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001-es BibID:BIBFORM106470
035-os BibID:(cikkazonosító)1208 (WoS)000915651700001 (Scopus)85146742732
Első szerző:Czajlik András (gyógyszerész)
Cím:DMSO-Induced Unfolding of the Antifungal Disulfide Protein PAF and Its Inactive Variant: A Combined NMR and DSC Study / András Czajlik, Ágnes Batta, Kinga Kerner, Ádám Fizil, Dorottya Hajdu, Mária Raics, Katalin E. Kövér, Gyula Batta
Dátum:2023
ISSN:1422-0067
Megjegyzések:PAF and related antifungal proteins are promising antimicrobial agents. They have highly stable folds around room temperature due to the presence of 3-4 disulfide bonds. However, unfolded states persist and contribute to the thermal equilibrium in aqueous solution, and low-populated states might influence their biological impact. To explore such equilibria during dimethyl sulfoxide (DMSO)-induced chemical unfolding, we studied PAF and its inactive variant PAFD19S using nuclear magnetic resonance (NMR) and differential scanning calorimetry (DSC). According to the NMR monitoring at 310 K, the folded structures disappear above 80 v/v% DMSO concentration, while the unfolding is completely reversible. Evaluation of a few resolved peaks from viscosity-compensated 15N-1H HSQC spectra of PAF yielded G = 23 ± 7 kJ/M as the average value for NMR unfolding enthalpy. The NMR-based structures of PAF and the mutant in 50 v/v% DMSO/H2O mixtures were more similar in the mixed solvents then they were in water. The 15N NMR relaxation dynamics in the same mixtures verified the rigid backbones of the NMR-visible fractions of the proteins; still, enhanced dynamics around the termini and some loops were observed. DSC monitoring of the Tm melting point showed parabolic dependence on the DMSO molar fraction and suggested that PAF is more stable than the inactive PAFD19S. The DSC experiments were irreversible due to the applied broad temperature range, but still suggestive of the endothermic unfolding of PAF.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
antifungal protein
PAF
disulfide bond
DMSO-induced unfolding
nuclear magnetic resonance (NMR)
differential scanning calorimetry (DSC)
Megjelenés:International Journal Of Molecular Sciences. - 24 : 2 (2023), p. 1-13. -
További szerzők:Batta Ágnes Kerner Kinga Fizil Ádám (1988-) (biológus) Hajdu Dorottya (1987-) (biológus) Hadháziné Raics Mária (1991-) (vegyész) Kövér Katalin, E. (1956-2023) (vegyész) Batta Gyula (1953-) (molekula-szerkezet kutató)
Pályázati támogatás:TKP2020-NKA-11
Egyéb
NN 128368
OTKA
GINOP-2.3.2-15-2016-00008
GINOP
GINOP-2.3.3-15-2016-00004
GINOP
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