correlated with the time of FXIII activation, while there was no significant relationship between the time of FXIII activation and FXIII-AVal34Leu genotype. However, in the case of Leu34 variant the lag phase between fibrin formation and FXIII-A truncation was significantly shorter than in the case of Val34 variant. The results suggest that in whole plasma the onset of FXIII activation is determined by fibrin formation, while the rate of activation is modulated by Val34Leu polymorphism.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Factor XIII Val34Leu polymorphism
Fibrinogen
Fibrin polymerization
Thrombin
Transglutaminase
Megjelenés:Biochimica et Biophysica Acta (BBA). Proteins and Proteomics. - 1764 : 8 (2006), p. 1420-1423. -
További szerzők:Haramura Gizella (1957-) (vezető analitikus) Bagoly Zsuzsa (1978-) (orvos) Muszbek László (1942-) (haematológus, kutató orvos)
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Intézményi repozitóriumban (DEA) tárolt változat
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6.

001-es BibID:BIBFORM082447
Első szerző:Tüű-Szabó Boldizsár
Cím:Altered dynamics may drift pathological fibrillization in membraneless organelles / B. Tüű-Szabó, G. Hoffka, N. Duro, M. Fuxreiter
Dátum:2019
ISSN:1570-9639
Megjegyzések:Protein phase transition can generate non-membrane bound cellular compartments, which can convert from liquid-like to solid-like states. While the molecular driving forces of phase separation have been largely understood, much less is known about the mechanisms of material-state conversion. We apply a recently developed algorithm to describe the weak interaction network of multivalent motifs, and simulate the effect of pathological mutations. We demonstrate that linker dynamics is critical to the material-state of biomolecular condensates. We show that linker flexibility/mobility is a major regulator of the weak, heterogeneous meshwork of multivalent motifs, which promotes phase transition and maintains a liquid-like state. Decreasing linker dynamics increases the propensity of amyloid-like fragments via hampering the motif-exchange and reorganization of the weak interaction network. In contrast, increasing linker mobility may compensate rigidifying mutations, suggesting that the meshwork of weak, variable interactions may provide a rescue mechanism from aggregation. Motif affinity, on the other hand, has a moderate impact on fibrillization. Here we demonstrate that the fuzzy framework provides an efficient approach to handle the intricate organization of membraneless organelles, and could also be applicable to screen for pathological effects of mutations.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Matematikai és természettudományok - Kémiai tudományok
Megjelenés:Biochimica et Biophysica Acta (BBA). Proteins and Proteomics. - 1867 : 10 (2019), p. 988-998. -
További szerzők:Hoffka Gyula (1992-) (vegyész) Duró Norbert (1990-) (biotechnológus) Fuxreiter Mónika (1969-) (kutató vegyész)
Pályázati támogatás:GINOP-2.3.2-15-2016-00044
GINOP
MTA-DE Lendület
MTA
Fehérjedinamikai Kutatócsoport
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