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Biophysical Journal, ISSN 0006-3495, 2010, Volume 98, Issue 2, pp. 248 - 257
A 21-residue peptide segment, LL7-27 (RKSKEKIGKEFKRIVQRIKDF), corresponding to residues 7–27 of the only human cathelicidin antimicrobial peptide, LL37, is... 
HOST-DEFENSE PEPTIDES | LL-37 | BIOPHYSICS | MECHANISM | LIPID-BILAYER DISRUPTION | MAGAININ | ORIENTATION | RESOLUTION | STATE NMR-SPECTROSCOPY | PROTEINS | BIOMEMBRANES | Gram-Positive Bacteria - drug effects | Gram-Positive Bacteria - chemistry | Humans | Peptide Fragments - pharmacology | Unilamellar Liposomes - chemistry | Phase Transition | Cell Membrane - chemistry | Cholesterol - chemistry | Anti-Bacterial Agents - chemistry | Nuclear Magnetic Resonance, Biomolecular | Cell Membrane - metabolism | Cathelicidins - pharmacology | Circular Dichroism | Cell Membrane - drug effects | Phosphorus Isotopes | Peptide Fragments - metabolism | Protein Structure, Secondary | Phosphatidylcholines - chemistry | Escherichia coli - chemistry | Cathelicidins - chemistry | Gram-Negative Bacteria - drug effects | Liposomes - chemistry | Peptide Fragments - chemistry | Phosphatidylglycerols - chemistry | Gram-Negative Bacteria - chemistry | Cathelicidins - metabolism | Calorimetry, Differential Scanning | Anti-Bacterial Agents - pharmacology | Lipid Bilayers - chemistry | Dimyristoylphosphatidylcholine - chemistry | Drug resistance in microorganisms | Peptides | Surface active agents | Analysis | Escherichia coli | Fluorescence | Sport-utility vehicles | Membranes | Microorganisms | Vesicles | Erythrocytes | Dichroism | Bacteria | Lipids | Nuclear magnetic resonance | MLV, multilamellar vesicle | DSC, differential scanning calorimetry | ANS, anilinonaphthalene-8-sulfonic acid | MIC, minimum inhibitory concentration | AMP, antimicrobial peptide | SUV, small unilamellar vesicle | POPG, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylglycerol | PBS, phosphate-buffered saline | NMR, nuclear magnetic resonance | DMPG, 1,2-dimyristoyl-glycero-3-phosphatidylglycerol | Membrane | POPC, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylcholine | DMPC, 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine | CP, cross-polarization | PISEMA, polarization inversion spin exchange at the magic angle | CD, circular dichroism
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2015, Volume 290, Issue 32, pp. 19933 - 19941
Journal Article
BBA - Biomembranes, ISSN 0005-2736, 08/2017, Volume 1859, Issue 8, pp. 1350 - 1361
Antimicrobial peptides are essential components of the innate immune system of multicellular organisms. Although cationic and hydrophobic amino acids are known... 
Membrane permeation | Membrane composition | Molecular probe | Host defense peptides | Native sequence | Charge swap | ANTI-BIOFILM | BIOCHEMISTRY & MOLECULAR BIOLOGY | SMALLEST ANTIMICROBIAL PEPTIDE | MEMBRANES | FUNCTIONAL ROLES | SIDE-CHAINS | FRAGMENTS | CIRCULAR-DICHROISM | BIOPHYSICS | AMINO-ACIDS | HUMAN CATHELICIDIN LL-37 | BINDING | Phosphatidylethanolamines - isolation & purification | Klebsiella pneumoniae - drug effects | Cardiolipins - isolation & purification | Species Specificity | Escherichia coli - drug effects | Humans | Pseudomonas aeruginosa - growth & development | Structure-Activity Relationship | Cell Membrane - chemistry | Microbial Sensitivity Tests | Escherichia coli - growth & development | Cell Membrane - drug effects | Amino Acid Sequence | Phosphatidylglycerols - isolation & purification | Antimicrobial Cationic Peptides - pharmacology | Models, Molecular | Pseudomonas aeruginosa - drug effects | Escherichia coli - chemistry | Cardiolipins - chemistry | Arginine - chemistry | Peptides - pharmacology | Staphylococcus aureus - chemistry | Phosphatidylglycerols - chemistry | Pseudomonas aeruginosa - chemistry | Cell Membrane Permeability - drug effects | Klebsiella pneumoniae - growth & development | Anti-Bacterial Agents - pharmacology | Lysine - chemistry | Staphylococcus aureus - drug effects | Staphylococcus aureus - growth & development | Phosphatidylethanolamines - chemistry | Klebsiella pneumoniae - chemistry | Hydrogen-Ion Concentration | Membrane lipids | Swaps (Finance) | Biological products | Peptides | Surface active agents | Arginine | Lysine | Escherichia coli | Cardiolipin | Cells | Microbiology | Bacteria | Index Medicus
Journal Article
Biochemistry, ISSN 0006-2960, 10/2014, Volume 53, Issue 41, pp. 6426 - 6429
A cathelin-related antimicrobial peptide (CRAMP) of 37 amino acid residues is thought to regulate innate immunity and provide a host defense mechanism in... 
MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | INSIGHTS | Hemolysis - drug effects | Cytoskeletal Proteins - antagonists & inhibitors | Hydrolysis - drug effects | Cytoskeletal Proteins - genetics | Escherichia coli - drug effects | Humans | Bacterial Proteins - chemistry | Peptide Fragments - pharmacology | Guanosine Triphosphate - metabolism | GTP Phosphohydrolases - antagonists & inhibitors | Antimicrobial Cationic Peptides - metabolism | GTP Phosphohydrolases - chemistry | Bacillus subtilis - growth & development | Anti-Bacterial Agents - chemistry | Enzyme Inhibitors - chemistry | Escherichia coli - metabolism | Cytoskeletal Proteins - metabolism | Escherichia coli - growth & development | Binding Sites | Cathelicidins - pharmacology | Mutant Proteins - antagonists & inhibitors | Cytokinesis - drug effects | Membrane Potentials - drug effects | Bacterial Proteins - antagonists & inhibitors | Microscopy, Electron, Transmission | Peptide Fragments - metabolism | Enzyme Inhibitors - metabolism | Antimicrobial Cationic Peptides - chemistry | Antimicrobial Cationic Peptides - pharmacology | Bacterial Proteins - genetics | Enzyme Inhibitors - pharmacology | Models, Molecular | Anti-Bacterial Agents - metabolism | Mutant Proteins - metabolism | Cytoskeletal Proteins - chemistry | Cathelicidins - chemistry | Peptide Fragments - chemistry | Animals | GTP Phosphohydrolases - metabolism | Cathelicidins - metabolism | Mutant Proteins - chemistry | Bacterial Proteins - metabolism | Protein Conformation | Anti-Bacterial Agents - pharmacology | Mice | Molecular Docking Simulation | Bacillus subtilis - metabolism | Bacillus subtilis - drug effects
Journal Article
Natural Product Reports, ISSN 0265-0568, 2009, Volume 26, Issue 12, pp. 1572 - 1584
Journal Article
Amino Acids, ISSN 0939-4451, 4/2018, Volume 50, Issue 3, pp. 453 - 468
Facing rising global antibiotics resistance, physical membrane-damaging antimicrobial peptides (AMPs) represent promising antimicrobial agents. Various... 
Life Sciences | Biochemistry, general | Hemolysis | Analytical Chemistry | Life Sciences, general | Biochemical Engineering | Proteomics | Neurobiology | Cell selectivity | Interspecific hybrid peptides | Membrane | Bactericidal mechanism | HELICAL ANTIMICROBIAL PEPTIDES | DESIGN | LL-37 | BETA-HAIRPIN PEPTIDES | BIOCHEMISTRY & MOLECULAR BIOLOGY | INDOLICIDIN | MODEL | CECROPIN | IN-VITRO | GRAM-NEGATIVE BACTERIA | MOLECULAR-BASIS | Humans | Microbial Sensitivity Tests | Peptides - chemical synthesis | Nematoda - chemistry | Swine | Anti-Bacterial Agents - chemistry | Drug Design | Cathelicidins - chemical synthesis | Cathelicidins - pharmacology | Circular Dichroism | Amino Acid Sequence | Antimicrobial Cationic Peptides - chemical synthesis | Peptides - chemistry | Antimicrobial Cationic Peptides - chemistry | Antimicrobial Cationic Peptides - pharmacology | Rats | Cathelicidins - chemistry | Erythrocytes - drug effects | Peptides - pharmacology | Anti-Bacterial Agents - chemical synthesis | Gram-Negative Bacteria - drug effects | Animals | Cell Membrane Permeability - drug effects | Gram-Negative Bacteria - pathogenicity | Anti-Bacterial Agents - pharmacology | Drug resistance in microorganisms | Bacteria | Peptides | Nematoda | Binding | Flow cytometry | Antimicrobial activity | Indolicidin | Motility | Fluorescence | Antimicrobial agents | Interspecific | Selectivity | Drug resistance | Antiinfectives and antibacterials | Lipopolysaccharides | Cytometry | Antibiotics | Antimicrobial peptides | Cecropin | Swimming | Gram-negative bacteria | Damage | Conformation
Journal Article
Journal Article
Journal of Controlled Release, ISSN 0168-3659, 08/2016, Volume 235, pp. 112 - 124
Tuberculosis (TB), a disease caused by the human pathogen , recently joined HIV/AIDS on the top rank of deadliest infectious diseases. Low patient compliance... 
Cathelicidin | Infectious diseases | Macrophages | Mycobacteria | Antimicrobial peptide | DRUG-DELIVERY | MYCOBACTERIUM-AVIUM INFECTION | FUTURE-PROSPECTS | CHEMISTRY, MULTIDISCIPLINARY | CAP18/LL-37-DERIVED ANTIMICROBIAL PEPTIDES | NANOPARTICLES | MULTIDRUG-RESISTANT TUBERCULOSIS | IN-VIVO | PHARMACOLOGY & PHARMACY | MOUSE MACROPHAGES | BCG VACCINATION | CATHELICIDIN LL-37 | Hyaluronic Acid - therapeutic use | Tuberculosis, Pulmonary - microbiology | Antitubercular Agents - chemistry | Drug Carriers - therapeutic use | Drug Carriers - administration & dosage | Tuberculosis, Pulmonary - drug therapy | Antimicrobial Cationic Peptides - administration & dosage | Mycobacterium avium - drug effects | Mycobacterium tuberculosis - drug effects | Drug Carriers - chemistry | Tumor Necrosis Factor-alpha - immunology | Gels - chemistry | Macrophages - immunology | Macrophages - microbiology | Nanostructures - therapeutic use | Antitubercular Agents - therapeutic use | Cell Survival - drug effects | Hyaluronic Acid - administration & dosage | Antimicrobial Cationic Peptides - chemistry | Gels - administration & dosage | Mice, Inbred C57BL | Cells, Cultured | Hyaluronic Acid - chemistry | Antimicrobial Cationic Peptides - therapeutic use | Animals | Nanostructures - administration & dosage | Interleukin-6 - immunology | Antitubercular Agents - administration & dosage | Nanostructures - chemistry | Macrophages - drug effects | Gels - therapeutic use | Mycobacterium avium - growth & development | Mycobacterium tuberculosis - growth & development | Rankings | Tuberculosis | Peptides | Drug therapy | Hyaluronic acid | Patient compliance
Journal Article