title: Denatured bactericidal proteins: active per se, or reservoirs of active peptides?
abstract: According to the structure-to-function paradigm proteins fold into a 3D structure for exerting their functions. Intrinsically destructured proteins with important biological functions have been identified and studied, but they assume a structure when interacting in the cell with their partners. There are instead bactericidal proteins, endowed also with other diverse activities (glycoside hydrolases, RNases, a defensin), which are lost when the proteins are denatured or inactivated, whereas the bactericidal activity is surprisingly conserved. The hypothesis is advanced that these proteins are not bactericidal per se, but because they store in their amino acid sequences peptide segments that display bactericidal activity when cut out as free peptides from the proteins. These bactericidal proteins would thus be merely containers of bactericidal peptides.
authors.affiliation: Department of Structural and Functional Biology, University of Naples, Federico II, Naples, Italy. dalessio@unina.it
authors.forename: Giuseppe
authors.initials: G
authors.lastname: D'Alessio
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000276:immunology; D001770:Blood Bactericidal Activity / Q000276:immunology; D006801:Humans; D010446:Peptide Fragments / Q000276:immunology; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry* / Q000276:immunology*
chemical_list: D023181:Antimicrobial Cationic Peptides; D010446:Peptide Fragments; D011506:Proteins