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1. Full Text Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk protein-derived dipeptides and hydrolysates
by Nongonierma, Alice B and FitzGerald, Richard J
Peptides, ISSN 0196-9781, 01/2013, Volume 39, Issue 1, pp. 157 - 163
► Antioxidant and DPP-IV inhibitory dipeptides/milk-protein hydrolysates were studied. ► 8 dipeptides and 5 milk protein hydrolysates could inhibit DDP-IV. ►... 
Lactoferrin | Tryptophan | Superoxide | Antioxidant | Dipeptidyl peptidase IV inhibitors | 2,2-diphenyl-1-picrylhydrazyl (DPPH) | Bioactive peptides | BIOCHEMISTRY & MOLECULAR BIOLOGY | WHEY-PROTEIN | BLOOD-GLUCOSE | CO-INGESTION | INSULIN RESPONSES | IDENTIFICATION | HPLC-MS/MS | AMINO-ACIDS | PHARMACOLOGY & PHARMACY | CASEIN | ACTIVE PEPTIDES | CONVERTING-ENZYME | Free Radical Scavengers - chemistry | Free Radicals - chemistry | Superoxides - chemistry | Dipeptidyl-Peptidase IV Inhibitors - chemistry | Dipeptides - chemistry | Hydrolysis | Superoxide Dismutase - chemistry | Lactoferrin - chemistry | Peptide Fragments - chemistry | Animals | Milk Proteins - chemistry | Caseins - chemistry | Cattle | Picrates - chemistry | Whey Proteins | Biphenyl Compounds - chemistry | Sus scrofa | Antioxidants | Peptides | Analysis | Protein hydrolysates | Lactoferrins | Milk
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2. Full Text Lactoferrin: A natural glycoprotein involved in iron and inflammatory homeostasis
by Rosa, Luigi and Cutone, Antimo and Lepanto, Maria Stefania and Paesano, Rosalba and Valenti, Piera
International Journal of Molecular Sciences, ISSN 1661-6596, 09/2017, Volume 18, Issue 9, p. 1985
Human lactoferrin (hLf), an iron-binding multifunctional cationic glycoprotein secreted by exocrine glands and by neutrophils, is a key element of host... 
Lactoferrin | Cytokines | Anemia | Homeostasis | Inflammation | Iron | Athletes | Oral care | STREPTOCOCCUS-MUTANS | HUMAN-MILK LACTOFERRIN | PORPHYROMONAS-GINGIVALIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | oral care | athletes | MATERNAL SERUM INTERLEUKIN-6 | CHEMISTRY, MULTIDISCIPLINARY | anemia | 3-DIMENSIONAL STRUCTURE | homeostasis | inflammation | PSEUDOMONAS-AERUGINOSA | lactoferrin | iron | cytokines | HEPCIDIN EXPRESSION | BINDING-PROPERTIES | BOVINE LACTOFERRIN | Anti-Infective Agents - metabolism | Anti-Infective Agents - pharmacology | Humans | Glycoproteins - metabolism | Structure-Activity Relationship | Glycoproteins - pharmacology | Anti-Inflammatory Agents - metabolism | Inflammation - complications | Inflammation - metabolism | Lactoferrin - pharmacology | Anti-Infective Agents - chemistry | Female | Glycoproteins - chemistry | Premature Birth - prevention & control | Anemia - etiology | Glycoproteins - genetics | Lactoferrin - metabolism | Anti-Inflammatory Agents - pharmacology | Anemia, Iron-Deficiency - etiology | Iron - chemistry | Premature Birth - metabolism | Iron - metabolism | Lactoferrin - genetics | Pregnancy | Anemia - metabolism | Lactoferrin - chemistry | Animals | Anti-Inflammatory Agents - chemistry | Inflammation - genetics | Protein Binding | Oral Health | Anemia, Iron-Deficiency - metabolism | Transferrin | Glands | Interleukin | Ferritin | Homology | Interleukin 6 | Next-generation sequencing | Bacteria | Supplementation | Binding | Antiinflammatory agents | Dietary supplements | Glycoprotein | Oral administration | Cures | Leukocytes (neutrophilic) | Exocrine glands | Biofilms
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3. Full Text Susceptibility of milk protein-derived peptides to dipeptidyl peptidase IV (DPP-IV) hydrolysis
by Nongonierma, Alice B and FitzGerald, Richard J
Food Chemistry, ISSN 0308-8146, 02/2014, Volume 145, pp. 845 - 852
[Display omitted] •In silico digestion of caseins allowed identification of DPP-IV peptide substrates.•DPP-IV could cleave peptides with a Pro at position 2 in... 
Prodrug-type inhibition | Substrate-type inhibition | Antioxidant | Dipeptidyl peptidase IV inhibitors | Bioactive peptides | Milk | INHIBITORY PEPTIDES | FOOD SCIENCE & TECHNOLOGY | ASSIMILATION | BETA-LACTOGLOBULIN | NUTRITION & DIETETICS | CASEIN | CHEMISTRY, APPLIED | Dipeptidyl Peptidase 4 - metabolism | Protein Hydrolysates - metabolism | Expert Systems | Free Radical Scavengers - chemistry | Dipeptidyl Peptidase 4 - chemistry | Caseins - metabolism | Milk Proteins - chemistry | Caseins - chemistry | Cattle | Proteolysis | Dipeptidyl-Peptidase IV Inhibitors - metabolism | Whey Proteins | Protein Stability | Oligopeptides - chemistry | Milk Proteins - metabolism | Amino Acid Sequence | Lactoferrin - metabolism | Peptide Fragments - metabolism | Protein Hydrolysates - chemistry | Free Radical Scavengers - metabolism | Computational Biology | Dipeptidyl-Peptidase IV Inhibitors - chemistry | Digestion | Oligopeptides - metabolism | Lactoferrin - chemistry | Peptide Fragments - chemistry | Animals | Models, Biological | Sus scrofa | Hydrolysis | Milk proteins | Peptides
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4. Full Text Bioinorganic Chemistry of Bismuth and Antimony:  Target Sites of Metallodrugs
by Ge, Ruiguang and Sun, Hongzhe
Accounts of Chemical Research, ISSN 0001-4842, 04/2007, Volume 40, Issue 4, pp. 267 - 274
The biocoordination chemistry of antimony and bismuth has been extensively investigated due to the historical use of these metals in medicine. Structures of... 
PENTAVALENT ANTIMONY | TRANSFERRIN | HELICOBACTER-PYLORI INFECTION | CRYSTAL-STRUCTURE | BLOOD-PLASMA | HISTIDINE-RICH PROTEIN | LEISHMANIA-DONOVANI | TRYPANOTHIONE | CHEMISTRY, MULTIDISCIPLINARY | SB-V | AQUEOUS-SOLUTION | Enzymes - chemistry | Glutathione - metabolism | Spermidine - analogs & derivatives | Spermidine - metabolism | Spermidine - chemistry | Urease - chemistry | Nucleotides - chemistry | Antimony - metabolism | Bismuth - chemistry | Spectrometry, Mass, Electrospray Ionization | Time Factors | Drug Design | Molecular Structure | Enzymes - metabolism | Lactoferrin - metabolism | Glutathione - analogs & derivatives | Magnetic Resonance Spectroscopy | Antimony - chemistry | Nucleotides - metabolism | Lactoferrin - chemistry | Proteins - metabolism | Transferrin - chemistry | Bismuth - metabolism | Protein Binding | Urease - metabolism | Cations | Glutathione - chemistry | Proteins - chemistry | Transferrin - metabolism | X-ray crystallography | Analysis | Bismuth | Nuclear magnetic resonance spectroscopy | Liquid chromatography | Chemical properties | Structure | Observations
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5. Full Text Effect of the incorporation of antimicrobial/antioxidant proteins on the properties of potato starch films
by Moreno, Olga and Atarés, Lorena and Chiralt, Amparo
Carbohydrate Polymers, ISSN 0144-8617, 11/2015, Volume 133, pp. 353 - 364
•Lactoferrin and lysozyme in potato starch films increased glass transition temperature.•Films with proteins were more brittle and less extensible, regardless... 
Bioactive properties | Lactoferrin | Lysozyme | Edible films | Potato starch | ANTIOXIDANT ACTIVITY | POLYMER SCIENCE | CHEMISTRY, ORGANIC | FATTY-ACIDS | COMPOSITES | EDTA | VAPOR BARRIER PROPERTIES | CORN STARCH | CHEMISTRY, APPLIED | CELLULOSE | BOVINE LACTOFERRIN | Temperature | Starch - pharmacology | Antioxidants - chemistry | Muramidase - chemistry | Anti-Infective Agents - pharmacology | Optical Phenomena | Antioxidants - pharmacology | Permeability | Lactoferrin - chemistry | Starch - chemistry | Anti-Infective Agents - chemistry | Solanum tuberosum - chemistry | Oxygen - chemistry | Water - chemistry | Proteins | Analysis | Lactoferrins | Antioxidants | Thermoplastics | Potatoes | Escherichia coli
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6. Full Text The proton permeability of self-assembled polymersomes and their neuroprotection by enhancing a neuroprotective peptide across the blood-brain barrier after modification with lactoferrin
by Yu, Yuan and Jiang, Xinguo and Gong, Shuyu and Feng, Liang and Zhong, Yanqiang and Pang, Zhiqing
Nanoscale, ISSN 2040-3364, 03/2014, Volume 6, Issue 6, pp. 3250 - 3258
Biotherapeutics such as peptides possess strong potential for the treatment of intractable neurological disorders. However, because of their low stability and... 
DRUG | NANOPARTICLES | APOPTOSIS | PHYSICS, APPLIED | VESICLES | MATERIALS SCIENCE, MULTIDISCIPLINARY | MEMBRANES | NANOSCIENCE & NANOTECHNOLOGY | CHEMISTRY, MULTIDISCIPLINARY | DELIVERY | IMPAIRMENT | Neuroprotective Agents - therapeutic use | Protons | Neuropeptides - pharmacokinetics | Peptides - pharmacokinetics | Coumarins - chemistry | Polyethylene Glycols - chemistry | Tissue Distribution | Brain Diseases - drug therapy | Cattle | Amyloid beta-Peptides - metabolism | Serum Albumin, Bovine - chemistry | Polyglactin 910 - chemistry | Nanomedicine | Lactoferrin - metabolism | Peptide Fragments - metabolism | Neuroprotective Agents - chemistry | Peptides - chemistry | Rats | Memory, Short-Term - drug effects | Serum Albumin, Bovine - metabolism | Blood-Brain Barrier - drug effects | Blood-Brain Barrier - metabolism | Neuropeptides - therapeutic use | Lactoferrin - chemistry | Liposomes - chemistry | Peptide Fragments - chemistry | Animals | Liposomes - metabolism | Mice | Amyloid beta-Peptides - chemistry | Peptides - therapeutic use | Neuropeptides - chemistry
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7. Full Text Recognition of microbial glycans by human intelectin-1
by Wesener, Darryl A and Wangkanont, Kittikhun and McBride, Ryan and Song, Xuezheng and Kraft, Matthew B and Hodges, Heather L and Zarling, Lucas C and Splain, Rebecca A and Smith, David F and Cummings, Richard D and Paulson, James C and Forest, Katrina T and Kiessling, Laura L and Univ. of Wisconsin, Madison, WI (United States)
Nature Structural and Molecular Biology, ISSN 1545-9993, 08/2015, Volume 22, Issue 8, pp. 603 - 610
The glycans displayed on mammalian cells can differ markedly from those on microbes. Such differences could, in principle, be 'read' by carbohydrate-binding... 
MANNOSE-BINDING LECTIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | GALACTOFURANOSE | HOST | SIALIC-ACID | LAEVIS OOCYTE LECTIN | UDP-GALACTOPYRANOSE MUTASE | CELL BIOLOGY | BIOPHYSICS | INTESTINAL NEMATODE | CARBOHYDRATE-RECOGNITION | HUMAN LACTOFERRIN | CONFORMATIONAL-ANALYSIS | Surface Plasmon Resonance | Epitopes - metabolism | Models, Chemical | Humans | Lipopolysaccharides - metabolism | Molecular Sequence Data | Crystallography, X-Ray | Cytokines - chemistry | Lectins - metabolism | Streptococcus pneumoniae - chemistry | Streptococcus pneumoniae - metabolism | HEK293 Cells | Polysaccharides - chemistry | Molecular Structure | Lectins - chemistry | Cytokines - genetics | Carbohydrate Sequence | Protein Structure, Tertiary | Amino Acid Sequence | Cytokines - metabolism | Models, Molecular | GPI-Linked Proteins - metabolism | Polysaccharides - metabolism | Sequence Homology, Amino Acid | Animals | GPI-Linked Proteins - chemistry | Protein Binding | Lectins - genetics | Ligands | Epitopes - chemistry | Lipopolysaccharides - chemistry | Mice | Monosaccharides - metabolism | Monosaccharides - chemistry | GPI-Linked Proteins - genetics | Lectins | Physiological aspects | Research | Structure | Antigenic determinants | Cellular biology | Microbiology | Proteases | Carbohydrates | 60 APPLIED LIFE SCIENCES
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8. Full Text Clinical applications of bioactive milk components
by Hill, David R and Newburg, David S
Nutrition Reviews, ISSN 0029-6643, 07/2015, Volume 73, Issue 7, pp. 463 - 476
Milk represents a unique resource for translational medicine: It contains a rich pool of biologically active molecules with demonstrated clinical benefits. The... 
Antimicrobial | Human milk | Translational research | Prebiotics | antimicrobial | PEDIATRIC CROHNS-DISEASE | APOPTOSIS-LIKE MECHANISM | HYPERIMMUNE BOVINE COLOSTRUM | WHEY-PROTEIN RICH | human milk | GROWTH-FACTOR-BETA | NUTRITION & DIETETICS | HUMAN ALPHA-LACTALBUMIN | INFLAMMATORY-BOWEL-DISEASE | BIRTH-WEIGHT INFANTS | HELICOBACTER-PYLORI INFECTION | HYDROLYSATE C-12 PEPTIDE | prebiotics | translational research | Milk - chemistry | Anti-Infective Agents - pharmacology | Humans | Milk, Human - chemistry | Oligosaccharides - pharmacology | Caseins - chemistry | Lactoferrin - pharmacology | Cattle | Anti-Infective Agents - chemistry | Oligosaccharides - chemistry | Antineoplastic Agents - pharmacology | Milk - immunology | Transforming Growth Factor beta - immunology | Anti-Inflammatory Agents - pharmacology | Lactalbumin - chemistry | Antineoplastic Agents - chemistry | Randomized Controlled Trials as Topic | Lactoferrin - chemistry | Animals | Anti-Inflammatory Agents - chemistry | Lactalbumin - pharmacology | Crohn Disease - drug therapy | Cell Line, Tumor | Milk, Human - immunology | Caseins - pharmacology | Health aspects | Milk proteins | Composition | Special
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9. Full Text Formation and characterization of lactoferrin-hyaluronic acid conjugates and their effects on the storage stability of sesamol emulsions
by Liu, Runhua and Liu, Runhua and Zhang, Jinhong and Zhang, Jinhong and Zhao, Caicai and Zhao, Caicai and Duan, Xiang and Duan, Xiang and McClements, David Julian and McClements, David Julian and Liu, Xuebo and Liu, Xuebo and Liu, Fuguo and Liu, Fuguo
Molecules, ISSN 1420-3049, 12/2018, Volume 23, Issue 12, p. 3291
The purpose of this study was to fabricate biopolymer conjugates from lactoferrin (LF) and hyaluronic acid (HA) and then to investigate their potential as... 
Lactoferrin | Stability | Covalent complex | Hyaluronic acid | Sesamol emulsion | IMPROVE | DESIGN | PROTEIN | COVALENT | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMPLEXES | CHITOSAN | DEXTRAN | sesamol emulsion | CHEMISTRY, MULTIDISCIPLINARY | hyaluronic acid | DELIVERY | covalent complex | OIL | POLYSACCHARIDES | lactoferrin | stability | Particle Size | Lactoferrin - chemistry | Emulsions - chemistry | Drug Stability | Electrophoresis, Polyacrylamide Gel | Emulsifying Agents - chemistry | Hyaluronic Acid - chemistry | Spectrometry, Fluorescence | Phenols - chemistry | Benzodioxoles - chemistry | Spectroscopy, Fourier Transform Infrared
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10. Full Text Targeting delivery of etoposide to inhibit the growth of human glioblastoma multiforme using lactoferrin- and folic acid-grafted poly(lactide-co-glycolide) nanoparticles
by Kuo, Yung-Chih and Chen, Yu-Chun
International Journal of Pharmaceutics, ISSN 0378-5173, 02/2015, Volume 479, Issue 1, pp. 138 - 149
[Display omitted] Lactoferrin (Lf) and folic acid (FA) were crosslinked on poly(lactide-co-glycolide) (PLGA) nanoparticles (NPs) for transporting etoposide... 
Etoposide | Lactoferrin | Poly(lactide-co-glycolide) | Glioblastoma multiforme | Folic acid | Blood–brain barrier | Blood-brain barrier | CONJUGATED POLYMER MICELLES | DRUG-DELIVERY | MICROVASCULAR ENDOTHELIAL-CELLS | BIODEGRADABLE NANOPARTICLES | BLOOD-BRAIN-BARRIER | SOLID LIPID NANOPARTICLES | ARTERIAL UPTAKE | IN-VITRO | PHARMACOLOGY & PHARMACY | ORAL DELIVERY | PLGA NANOPARTICLES | Endothelial Cells | Nanoparticles - chemistry | Humans | Glioblastoma | Topoisomerase II Inhibitors - administration & dosage | Brain Neoplasms | Drug Delivery Systems | Antineoplastic Agents, Phytogenic - administration & dosage | Topoisomerase II Inhibitors - chemistry | Microscopy, Electron, Transmission | Microscopy, Electron, Scanning | Lactic Acid - chemistry | Astrocytes | Cell Survival | Cells, Cultured | Folic Acid - chemistry | Nanoparticles - ultrastructure | Receptors, Cell Surface - metabolism | Antineoplastic Agents, Phytogenic - chemistry | Etoposide - administration & dosage | Folate Receptors, GPI-Anchored - metabolism | Blood-Brain Barrier - metabolism | Lactoferrin - chemistry | Polyglycolic Acid - chemistry | Cell Line, Tumor | Etoposide - chemistry | Nanoparticles - administration & dosage | Gliomas | Lactoferrins
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11. Full Text Characterization of the bovine milk proteome in early-lactation Holstein and Jersey breeds of dairy cows
by Tacoma, Rinske and Fields, Julia and Ebenstein, David B and Lam, Ying-Wai and Greenwood, Sabrina L
Journal of Proteomics, ISSN 1874-3919, 01/2016, Volume 130, pp. 200 - 210
Milk is a highly nutritious natural product that provides not only a rich source of amino acids to the consumer but also hundreds of bioactive peptides and... 
Whey | Bioactive proteins | Low abundance proteins | Milk - chemistry | Species Specificity | Computational Biology | Osteopontin - chemistry | Blood Proteins - chemistry | Chromatography, High Pressure Liquid | Proteome - chemistry | Whey Proteins - chemistry | Food Analysis | Animals | Milk Proteins - chemistry | Cattle | Complement C2 - chemistry | Mass Spectrometry | Proteomics | Female | Trypsin - chemistry | Lactoperoxidase - chemistry | UREA NITROGEN | LACTOFERRIN | HUMAN COLOSTRUM | BLOOD-PLASMA | BIOCHEMICAL RESEARCH METHODS | 2-DIMENSIONAL ELECTROPHORESIS | IDENTIFICATION | PEPTIDES | CASEIN | MINOR PROTEINS | MATURE MILK | Proteins | Dairy cattle
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12. Full Text Physicochemical properties of β-carotene emulsions stabilized by chlorogenic acid–lactoferrin–glucose/polydextrose conjugates
by Liu, Fuguo and Wang, Di and Xu, Honggao and Sun, Cuixia and Gao, Yanxiang
Food Chemistry, ISSN 0308-8146, 04/2016, Volume 196, pp. 338 - 346
•Polyphenol–lactoferrin–carbohydrate conjugates were used to stabilize β-carotene emulsions.•The droplet characteristics and stability of β-carotene emulsions... 
Maillard reaction | Polydextrose | Chlorogenic acid–lactoferrin conjugate | Glucose | β-Carotene emulsions | Physicochemical stability | Chlorogenic acidlactoferrin conjugate | b-Carotene emulsions | PROTEIN ISOLATE | RHEOLOGICAL PROPERTIES | FOOD SCIENCE & TECHNOLOGY | WHEY-PROTEIN | DEXTRAN | beta-Carotene emulsions | IMPACT | NUTRITION & DIETETICS | Chlorogenic acid-lactoferrin conjugate | BEET PECTIN | EMULSIFYING PROPERTIES | CHEMISTRY, APPLIED | BOVINE SERUM-ALBUMIN | IN-WATER EMULSIONS | Lactoferrin - chemistry | Emulsions - chemistry | Drug Stability | Emulsifying Agents - chemistry | Maillard Reaction | Chemical Phenomena | Glucose - chemistry | Glucans - chemistry | Chlorogenic Acid - chemistry | beta Carotene - chemistry | Lipolysis
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