2012
DOI: 10.1002/psc.2411
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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 t… Show more

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Cited by 28 publications
(26 citation statements)
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“…Previously, a number of strategies including pH mediated control 21, 22 , solvent mediated control 23 , covalent modifications 24 , vapour deposition 25, 26 , temperature 27 , surface 28, 29 , relative humidity 30 , symmetry 31 and magnetite coating on the surface of nanotubes 32 have been employed to regulate the architecture of diphenylalanine self-assemblies. But studies with fairly high magnetic fields have not yielded the level of response as expected, though a response was forced, at a magnetic field range of 12 T or more 33 .…”
Section: Introductionmentioning
confidence: 99%
“…Previously, a number of strategies including pH mediated control 21, 22 , solvent mediated control 23 , covalent modifications 24 , vapour deposition 25, 26 , temperature 27 , surface 28, 29 , relative humidity 30 , symmetry 31 and magnetite coating on the surface of nanotubes 32 have been employed to regulate the architecture of diphenylalanine self-assemblies. But studies with fairly high magnetic fields have not yielded the level of response as expected, though a response was forced, at a magnetic field range of 12 T or more 33 .…”
Section: Introductionmentioning
confidence: 99%
“…10 Other key properties of the dipeptide nanostructures include intrinsic ferro- 11 and piezoelectricity 12 as well as high mechanical 13 and thermal stability. 14 It has been shown that the morphologies of the assemblies can be varied through chemical modification of the FF peptide 15,16 or through control of the external conditions during the self-assembly process. 17 The most common method of preparation of crystalline FF for such applications is the dilution of a stock solution of FF in hexafluoroisopropanol (HFIP) (typically 100 g/l, 321 mM) at a ratio of 1:50 in water, producing a fine suspension of visible crystallites within seconds.…”
mentioning
confidence: 99%
“…[10] In order to improve its aqueous solubility, mannose residues were covalently attached to yield constructs 8-10 (Scheme 2). [31] Interestingly, mannose conjugation leads to a morphology switch from tubular to fibrillar and spherical structures.…”
Section: Carbohydrate Conjugationmentioning
confidence: 99%