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PHOSPHORYLATION --- SOIL MOISTURE CONTENT --- PHOTOPERIODISM --- PHOTOSYNTHESIS --- ORGANOGENESIS --- TISSUE CULTURE --- TRANSPORT PROPERTIES --- TROPISMS --- FRUIT GROWTH --- ABSCISSION --- DORMANCY --- GERMINATION --- SENESCENCE --- FLOWERING --- MODEL MEMBRANES --- INHIBITORS --- CELL DIVISION --- PLANT MEMBRANES --- NUCLEIC ACIDS --- ENZYMES --- PLANT HORMONES --- BIOLOGICAL ACTION --- PLANT METABOLISM --- GROWTH REGULATORS --- PLANT GROWTH --- ENZYMES --- PHOSPHORYLATION --- SOIL MOISTURE CONTENT --- PHOTOPERIODISM --- PHOTOSYNTHESIS --- ORGANOGENESIS --- TISSUE CULTURE --- TRANSPORT PROPERTIES --- TROPISMS --- FRUIT GROWTH --- ABSCISSION --- DORMANCY --- GERMINATION --- SENESCENCE --- FLOWERING --- MODEL MEMBRANES --- INHIBITORS --- CELL DIVISION --- PLANT MEMBRANES --- NUCLEIC ACIDS --- ENZYMES --- PLANT HORMONES --- BIOLOGICAL ACTION --- PLANT METABOLISM --- GROWTH REGULATORS --- PLANT GROWTH --- ENZYMES

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Cell membranes are complex structures able to contain the main elements of the cell and to protect them from the external surroundings, becoming the most fundamental interface in Biology. The main subject of this book is the study of the structure and characteristics of lipid membranes in a wide variety of environments, ranging from simple phospholipid membranes to complex systems including proteins, peptides, or oncogenes as well as the analysis of the interactions of the membrane components with small molecules and drugs. The scope of this book is to provide recent developments on membrane structure, composition and function by means of theoretical and experimental techniques, some of them combining computer simulations with available data obtained at the laboratory.This Special Issue aims to report brand new key contributions to the field and also to give an overview about the connection between experiments and computer simulations, addressing fundamental aspects and applied research in biological membranes, with particular attention paid to the applications of computer modeling and simulation to medicine.

peptide --- MD --- GUV --- LUV --- azo-amino acid --- KRas-4B --- mutation --- post-translational modification --- HVR --- anionic plasma membrane --- signaling --- cholesterol --- model membranes --- molecular dynamics --- calorimetry --- Schiff base --- imine --- benzimidazole --- 2,4-dihydroxybenzaldehyde --- neutron reflectometry --- X-ray reflectometry --- small-angle neutron scattering --- small-angle X-ray scattering --- molecular dynamics simulations --- scattering length density profile --- phospholipid membrane --- phosphatidylserine --- cancer cells --- MD simulation --- membrane permeability --- withaferin A --- withanone --- CAPE --- artepillin C --- membrane elasticity --- red blood cells --- hemodynamics --- hemorheology --- microfluidics --- benzothiadiazine derivatives --- drug design --- KCNE3 --- structural dynamics --- lipid bilayers --- molecular dynamics simulation --- membrane mimetic --- n/a

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This book summarizes the importance of peptide–membrane interactions, mostly aiming at developing new therapeutic approaches. The experimental and computational methodologies used to investigate such interactions reveal the evolution of existing biophysical methodologies, shedding some light on potential applications of peptides, as well as on the improvement of their design. Understanding the determinants for peptide–membrane interactions may also improve the knowledge of membrane functions such as the membrane transport, fusion, and signaling processes, contributing to the development of new agents for highly relevant applications ranging from disease treatment to food technology.

Research & information: general --- Biology, life sciences --- tachyplesin --- host defense peptide --- anticancer --- antimicrobial --- antibiofilm --- peptide-membrane interaction --- structure-activity --- model membranes --- nuclear magnetic resonance solution structure --- accelerated molecular dynamics --- alamethicin --- membrane --- peptaibol --- cell-penetrating peptide --- peptide–lipid interaction --- lipid model systems --- molecular dynamics --- NMR --- membrane biophysics --- antimicrobial peptides --- non-lytic peptides --- bacterial membranes --- calcium hydroxide --- chemokine --- human beta defensin-3-C15 --- human dental pulp cell --- Streptococcus gordonii lipoprotein --- luffa sponge --- phosphopeptide --- mass spectrometry --- Matrix-assisted laser desorption ionization --- solid-phase extraction --- surface plasmon resonance --- melittin --- liposomes --- peptide–lipid interactions --- anti-microbial peptides --- pore-forming peptides --- ESKAPE pathogens --- Staphylococcus aureus --- KR12 --- LL-37 --- lipopeptide --- critical aggregation concentration --- CD spectroscopy --- biofilm --- cytotoxicity --- organisms --- sequence analysis --- machine learning --- feature selection --- sesame protein --- ACE inhibitory peptides --- simulated gastrointestinal digestion --- amino acid sequence --- molecular docking --- chionodracines --- circular dichroism --- membrane affinity --- cell-penetrating peptides --- circular dichroism spectroscopy --- atomic force microscopy --- mycolic acid --- Langmuir monolayer --- drug–peptide conjugates --- metastasis model of B16F10 melanoma --- Pisum sativum defensin 1 (Psd1) --- anti-metastatic activity --- glucosylceramide (GlcCer) --- cyclin F --- anti-inflammatory peptide --- cell permeable peptide --- heparin-binding peptide --- collagen-induced arthritis --- inducible nitric oxide --- interferon gamma --- interleukin-6 --- Enbrel --- tachyplesin --- host defense peptide --- anticancer --- antimicrobial --- antibiofilm --- peptide-membrane interaction --- structure-activity --- model membranes --- nuclear magnetic resonance solution structure --- accelerated molecular dynamics --- alamethicin --- membrane --- peptaibol --- cell-penetrating peptide --- peptide–lipid interaction --- lipid model systems --- molecular dynamics --- NMR --- membrane biophysics --- antimicrobial peptides --- non-lytic peptides --- bacterial membranes --- calcium hydroxide --- chemokine --- human beta defensin-3-C15 --- human dental pulp cell --- Streptococcus gordonii lipoprotein --- luffa sponge --- phosphopeptide --- mass spectrometry --- Matrix-assisted laser desorption ionization --- solid-phase extraction --- surface plasmon resonance --- melittin --- liposomes --- peptide–lipid interactions --- anti-microbial peptides --- pore-forming peptides --- ESKAPE pathogens --- Staphylococcus aureus --- KR12 --- LL-37 --- lipopeptide --- critical aggregation concentration --- CD spectroscopy --- biofilm --- cytotoxicity --- organisms --- sequence analysis --- machine learning --- feature selection --- sesame protein --- ACE inhibitory peptides --- simulated gastrointestinal digestion --- amino acid sequence --- molecular docking --- chionodracines --- circular dichroism --- membrane affinity --- cell-penetrating peptides --- circular dichroism spectroscopy --- atomic force microscopy --- mycolic acid --- Langmuir monolayer --- drug–peptide conjugates --- metastasis model of B16F10 melanoma --- Pisum sativum defensin 1 (Psd1) --- anti-metastatic activity --- glucosylceramide (GlcCer) --- cyclin F --- anti-inflammatory peptide --- cell permeable peptide --- heparin-binding peptide --- collagen-induced arthritis --- inducible nitric oxide --- interferon gamma --- interleukin-6 --- Enbrel