Membrane-Peptide Interactions From Basics to Current Applications

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 pote...

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Bibliographic Details
Other Authors: Santos, Nuno C. (Editor), Gonçalves, Sónia (Editor)
Format: Electronic Book Chapter
Language:English
Published: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute 2020
Subjects:
NMR
Online Access:DOAB: download the publication
DOAB: description of the publication
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520 |a 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. 
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653 |a tachyplesin 
653 |a host defense peptide 
653 |a anticancer 
653 |a antimicrobial 
653 |a antibiofilm 
653 |a peptide-membrane interaction 
653 |a structure-activity 
653 |a model membranes 
653 |a nuclear magnetic resonance solution structure 
653 |a accelerated molecular dynamics 
653 |a alamethicin 
653 |a membrane 
653 |a peptaibol 
653 |a cell-penetrating peptide 
653 |a peptide-lipid interaction 
653 |a lipid model systems 
653 |a molecular dynamics 
653 |a NMR 
653 |a membrane biophysics 
653 |a antimicrobial peptides 
653 |a non-lytic peptides 
653 |a bacterial membranes 
653 |a calcium hydroxide 
653 |a chemokine 
653 |a human beta defensin-3-C15 
653 |a human dental pulp cell 
653 |a Streptococcus gordonii lipoprotein 
653 |a luffa sponge 
653 |a phosphopeptide 
653 |a mass spectrometry 
653 |a Matrix-assisted laser desorption ionization 
653 |a solid-phase extraction 
653 |a surface plasmon resonance 
653 |a melittin 
653 |a liposomes 
653 |a peptide-lipid interactions 
653 |a anti-microbial peptides 
653 |a pore-forming peptides 
653 |a ESKAPE pathogens 
653 |a Staphylococcus aureus 
653 |a KR12 
653 |a LL-37 
653 |a lipopeptide 
653 |a critical aggregation concentration 
653 |a CD spectroscopy 
653 |a biofilm 
653 |a cytotoxicity 
653 |a organisms 
653 |a sequence analysis 
653 |a machine learning 
653 |a feature selection 
653 |a sesame protein 
653 |a ACE inhibitory peptides 
653 |a simulated gastrointestinal digestion 
653 |a amino acid sequence 
653 |a molecular docking 
653 |a chionodracines 
653 |a circular dichroism 
653 |a membrane affinity 
653 |a cell-penetrating peptides 
653 |a circular dichroism spectroscopy 
653 |a atomic force microscopy 
653 |a mycolic acid 
653 |a Langmuir monolayer 
653 |a drug-peptide conjugates 
653 |a metastasis model of B16F10 melanoma 
653 |a Pisum sativum defensin 1 (Psd1) 
653 |a anti-metastatic activity 
653 |a glucosylceramide (GlcCer) 
653 |a cyclin F 
653 |a anti-inflammatory peptide 
653 |a cell permeable peptide 
653 |a heparin-binding peptide 
653 |a collagen-induced arthritis 
653 |a inducible nitric oxide 
653 |a interferon gamma 
653 |a interleukin-6 
653 |a Enbrel 
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