% Encoding: UTF-8
@COMMENT{BibTeX export based on data in FAU CRIS: https://cris.fau.de/}
@COMMENT{For any questions please write to cris-support@fau.de}
@article{faucris.203401739,
abstract = {To evaluate if the recently identified antimicrobial milk peptides alpha(S2)-casein(182-207) and alpha(S2)-casein(151-181) can be of physiological or technological relevance, their presence in commercial milk was investigated. Thus, a UHPLC-ESI-MS/MS scheduled multiple reaction monitoring method was developed for quantification using stable isotope-labeled peptides. The developed protocol gave very good linear response (R-2 > 0.99) for both peptides, recovery > 95% and coefficients of variations of 5.51% and 4.79%. The limits of detection (0.3 nM alpha(S2)-casein(182-207) and 0.5 nM alpha(S2)-casein(151-181)) were low enough to detect both peptides without further enrichment. The highest peptide concentration was recorded in pasteurized milk (1.36 mu M alpha(S2)-casein(182-207) and 0.20 mu M alpha(S2)-casein(151-181)). The concentration of alpha(S2)-casein(182-207) was in a range that was previously reported to act bacteriostatic against Bacillus subtilis. Industrial milk processing led to a significant loss of both peptides resulting in a mean concentration of 0.47 mu M alpha(S2)-casein(182-207) and 0.098 mu M alpha(S2)-casein(151-181) in ultrahigh-temperature milk.},
author = {Liu, Yufang and Pischetsrieder, Monika},
doi = {10.1016/j.foodchem.2018.04.004},
faupublication = {yes},
journal = {Food Chemistry},
keywords = {alpha(S2)-casein(182-207);Antimicrobial peptides;Milk;UHPLC-ESI-MS/MS-sMRM;Absolute quantification},
pages = {15-20},
peerreviewed = {Yes},
title = {{Absolute} quantification of two antimicrobial peptides alpha({S2})-casein(182-207) and alpha({S2})-casein(151-181) in bovine milk by {UHPLC}-{ESI}-{MS}/{MS} in {sMRM} mode},
volume = {261},
year = {2018}
}
@article{faucris.122157244,
abstract = {Hierarchically porous bioactive glass particles (BGPs) were synthesized by a facile sol-gel process using pollen grains as the templates. The synthesized pollen-templated bioactive glass particles (PBGPs) exhibited dual macro-nano porous structure. The macro pores (~1μm) were inherited from the template of pollen grains while the nano pores (~9.5nm) were induced by the intrinsic mechanism of the sol-gel process. PBGPs possessed a high specific surface area (111.4m/g) and pore volume (0.35cm/g). Hydroxyapatite (HA) formation on PBGPs was detected within 3 days after immersion in simulated body fluid (SBF). Due to their larger specific surface area and pore volume, PBGPs could be loaded with more tetracycline hydrochloride (TCH) than non-templated BGPs and conventional melt-derived 45S5 BGPs. In addition, PBGPs exhibited a low initial burst release (within 10% of the loaded amount) within 18h and a sustained release with a two-stage release pattern for up to 6 days in phosphate buffered saline (PBS). The antibacterial assay confirmed that the TCH-loaded PBGPs could release TCH within 5 days, and the released TCH could reach the minimum inhibitory concentration (MIC) against Escherichia coli. MTT assay indicated that PBGPs showed non-cytotoxic effects toward human hepatocellular carcinoma (Hep G2) cells after co-culture for up to 72h in vitro. These results showed that the biocompatible hierarchically macro-nano porous PBGPs are potential for bone regeneration and local drug delivery applications.},
author = {Zheng, Kai and Bortuzzo, Judith Agnes and Liu, Yufang and Li, Wei and Pischetsrieder, Monika and Roether, Judith and Lu, Miao and Boccaccini, Aldo R.},
doi = {10.1016/j.colsurfb.2015.03.038},
faupublication = {yes},
journal = {Colloids and Surfaces B: Biointerfaces},
keywords = {Bio-template; Bioactive glass; Drug delivery; Hierarchical pores},
pages = {825-832},
peerreviewed = {unknown},
title = {{Bio}-templated bioactive glass particles with hierarchical macro-nano porous structure and drug delivery capability},
volume = {135},
year = {2014}
}
@article{faucris.106694544,
abstract = {The promising potential of magnetic polymer microspheres in various biomedical applications has been frequently reported. However, the surface hydrophilicity of superparamagnetic iron oxide nanoparticles (SPIONs) usually leads to poor or even failed encapsulation of SPIONs in hydrophobic polymer microspheres using the emulsion method. In this study, the stability of SPIONs in poly(3-hydroxybutyrate-co-3-hydroxyvalerate) (PHBV) solution was significantly increased after surface modification with lauric acid. As a result, magnetic PHBV microspheres with high encapsulation efficiencies (71.0-87.4%) were prepared using emulsion-solvent extraction/evaporation method. Magnetic resonance imaging (MRI) showed significant contrast for the magnetic PHBV microspheres. The toxicity of these magnetic PHBV microspheres towards human T-lymphoma suspension cells and adherent colon carcinoma HT-29 cells was investigated using flow cytometry, and they were shown to be non-toxic in a broad concentration range. A model drug, tetracycline hydrochloride, was used to demonstrate the drug delivery capability and to investigate the drug release behavior of the magnetic PHBV microspheres. The drug was successfully loaded into the microspheres using lauric acid-coated SPIONs as drug carrier, and was released from the microspheres in a diffusion controlled manner. The developed magnetic PHBV microspheres are promising candidates for biomedical applications such as targeted drug delivery and MRI.},
author = {Li, Wei and Zaloga, Jan and Ding, Yaping and Liu, Yufang and Janko, Christina and Pischetsrieder, Monika and Alexiou, Christoph and Boccaccini, Aldo R.},
doi = {10.1038/srep23140},
faupublication = {yes},
journal = {Scientific Reports},
peerreviewed = {Yes},
title = {{Facile} preparation of multifunctional superparamagnetic {PHBV} microspheres containing {SPIONs} for biomedical applications},
volume = {6},
year = {2016}
}
@article{faucris.108255444,
abstract = {Health-promoting effects of kefir may be partially caused by bioactive peptides. To evaluate their formation or degradation during gastrointestinal digestion, we monitored changes of the peptide profile in a model of (1) oral, (2) gastric, and (3) small intestinal digestion of kefir. Matrix-assisted laser desorption/ionization time-of-flight mass spectroscopy analyses revealed clearly different profiles between digests 2/3 and kefir/digest 1. Subsequent ultraperformance liquid chromatography-electrospray ionization-tandem mass spectrometry identified 92 peptides in total (25, 25, 43, and 30, partly overlapping in kefir and digests 1, 2, and 3, respectively), including 16 peptides with ascribed bioactivity. Relative quantification in scheduled multiple reaction monitoring mode showed that many bioactive peptides were released by simulated digestion. Most prominently, the concentration of angiotensin-converting enzyme inhibitor β-casein203-209 increased approximately 10 000-fold after combined oral, gastric, and intestinal digestion. Thus, physiological digestive processes may promote bioactive peptide formation from proteins and oligopeptides in kefir. Furthermore, bioactive peptides present in certain compartments of the gastrointestinal tract may exert local physiological effects.},
author = {Liu, Yufang and Pischetsrieder, Monika},
doi = {10.1021/acs.jafc.6b05385},
faupublication = {yes},
journal = {Journal of agricultural and food chemistry},
keywords = {Kefir; peptide profile; bioactive peptides; gastrointestinal digestion},
pages = {1865-1873},
peerreviewed = {unknown},
title = {{Identification} and {Relative} {Quantification} of {Bioactive} {Peptides} {Sequentially} {Released} during {Simulated} {Gastrointestinal} {Digestion} of {Commercial} {Kefir}.},
volume = {65},
year = {2017}
}
@article{faucris.107009144,
abstract = {In this study, highly monodispersed spherical bioactive glass nanoparticles (BGS) with a particle size of 408 $±$ 36 nm were synthesized using a modified Stöber method. The BGS was then functionalized with lysozyme (LY) via a simple electrostatic interaction routine under selected conditions. The LY-functionalized BGS (LY-BGS) exhibited monodispersity, spherical morphology and homogeneity in size. The incorporated content of LY could be tailored conveniently by adjusting the initial concentration of the LY precursor for functionalization. Hydroxyapatite (HA) formed on the LY-BGS after soaking in simulated body fluid (SBF) for 7 d, but the formation was retarded compared to the non-functionalized BGS. The LY-BGS showed antibacterial activity towards Gram-positive B. subtilis and >90% of the bacteria was killed within 24 h after culture with the LY-BGS at a concentration of 1 mg ml$-$1. The LY-BGS also showed cytotoxicity towards the human hepatocellular carcinoma (HepG2) cell line. In addition, the relative cytotoxicity increased with an increase in the concentration of the LY-BGS in contact with the cells. As a comparison, the LY-BGS exhibited reduced or no cytotoxicity towards human umbilical vein endothelial cells (HUVECs) at the same concentration with respect to the HepG2 groups. Notably, the relative cell viability of HepG2 was 45.9% after exposure to the LY-BGS at a concentration of 10 \textgreekmg ml$-$1 for 24 h, while no decrease in relative viability for the HUVECs was observed under the same conditions. This cytotoxicity window between cancerous cells and healthy cells could be expected for cancer treatment. Furthermore, the antibacterial properties and the bioactivity of LY-BGS make it a promising material for biomedical applications, particularly in the treatment of bone defects caused by tumors.},
author = {Zheng, Kai and Lu, Miao and Liu, Yufang and Chen, Qiang and Taccardi, Nicola and Hueser, Norbert and Boccaccini, Aldo R.},
doi = {10.1088/1748-6041/11/3/035012},
faupublication = {yes},
journal = {Biomedical Materials},
keywords = {antibacterial activity; anticancer activity; bioactive glasses; lysozyme; nanocomposites},
peerreviewed = {Yes},
title = {{Monodispersed} lysozyme-functionalized bioactive glass nanoparticles with antibacterial and anticancer activities},
volume = {11},
year = {2016}
}
@article{faucris.217011535,
abstract = {Casein phosphopeptides are multiphosphorylated
milk peptides, which can have anticariogenic activity and improve mineral
absorption by binding bivalent metal ions. The present study investigated
phosphopeptides in kefir, because fermentation may lead to their enhanced
release from milk proteins. After selective enrichment by hydroxyapatite
extraction, phosphopeptides and their phosphorylation degree were identified by
MALDI-TOF-MS before and after enzymatic dephosphorylation. Peptide structures
were determined by UHPLC–ESI–MS/MS revealing 27 phosphopeptides in kefir,
including nine peptides containing the motif pSpSpSEE, which binds minerals most
efficiently. The majority (18) of phosphopeptides derived from β-casein,
but only three from the most abundant milk protein αs1-casein.
After simulated gastrointestinal digestion,
MALDI-TOF-MS analysis detected eight putative phosphopeptides in kefir; four of
which were assigned by UHPLC–ESI–MS/MS to αs2-casein124-133,
αs2-casein137-146, β-casein30-40,
and κ-casein147-161. These results indicate that kefir is a good
dietary source of multiphosphorylated peptide},
author = {Savastano, Maria Luisa and Liu, Yufang and Ebner, Jennifer and Dittrich, Daniel and Haus, Sabrina and Gensberger-Reigl, Sabrina and Pischetsrieder, Monika},
doi = {10.1021/acsomega.8b03105},
faupublication = {yes},
journal = {ACS Omega},
keywords = {casein phosphopeptides; gastrointestinal digestion; kefir; MALDI-TOF-MS; pSpSpSEE; UHPLC–ESI–MS/MS},
pages = {7963-7970},
peerreviewed = {Yes},
title = {{Profiling} of multiphosphorylated peptides in kefir and their release during simulated gastrointestinal digestion},
url = {https://pubs.acs.org/doi/10.1021/acsomega.8b03105},
volume = {4},
year = {2019}
}
@article{faucris.119564544,
author = {Kozon, Dominika and Zheng, Kai and Boccardi, Elena and Liu, Yufang and Liverani, Liliana and Boccaccini, Aldo R.},
doi = {10.3390/ma9040225},
faupublication = {yes},
journal = {Materials},
keywords = {Antibacterial activity; Bioactive glass nanoparticle; Bioactivity; Silver; Surface modification},
peerreviewed = {Yes},
title = {{Synthesis} of monodispersed {Ag}-doped bioactive glass nanoparticles via surface modification},
volume = {9},
year = {2016}
}
@article{faucris.114022304,
abstract = {Scope: Milk provides a wide range of bioactive substances, such as antimicrobial peptides and
proteins. Our study aimed to identify novel antimicrobial peptides naturally present in milk.
Methods and results: The components of an endogenous bovine milk peptide database were
virtually screened for charge, amphipathy, and predicted secondary structure. Thus, 23 of
248 screened peptides were identified as candidates for antimicrobial effects. After commercial
synthesis, their antimicrobial activities were determined against Escherichia coli NEB5 alpha,
E. coli ATCC25922, and Bacillus subtilis ATCC6051. In the tested concentration range (<2
mM), bacteriostatic activity of 14 peptides was detected including nine peptides inhibiting both
Gram-positive and Gram-negative bacteria. The most effective fragment was TKLTEEEKNRLNFLKKISQRYQKFALPQYLK corresponding to alpha(S2)-casein151–181, with minimum inhibitory concentration (MIC) of 4.0 muM against B. subtilis ATCC6051, and minimum inhibitory concentrations of 16.2 M against both E. coli strains. Circular dichroism spectroscopy revealed conformational changes of most active peptides in a membrane-mimic environment, transitioning from an unordered to alpha-helical structure.
Conclusion: Screening of food peptide databases by prediction tools is an efficient method
to identify novel antimicrobial food-derived peptides. Milk-derived antimicrobial peptides may
have potential use as functional food ingredients and help to understand the molecular mechanisms of anti-infective milk effects.},
author = {Liu, Yufang and Eichler, Jutta and Pischetsrieder, Monika},
doi = {10.1002/mnfr.201500182},
faupublication = {yes},
journal = {Molecular Nutrition & Food Research},
keywords = {antimicrobial peptide; circular dichroism; milk; Peptide database; virtual screening},
pages = {2243-2254},
peerreviewed = {Yes},
title = {{Virtual} screening of a milk peptide database for the identification of food-derived antimicrobial peptides},
volume = {59},
year = {2015}
}