TY  - JOUR
AU  - Taneva, Stefka G.
AU  - Krumova, Sashka
AU  - Bogár, Ferenc
AU  - Kincses, András
AU  - Stoichev, Svetozar
AU  - Todinova, Svetla
AU  - Danailova, Avgustina
AU  - Horváth, János
AU  - Násztor, Zoltán
AU  - Kelemen, Lóránd
AU  - Dér, András
TI  - Insights into graphene oxide interaction with human serum albumin in isolated state and in blood plasma
JF  - INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
J2  - INT J BIOL MACROMOL
VL  - 175
PY  - 2021
SP  - 19
EP  - 29
PG  - 11
SN  - 0141-8130
DO  - 10.1016/j.ijbiomac.2021.01.151
UR  - https://m2.mtmt.hu/api/publication/31876643
ID  - 31876643
LA  - English
DB  - MTMT
ER  - 

TY  - THES
AU  - Násztor, Zoltán
TI  - A Hofmeister effektus vizsgálata szimulációs módszerekkel [Investigation of the Hofmeister effect utilizing computational tools]
PB  - Szegedi Tudományegyetem (SZTE)
PY  - 2020
SP  - 104
DO  - 10.14232/phd.10377
UR  - https://m2.mtmt.hu/api/publication/31364361
ID  - 31364361
LA  - Hungarian
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Násztor, Zoltán
AU  - Dér, András
AU  - Bogár, Ferenc
TI  - Ion-induced alterations of the local hydration environment elucidate Hofmeister effect in a simple classical model of Trp-cage miniprotein
JF  - JOURNAL OF MOLECULAR MODELING
J2  - J MOL MODEL
VL  - 23
PY  - 2017
IS  - 10
PG  - 14
SN  - 1610-2940
DO  - 10.1007/s00894-017-3471-0
UR  - https://m2.mtmt.hu/api/publication/3271940
ID  - 3271940
AB  - Protein stability is known to be influenced by the presence of Hofmeister active ions in the solution. In addition to direct ion-protein interactions, this influence manifests through the local alterations of the interfacial water structure induced by the anions and cations present in this region. In our earlier works it was pointed out that the effects of Hofmeister active salts on the stability of Trp-cage miniprotein can be modeled qualitatively using non-polarizable force fields. These simulations reproduced the structure-stabilization and structure-destabilization effects of selected kosmotropic and chaotropic salts, respectively. In the present study we use the same model system to elucidate atomic processes behind the chaotropic destabilization and kosmotropic stabilization of the miniprotein. We focus on changes of the local hydration environment of the miniprotein upon addition of NaClO4 and NaF salts to the solution. The process is separated into two parts. In the first, ‘promotion’ phase, the protein structure is fixed, and the local hydration properties induced by the simultaneous presence of protein and ions are investigated, with a special focus on the interaction of Hofmeister active anions with the charged and polar sites. In the second, ‘rearrangement’ phase we follow changes of the hydration of ions and the protein, accompanying the conformational relaxation of the protein. We identify significant factors of an enthalpic and entropic nature behind the ion-induced free energy changes of the protein-water system, and also propose a possible atomic mechanism consistent with the Collins’s rule, for the chaotropic destabilization and kosmotropic stabilization of protein conformation.
LA  - English
DB  - MTMT
ER  - 

TY  - CHAP
AU  - Násztor, Zoltán
AU  - Der, A
AU  - Bogár, Ferenc
ED  - Jampilek, J
ED  - Marvanová, P
TI  - The Collins's Rule and the Hofmeister Effect as Revealed by a Simple Molecular Dynamics Model
T2  - 8th Central European Conference "Chemistry towards Biology"
PB  - University of Veterinary Medicine, Budapest
CY  - Brno
SN  - 9788073057770
PY  - 2016
SP  - 52
PG  - 1
UR  - https://m2.mtmt.hu/api/publication/3149059
ID  - 3149059
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Horváth, János
AU  - Násztor, Zoltán
AU  - Bartha, Ferenc
AU  - Bogár, Ferenc
AU  - Leitgeb, Balázs
TI  - Characterizing the structural and folding properties of long-sequence hypomurocin B peptides and their analogs
JF  - BIOPOLYMERS
J2  - BIOPOLYMERS
VL  - 106
PY  - 2016
IS  - 5
SP  - 645
EP  - 657
PG  - 13
SN  - 0006-3525
DO  - 10.1002/bip.22870
UR  - https://m2.mtmt.hu/api/publication/3104900
ID  - 3104900
N1  - Hungarian Academy of Sciences, Institute of Biophysics, Biological Research Centre, Temesvári Krt. 62, Szeged, H-6726, Hungary            
            Faculty of Medicine, Department of Medical Chemistry, University of Szeged, Dóm Tér 8, Szeged, H-6720, Hungary            
            MTA-SZTE Supramolecular and Nanostructured Materials Research Group of Hungarian Academy of Sciences, University of Szeged, Dóm tér 8, Szeged, H-6720, Hungary            
            Faculty of Science and Informatics, Department of Microbiology, University of Szeged, Közép Fasor 52, Szeged, H-6726, Hungary            
            Cited By :2            
            Export Date: 12 December 2019            
            CODEN: BIPMA            
            Correspondence Address: Leitgeb, B.; Hungarian Academy of Sciences, Institute of Biophysics, Biological Research Centre, Temesvári Krt. 62, Hungary; email: leitgeb.balazs@brc.mta.hu
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Násztor, Zoltán
AU  - Bogár, Ferenc
AU  - Dér, András
TI  - The interfacial tension concept, as revealed by fluctuations
JF  - CURRENT OPINION IN COLLOID & INTERFACE SCIENCE
J2  - CURR OPIN COLLOID IN
VL  - 23
PY  - 2016
SP  - 29
EP  - 40
PG  - 12
SN  - 1359-0294
DO  - 10.1016/j.cocis.2016.05.007
UR  - https://m2.mtmt.hu/api/publication/3077934
ID  - 3077934
AB  - Abstract A simple, didactic model that could have conclusively interpreted the complexity of specific salt (Hofmeister-) effects on protein solubility and function, using a single physical quantity as a central parameter, has long been missing. Via surveying a row of recent papers we show in this review that a phenomenological formalism based on the salt-induced change of protein–water interfacial tension (∆γ) is able to account for a wide range of Hofmeister effects, including also such “exceptions”, where inverse or “V-shaped” Hofmeister series occurs. A close relationship between protein–water interfacial tension and conformational fluctuations is pinpointed on theoretical grounds, then it is shown how one can use a complex experimental arsenal to demonstrate conformational fluctuations on two prototypical proteins, the membrane protein bacteriorhodopsin and the cytoplasmic protein myoglobin. Finally, via the results of recent and new molecular dynamics simulations on a model peptide, the tryptophan-cage miniprotein, independent evidences are given in favor of the interfacial tension concept, at the same time demonstrating the predictive power of the theory. It is shown that salt-induced fluctuation changes of surface-exposed amino acid groups can be used as a sensitive measure for mapping the local features of Hofmeister effects on protein conformations. General implications of the interfacial tension concept are also discussed.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Násztor, Zoltán
AU  - Horváth, János
AU  - Leitgeb, Balázs
TI  - Studying the Structural and Folding Features of Long-Sequence Trichobrachin Peptides
JF  - CHEMISTRY & BIODIVERSITY
J2  - CHEM BIODIVERS
VL  - 12
PY  - 2015
IS  - 9
SP  - 1365
EP  - 1377
PG  - 13
SN  - 1612-1872
DO  - 10.1002/cbdv.201400280
UR  - https://m2.mtmt.hu/api/publication/2974666
ID  - 2974666
N1  - Cited By :1            
            Export Date: 11 February 2020            
            CODEN: CBHIA            
            Correspondence Address: Leitgeb, B.; Institute of Biophysics, Biological Research Centre, Hungarian Academy of Sciences, Temesvári krt. 62, Hungary
AB  - In this theoretical study, the folding processes of long-sequence trichobrachin peptides (i.e., TB IIb peptides) were investigated by molecular dynamics methods. The formation of various helical structures (i.e., 3<inf>10</inf>-, α-, and left-handed α-helices) was studied with regard to the entire sequence of peptides, as well as to each amino acid. The results pointed out that TB IIb molecules showed a propensity to form helical conformations, and they could be characterized by 3<inf>10</inf>-helical structure rather than by α-helical structure. The formation of local (i.e., i←i+3 and i←i+4) as well as of non-local (i.e., i←i+n, where n>4; and all i→i+n) H-bonds was also examined. The results revealed that the occurrence of local, helix-stabilizing H-bonds was in agreement with the appearance of helical conformations, and the non-local H-bonds did not produce relevant effects on the evolution of helical structures. Based on the data obtained by our structural investigation, differences were observed between the TB IIb peptides, according to the type of amino acid located in the 17th position of their sequences. In summary, the folding processes were explored for TB IIb molecules, and our theoretical study led to the conclusion that these long-sequence peptaibols showed characteristic structural and folding features. © 2015 Verlag Helvetica Chimica Acta AG, Zrich.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Bogár, Ferenc
AU  - Simon, Dóra
AU  - Bozsó, Zsolt
AU  - Janáky, Tamás
AU  - Veszelka, Szilvia
AU  - Tóth, Andrea
AU  - Deli, Mária Anna
AU  - Borics, Attila
AU  - Násztor, Zoltán
AU  - Gyebrovszki, A
AU  - Penke, Botond
AU  - Fülöp, Lívia
TI  - Opposite effect of Ca2+/Mg2+ ions on the aggregation of native and precursor-derived Aβ42
JF  - STRUCTURAL CHEMISTRY
J2  - STRUCT CHEM
VL  - 26
PY  - 2015
IS  - 5-6
SP  - 1389
EP  - 1403
PG  - 15
SN  - 1040-0400
DO  - 10.1007/s11224-015-0660-2
UR  - https://m2.mtmt.hu/api/publication/2942329
ID  - 2942329
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Násztor, Zoltán
AU  - Horváth, János
AU  - Leitgeb, Balázs
TI  - In Silico Conformational Analysis of the Short-Sequence Hypomurocin A Peptides
JF  - INTERNATIONAL JOURNAL OF PEPTIDES
J2  - INT J PEPTIDES
VL  - 2015
PY  - 2015
PG  - 6
SN  - 1687-9767
DO  - 10.1155/2015/281065
UR  - https://m2.mtmt.hu/api/publication/2807137
ID  - 2807137
N1  - Admin megjegyzés-24425328
#JournalID1#
Name: INT J PEPT
ISSN: 1687-9767
#JournalID2#
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Bogár, Ferenc
AU  - Bartha, Ferenc
AU  - Násztor, Zoltán
AU  - Fábián, László
AU  - Leitgeb, Balázs
AU  - Dér, András
TI  - On the Hofmeister Effect: Fluctuations at the Protein-Water Interface and the Surface Tension.
JF  - JOURNAL OF PHYSICAL CHEMISTRY B
J2  - J PHYS CHEM B
VL  - 118
PY  - 2014
IS  - 29
SP  - 8496
EP  - 8504
PG  - 9
SN  - 1520-6106
DO  - 10.1021/jp502505c
UR  - https://m2.mtmt.hu/api/publication/2711661
ID  - 2711661
AB  - We performed mol. dynamics simulations on the tryptophane-cage miniprotein using a nonpolarizable force field, in order to model the effect of concd. water solns. of neutral salts on protein conformation, which is a manifestation of Hofmeister effects. From the equil. values and the fluctuations of the solvent accessible surface area of the miniprotein, the salt-induced changes of the mean value of protein-water interfacial tension were detd. At 300 K, the chaotropic ClO4- and NO3- decreased the interfacial tension according to their position in the Hofmeister series (by approx. 5 and 2.7 mN/m, resp.), while the kosmotropic F- increased it (by 1 mN/m). These values were compared to those obtained from the Gibbs equation using the excess surface adsorption calcd. from the probability distribution of the water mols. and ions around the miniprotein, and the two sets were found to be very close to each other. Our results present a direct evidence for the central role of interfacial tension and fluctuations at the protein-water interface in Hofmeister phenomena, and provide a computational method for the detn. of the protein-water interfacial tension, establishing a link between the phenomenol. and microscopic description of protein-water interfaces. [on SciFinder(R)]
LA  - English
DB  - MTMT
ER  -