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Controlling morphology of peptide‐based soft structures by covalent modifications
Author(s) -
Gour Nidhi,
Barman Apurba K.,
Verma Sandeep
Publication year - 2012
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2411
Subject(s) - dipeptide , concanavalin a , peptide , residue (chemistry) , mannose , covalent bond , chemistry , lectin , stereochemistry , biophysics , biochemistry , organic chemistry , biology , in vitro
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. Copyright © 2012 European Peptide Society and John Wiley & Sons, Ltd.