The In Vitro Activity of Fluconazole, Amphotericin B and Echinocandins Against Cyberlindnera fabianii Planktonic Cells and Biofilms.

Until recently, little was known about the susceptibility pattern of Cyberlindnera fabianii (Cy. fabianii) planktonic cells and biofilms regarding the most frequently administered systemic antifungals, despite the high mortality rate and its potential role in catheter-related infections. In the current study, the activity of fluconazole, amphotericin B and echinocandins (anidulafungin, caspofungin and micafungin) was determined against planktonic and sessile cells of Cy.

The Role of Side Chains in the Fine-Tuning of the Metal-Binding Ability of Multihistidine Peptides.

The systematic studies of copper(II), nickel(II) and zinc(II) ion complexes of protected multihistidine peptides containing amino acids with different side chains (Ac-SarHAH-NH, Ac-HADH-NH, Ac-HDAH-NH, Ac-HXHYH-NH X, Y = A, F, D or K, Ac-HXHAHXH-NH, X = F or D) have provided information about the metal ion and protein interaction and have made it possible to draw conclusions regarding general trends in the coordination of metal complexes of multihistidine peptides. The stability of the metal complexes significantly depends on the position of the histidines and amino acids, which are present in the neighbourhood of the histidine amino acids as well. The most significant effect was observed on peptides containing aspartic acid or phenylalanine.

Thermodynamics and structural characterization of the nickel(II) and zinc(II) complexes of various peptide fragments of tau protein.

Nickel(II) and zinc(II) complexes of various peptide fragments of tau protein have been investigated by potentiometric, UV-Vis, CD and ESI-MS techniques. The peptides include the native fragment tau(9-16) (Ac-EVMEDHAG-NH), and the Gln/Lys and Tyr/Ala mutated peptides (Ac-KGGYTMHK-NH and Ac-KGGATMHK-NH) of tau(26-33). Similar to copper(II) the complexes of a chimeric peptide containing both His14 and His32 residues in one molecule (Ac-EDHAGTMHQD-NH) were also studied.

Copper (II) binding properties of an octapeptide fragment from the R3 region of tau protein: A combined potentiometric, spectroscopic and mass spectrometric study.

The copper(II) complexes of a peptide fragment of the R3 domain of tau protein (tau(326-333) Ac-GNIHHKPG-NH) and its mutants (Ac-GNGHHKPG-NH, Ac-GNIHHKAG-NH, Ac-GNGAHKPG-NH and Ac-GNGHAKPG-NH) have been studied by potentiometric and spectroscopic (UV-Vis, CD) methods. ESR spectroscopy and mass spectrometry were also used to prove the coordination mode of the mononuclear complexes and the formation of dinuclear species, respectively. It has been demonstrated that the (326-333) fragment of tau protein is a versatile and effective ligand for copper(II) coordination.

Follow-up Study of Microflora Changes in Crevicular Gingival Fluid in Obese Subjects After Bariatric Surgery.

The objective of our study was to investigate the effect of weight loss on the crevicular microflora following bariatric surgery. Crevicular fluid samples were taken from 57 subjects: 22 were in the normal control group; 18 in the obese control group; and 17 patients had had bariatric surgery, who underwent a repeat sampling 6 to 12 months after the operation. Crevicular fluid samples were analyzed by MALDI-TOF MS analysis.