Temporin L (TempL) is a 13 residue Host Defense Peptide (HDP) isolated from the skin of frogs. It has a strong affinity for lipopolysaccharides (LPS), which is related to its high activity against Gram-negative bacteria and also to its strong tendency to neutralize the pro-inflammatory response caused by LPS release from inactivated bacteria. A designed analog with the Q3K substitution shows an enhancement in both these activities. In the present paper, Molecular Dynamics (MD) simulations have been used to investigate the origin of these improved properties. To this end, we have studied the behavior of the peptides both in water solution and in the presence of LPS lipid-A bilayers, demonstrating that the main effect through which the Q3K substitution improves the peptide activities is the destabilization of peptide aggregates in water.

Farrotti, A., Conflitti, P., Srivastava, S., Ghosh, J., Palleschi, A., Stella, L., et al. (2017). Molecular Dynamics Simulations of the Host Defense Peptide Temporin L and Its Q3K Derivative: An Atomic Level View from Aggregation in Water to Bilayer Perturbation. MOLECULES, 22(7), 1235 [10.3390/molecules22071235].

Molecular Dynamics Simulations of the Host Defense Peptide Temporin L and Its Q3K Derivative: An Atomic Level View from Aggregation in Water to Bilayer Perturbation

FARROTTI, ANDREA;CONFLITTI, PAOLO;PALLESCHI, ANTONIO;STELLA, LORENZO;BOCCHINFUSO, GIANFRANCO
2017-07-22

Abstract

Temporin L (TempL) is a 13 residue Host Defense Peptide (HDP) isolated from the skin of frogs. It has a strong affinity for lipopolysaccharides (LPS), which is related to its high activity against Gram-negative bacteria and also to its strong tendency to neutralize the pro-inflammatory response caused by LPS release from inactivated bacteria. A designed analog with the Q3K substitution shows an enhancement in both these activities. In the present paper, Molecular Dynamics (MD) simulations have been used to investigate the origin of these improved properties. To this end, we have studied the behavior of the peptides both in water solution and in the presence of LPS lipid-A bilayers, demonstrating that the main effect through which the Q3K substitution improves the peptide activities is the destabilization of peptide aggregates in water.
22-lug-2017
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore CHIM/02 - CHIMICA FISICA
English
LPS; Potential of Mean Force (PMF); Temporin; molecular dynamics simulations; peptide aggregation
Farrotti, A., Conflitti, P., Srivastava, S., Ghosh, J., Palleschi, A., Stella, L., et al. (2017). Molecular Dynamics Simulations of the Host Defense Peptide Temporin L and Its Q3K Derivative: An Atomic Level View from Aggregation in Water to Bilayer Perturbation. MOLECULES, 22(7), 1235 [10.3390/molecules22071235].
Farrotti, A; Conflitti, P; Srivastava, S; Ghosh, J; Palleschi, A; Stella, L; Bocchinfuso, G
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/187634
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