Design of a minimized cyclic tetrapeptide that neutralizes bacterial endotoxins

Journal of Peptide Science : an Official Publication of the European Peptide Society
Puig MoraFernando Albericio

Abstract

Septic shock is a leading cause of mortality in intensive care patients, and no specific drugs are as yet available for its treatment. Therefore, new leads are required in order to increase the number of active molecules that may develop into efficacious and safe LPS-neutralizing molecules during pre-clinical stages. We used peptides, derived from the binding regions of known LPS-binding proteins, as scaffolds to introduce modifications at the amino acid level. Structure-activity relationship studies have shown that these modifications generate highly active peptides. Thus, from a bioactive peptide with an initial 16 amino acid residues, a tetrapeptide sequence was determined. After inserting this sequence in a Cys cyclic peptide, it showed the same biological activity as the parent peptide. This sequence could provide the basis for the design of small molecules with LPS-binding properties.

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Citations

Nov 9, 2011·The Journal of Biological Chemistry·Yadira Palacios-RodríguezEnrique Pérez-Payá
Oct 4, 2008·ChemMedChem·Carlos Mas-MorunoFernando Albericio
Jul 29, 2010·Pancreas·Xiping ZhangXinge Jiang
Dec 21, 2016·Bioconjugate Chemistry·Wenxu ZhangCarsten Schmuck
Aug 26, 2011·Bioconjugate Chemistry·Angela TorresMiriam Royo
Mar 29, 2014·ACS Applied Materials & Interfaces·Carlos Mas-MorunoF Javier Gil

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