Aggregation of Temporin L and anti - endotoxin property 1 Introduction of a lysine residue Promotes
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منابع مشابه
Introduction of a lysine residue promotes aggregation of temporin L in lipopolysaccharides and augmentation of its antiendotoxin property.
Temporin L (TempL) is a 13-residue frog antimicrobial peptide that shows moderate bactericidal activity and antiendotoxin properties in macrophages. We envisioned that, due to its very hydrophobic nature, the peptide might fail to show its desired biological properties. It was predicted by employing the available algorithms that the replacement of a glutamine by lysine at position 3 could appre...
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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...
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For a frame $L$, consider the $f$-ring $ mathcal{F}_{mathcal P}L=Frm(mathcal{P}(mathbb R), L)$. In this paper, first we show that each minimal ideal of $ mathcal{F}_{mathcal P}L$ is a principal ideal generated by $f_a$, where $a$ is an atom of $L$. Then we show that if $L$ is an $mathcal{F}_{mathcal P}$-completely regular frame, then the socle of $ mathcal{F}_{mathcal P}L$ consists of those $f$...
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