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Effect of physicochemical properties of peptides from soy protein on their antimicrobial activity
- Source :
- Peptides. 94
- Publication Year :
- 2017
-
Abstract
- Antimicrobial peptides (AMPs) kill microbial cells through insertion and damage/permeabilization of the cytoplasmic cell membranes and has applications in food safety and antibiotic replacement. Soy protein is an attractive, abundant natural source for commercial production of AMPs. In this research, explicit solvent molecular dynamics (MD) simulation was employed to investigate the effects of (i) number of total and net charges, (ii) hydrophobicity (iii) hydrophobic moment and (iv) helicity of peptides from soy protein on their ability to bind to lipid bilayer and their transmembrane aggregates to form pores. Interaction of possible AMP segments from soy protein with 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine/1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol (POPC/POPG) bilayers, a mimic of bacterial cell membrane, was investigated. Pore formation was insensitive to helicity and occurred for hydrophobicity threshold in the range of -0.3-0kcal/mol, hydrophobic moment threshold of 0.3kcal/mol, net charge threshold of 2. Though low hydrophobicity and high number of charges help in the formation of water channel for transmembrane aggregates, insertion of peptides with these properties requires overcome of energy barrier, as shown by potential of mean force calculations, thereby resulting in low antimicrobial activity. Experimental evaluation of antimicrobial activity of these peptides against Gram positive L. monocytogenes and Gram negative E. coli as obtained by spot-on-lawn assay was consistent with simulation results. These results should help in the development of guidelines for selection of peptides with antimicrobial activity based on their physicochemical properties.
- Subjects :
- 0301 basic medicine
Physiology
Antimicrobial peptides
Molecular Dynamics Simulation
01 natural sciences
Biochemistry
Bacterial cell structure
03 medical and health sciences
Cellular and Molecular Neuroscience
chemistry.chemical_compound
Endocrinology
Anti-Infective Agents
0103 physical sciences
Escherichia coli
Lipid bilayer
POPC
Soy protein
010304 chemical physics
Cell Membrane
Antimicrobial
Listeria monocytogenes
Transmembrane protein
030104 developmental biology
Membrane
chemistry
Biophysics
Soybean Proteins
Soybeans
Hydrophobic and Hydrophilic Interactions
Antimicrobial Cationic Peptides
Subjects
Details
- ISSN :
- 18735169
- Volume :
- 94
- Database :
- OpenAIRE
- Journal :
- Peptides
- Accession number :
- edsair.doi.dedup.....f7933fa0c69b7803931185dee38dffea