Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/5366
Title: Molecular basis of branched peptides resistance to enzyme proteolysis.
Authors: Falciani, Chiara
Lozzi, Luisa
Pini, Alessandro
Corti, F
Fabbrini, M
Bernini, Andrea 
Lelli, Barbara
Niccolai, Neri 
Bracci, Luisa
Issue Date: 2007
Project: None 
Journal: CHEMICAL BIOLOGY & DRUG DESIGN
Abstract: 
We found that synthetic peptides in the form of dendrimers become resistant to proteolysis. To determine the molecular basis of this resistance, different bioactive peptides were synthesized in monomeric, two-branched and tetra-branched form and incubated with human plasma and serum. Proteolytic resistance of branched multimeric sequences was compared to that of the same peptides synthesized as multimeric linear molecules. Unmodified peptides and cleaved sequences were detected by high pressure liquid chromatography and mass spectrometry. An increase in peptide copies did not increase peptide resistance in linear multimeric sequences, whereas multimericity progressively enhanced proteolytic stability of branched multimeric peptides. A structure-based hypothesis of branched peptide resistance to proteolysis by metallopeptidases is presented.
Description: 
37845
URI: http://hdl.handle.net/20.500.12779/5366
ISSN: 1747-0277
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