title: Structure and hydrogel formation studies on homologs of a lactoglobulin-derived peptide.
abstract: In order to study the impact of the amino acid sequence on the morphology of peptide-based nanostructures and their hydrogel formation, we designed a series of analogs of a milk-derived octapeptide (OP), mainly using strategic amino acid substitutions. Electronic transmission microscopy (TEM) and circular dichroism (CD) spectropolarimetry were used to analyze the nanostructures formed, and to characterize some structural features of the modified peptides. Further, the potential to form hydrogels was investigated for all of the analogous peptides. We learned that those able to undergo secondary structure transition to β-sheet conformation form strong gels. The results reported highlight some key structural properties that explain the self-assembly propensity of Peptide OP.
authors.affiliation: PROTEO, Quebec Research Network on Protein Structure, Function and Engineering, and Département de chimie, Université Laval, Quebec City, QC, Canada, G1V 0A6.
authors.forename: Marie-Michèle
authors.initials: MM
authors.lastname: Guy
authors.forename: Normand
authors.initials: N
authors.lastname: Voyer
mesh_terms: D000595:Amino Acid Sequence; D020136:Hydrogel, Polyethylene Glycol Dimethacrylate / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D007782:Lactoglobulins / Q000737:chemistry*; D049329:Nanostructures / Q000737:chemistry / Q000648:ultrastructure; D009842:Oligopeptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D055672:Static Electricity
chemical_list: D007782:Lactoglobulins; D009842:Oligopeptides; D020136:Hydrogel, Polyethylene Glycol Dimethacrylate