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001-es BibID:BIBFORM077292
035-os BibID:(WoS)000466621200053 (Scopus)85061541042
Első szerző:Hajdu Dorottya (biológus)
Cím:Solution structure and novel insights into phylogeny and mode of action of the Neosartorya (Aspergillus) fischeri antifungal protein (NFAP) / Hajdu Dorottya, Huber Anna, Czajlik András, Tóth Liliána, Kele Zoltán, Kocsubé Sándor, Fizil Ádám, Marx Florentine, Galgóczy László, Batta Gyula
Dátum:2019
ISSN:0141-8130
Megjegyzések:Small, cysteine-rich and cationic antifungal proteins fromnatural sources are promising candidates for the development of novel treatment strategies to prevent and combat infections caused by drug-resistant fungi. However, limited information about their structure and antifungal mechanism hampers their future applications. In the present study, we determined the solution structure, dynamics and associated solvent areas of the Neosartorya (Aspergillus) fischeri antifungal protein NFAP. Genome mining within the genus revealed the presence of orthologous genes in N. fischeri and Neosartorya spathulata, and genes encoding closely related proteins can be found in Penicillium brasiliensis and Penicillium oxalicum. We show that the tertiary structure of these putative proteins can be resolved using the structure of NFAP as reliable template for in silico prediction. Localization studies with fluorescence-labelled protein pointed at an energy-dependent uptake mechanism of NFAP in the sensitive model fungus Neurospora crassa and subsequent cytoplasmic localization coincided with cell-death induction. The presented results contribute to a better understanding of the structure/function relationship of NFAP and related proteins and pave the way towards future antifungal drug development.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Neosartorya (Aspergillus) fischeri antifungal
protein (NFAP)
Nuclear magnetic resonance (NMR)
Antifungal mechanism
Megjelenés:International Journal of Biological Macromolecules. - 129 (2019), p. 511-522.
További szerzők:Huber Anna Czajlik András (1975-) (gyógyszerész) Tóth Liliána Kele Zoltán Kocsubé Sándor Fizil Ádám (1988-) (biológus) Marx, Florentine Galgóczy László (1950-) Batta Gyula (1953-) (molekula-szerkezet kutató)
Pályázati támogatás:GINOP-2.3.2-15-2016-00008
GINOP
GINOP-2.3.3-15-2016-00004
GINOP
PD 120808
OTKA
ANN 122833
OTKA
ANN 110821
OTKA
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2.

001-es BibID:BIBFORM099343
035-os BibID:(WoS)000608018200036 (Scopus)85097787135
Első szerző:Hámori Csaba (vegyész)
Cím:Colorado potato beetle alpha-amylase: Purification, action pattern and subsite mapping for exploration of active centre / Hámori Csaba, Remenyik Judit, Kandra Lili, Gyémánt Gyöngyi
Dátum:2021
ISSN:0141-8130
Megjegyzések:Colorado potato beetle is an invasive insect herbivore and one of the most challenging agricultural pests globally. This study is the first characterization of the active centre of Colorado potato beetle (Leptinotarsa decemlineata) alpha-amylase (LdAmy). Bond cleavage frequency values for LdAmy were determined by HPLC product analysis on a chromophore labelled maltooligomer substrate series. Binding energies between amino acid moieties of subsites and glucose residues of substrate were calculated. Active site contains six subsites in the binding region of LdAmy; four glycone- (-4, -3, -2, -1) and two aglycone-binding sites (+1, +2). Subsite map calculation resulted in apparent binding energies -11.8 and - 11.0 kJ/mol for subsites (+2) and (-3), respectively, which revealed very favorable interactions at these positions. Structures of binding sites of LdAmy and mammalian a-amylases show similarity, but there are variations in the binding energies at subsite (-2) and (-4). Differences were interpreted by comparison of amino acid sequences of human salivary alpha-amylase (HSA) and porcine pancreatic alpha-amylase (PPA) and two insect (Leptinotarsa decemlineata and Tenebrio molitor) enzymes. The observed substitution of positively charged His305 in HSA at subsite (-2) with an acidic Asp in LdAmy in the same position may explain the obtained energy reduction.
Tárgyszavak:Agrártudományok Növénytermesztési és kertészeti tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:International Journal Of Biological Macromolecules. - 168 (2021), p. 350-355. -
További szerzők:Gálné Remenyik Judit (1965-) (kémia tanár, okleveles vegyész) Kandra Lili (1943-) (biokémikus) Gyémánt Gyöngyi (1960-) (vegyész)
Pályázati támogatás:GINOP-2.3.2- 15-2016-00008
GINOP
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DOI
Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM116326
035-os BibID:(cikkazonosító)127694 (Scopus)85176460106 (WOS)001112357100001 (Pubmed)37898248
Első szerző:Pregi Emese
Cím:Effect of competitive interactions on the structure and properties of blends prepared from an industrial lignosulfonate polymer / Emese Pregi, Jan Blasius, Dáavid Kun, Oldamur Hollóczki, Béla Pukánszky
Dátum:2024
ISSN:0141-8130
Megjegyzések:To explore the possibility of applying lignin in practice, an industrial lignosulfonate (0?50 vol%) was blended with four ionomers. The concentrations of carboxyl and carboxylate groups were systematically varied in the ethylene-acrylic acid copolymers to study the competition of hydrogen and ionic bonds forming between the components. The mechanical properties of the blends were determined by tensile testing. The structure was investigated by scanning electron microscopy, while deformation and failure processes were studied by acoustic emission measurements and microscopy. Interfacial interactions were quantitatively characterized by analyzing local deformation processes and by evaluating the composition dependence of the tensile strength using appropriate models. Molecular dynamics simulations indicated that carboxylate groups preferably form clusters in the ionomer phase, consequently, the increasing degree of neutralization results in ionomers with more and more self-interactions of components deteriorating ionomer-lignin interactions. The novel combination of experiments, modeling, and simulation was done for the first time on such materials, and it pointed out that the role of hydrogen bonds is more critical in determining blend properties. Blends can be prepared for practical applications with a good combination of stiffness (0.8 GPa), tensile strength (22 MPa), and elongation-at-break (25 %) at 30 vol% lignosulfonate content and 33 % neutralization.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Adhesion
Deformation processes
Interaction
Mechanical properties
Molecular dynamics
Quantitative analysis
Megjelenés:International Journal Of Biological Macromolecules. - 254 (2024), p. 1-8. -
További szerzők:Blasius, Jan Kun Dávid Hollóczki Oldamur (1983-) (okleveles vegyészmérnök) Pukánszky Béla (kémikus)
Pályázati támogatás:OTKA-FK 138823
OTKA
ÚNKP-22-5
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Intézményi repozitóriumban (DEA) tárolt változat
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