期刊
MOLECULES
卷 22, 期 7, 页码 -出版社
MDPI
DOI: 10.3390/molecules22071235
关键词
LPS; Temporin; molecular dynamics simulations; Potential of Mean Force (PMF); peptide aggregation
资金
- Italian Ministry of Education, University and Research [PRIN 20157WW5EH_007]
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.
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