Exploiting enzymatic (reversed) hydrolysis in directed self-assembly of peptide nanostructures

Apurba K. Das, Richard Collins, Rein V. Ulijn

Research output: Contribution to journalArticle

118 Citations (Scopus)

Abstract

Enzyme-catalyzed reactions can be exploited to control molecular self-assembly under physiological conditions by converting nonassembling precursors into self-assembly building blocks. Two complementary approaches based on aromatic short-peptide derivatives that form molecular hydrogels are demonstrated. Firstly, it is shown that esterase-directed self assembly via hydrolysis of hydrophobic N-(fluorenyl-9-methoxycarbonyl) (Fmoc)-peptide methyl esters give rise to formation of transparent hydrogels composed of defined peptide nanotubes. The internal and external diameters of these tubes are highly tunable, depending on the amino acid composition and chain length, of the building blocks. Secondly, protease-directed self-assembly of Fmoc-peptide esters is achieved via amide-bond formation (reversed hydrolysis) for combinations of Fmoc-threonine and leucine/phenylalanine methyl esters, producing fibrous hydrogels. Upon treatment with an esterase, these systems revert back to solution, thus providing a two-stage solution-gel-solution transition.

LanguageEnglish
Pages279-287
Number of pages9
JournalSmall
Volume4
Issue number2
DOIs
Publication statusPublished - 1 Feb 2008

Fingerprint

Hydrogels
Enzymatic hydrolysis
Nanostructures
Self assembly
Peptides
Hydrolysis
Esterases
Esters
Peptide Nanotubes
Threonine
Amides
Peptide Hydrolases
Gels
Chain length
Leucine
Nanotubes
Amino acids
Amino Acids
Enzymes
Derivatives

Keywords

  • enzymatic (reversed) hydrolysis
  • peptide nanostructures
  • self-assembly
  • self-assembly
  • enzymes
  • hydrogels
  • hydrolysis
  • nanotubes

Cite this

Das, Apurba K. ; Collins, Richard ; Ulijn, Rein V. / Exploiting enzymatic (reversed) hydrolysis in directed self-assembly of peptide nanostructures. In: Small. 2008 ; Vol. 4, No. 2. pp. 279-287.
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Exploiting enzymatic (reversed) hydrolysis in directed self-assembly of peptide nanostructures. / Das, Apurba K.; Collins, Richard; Ulijn, Rein V.

In: Small, Vol. 4, No. 2, 01.02.2008, p. 279-287.

Research output: Contribution to journalArticle

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AB - Enzyme-catalyzed reactions can be exploited to control molecular self-assembly under physiological conditions by converting nonassembling precursors into self-assembly building blocks. Two complementary approaches based on aromatic short-peptide derivatives that form molecular hydrogels are demonstrated. Firstly, it is shown that esterase-directed self assembly via hydrolysis of hydrophobic N-(fluorenyl-9-methoxycarbonyl) (Fmoc)-peptide methyl esters give rise to formation of transparent hydrogels composed of defined peptide nanotubes. The internal and external diameters of these tubes are highly tunable, depending on the amino acid composition and chain length, of the building blocks. Secondly, protease-directed self-assembly of Fmoc-peptide esters is achieved via amide-bond formation (reversed hydrolysis) for combinations of Fmoc-threonine and leucine/phenylalanine methyl esters, producing fibrous hydrogels. Upon treatment with an esterase, these systems revert back to solution, thus providing a two-stage solution-gel-solution transition.

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