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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

Choose an application

• Reference Manager
• EndNote
• RefWorks (Direct export to RefWorks)

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.

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