title: Controlling morphology of peptide-based soft structures by covalent modifications.
abstract: Control of gross morphology of soft matter remains an area of continued interest. Towards this goal, this paper describes conjugation of mannose residues and introduction of thiol functionalities to diphenylalanine (FF) dipeptide, a fibrillating motif from amyloid-β peptide, as covalent modifiers of its solution-phase self-assembly process. It was found that covalent attachment of a single mannose residue to FF leads to the retention of tubular structures, whereas the conjugation of two mannose units, linked through a Lys residue, resulted in a dramatic change from tubular morphology to spherical structures. However, a similar switch to spherical objects could be achieved by introducing a thiol residue in the mono-mannosylated FF dipeptide. Interestingly, these glycopeptides also exhibited interaction with concanavalin A, thereby providing an indirect evidence for the availability of mannose units for the process of lectin-carbohydrate interaction in the self-organized state.
authors.affiliation: Department of Chemistry, Indian Institute of Technology Kanpur, Kanpur-208 016 UP, India.
authors.forename: Nidhi
authors.initials: N
authors.lastname: Gour
authors.forename: Apurba K
authors.initials: AK
authors.lastname: Barman
authors.forename: Sandeep
authors.initials: S
authors.lastname: Verma
mesh_terms: D004151:Dipeptides / Q000138:chemical synthesis / Q000737:chemistry*; D008358:Mannose / Q000737:chemistry; D008968:Molecular Conformation; D010316:Particle Size; D010649:Phenylalanine / Q000031:analogs & derivatives / Q000737:chemistry; D012996:Solutions
chemical_list: D004151:Dipeptides; D012996:Solutions; C026650:phenylalanylphenylalanine; D010649:Phenylalanine; D008358:Mannose