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dc.contributor.authorMora, Puig
dc.contributor.authorMas Moruno, Carlos
dc.contributor.authorTamborero, Silvia
dc.contributor.authorCruz, Luis Javier
dc.contributor.authorPérez-Payá, Enrique
dc.contributor.authorAlbericio, Fernando
dc.contributor.otherUniversitat Politècnica de Catalunya. Departament de Ciència dels Materials i Enginyeria Metal·lúrgica
dc.identifier.citationMora, P. [et al.]. Design of a minimized cyclic tetrapeptide that neutralizes bacterial endotoxins. "Journal of peptide science", 2006, vol. 12, p. 491-496.
dc.description.abstractSeptic 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 ar e required in order to increase the numbe r of active molecules that may develop into efficacious and safe LPS-neutralizing mol ecules during pre-clinical stages. We used pe ptides, derived from the binding regions of known LPS-binding proteins, as scaffolds to introduce modifications at the amino aci d level. Structure–activity relationship studies have shown that these modifications generate highly acti ve peptides. Thus, from a bioactive peptide with an initial 16 amino acid residues, a tetrapeptide sequence was determined. A fter inserting this sequence in a Cys cyclic peptide, it showed the same biological activity as the parent peptide. This sequenc e could provide the basis for the design of small molecules with LPS-binding properties
dc.format.extent6 p.
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Spain
dc.subjectÀrees temàtiques de la UPC::Enginyeria química
dc.titleDesign of a minimized cyclic tetrapeptide that neutralizes bacterial endotoxins
dc.description.peerreviewedPeer Reviewed
dc.rights.accessRestricted access - publisher's policy
dc.description.versionPostprint (published version)
local.citation.authorMora, P.; Mas-Moruno, C.; Tamborero, S.; Cruz, L.J.; Pérez-Payá, E.; Albericio, F.
local.citation.publicationNameJournal of peptide science

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