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

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

Research output: Contribution to journalArticlepeer-review

135 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)279-287
Number of pages9
Issue number2
Publication statusPublished - 1 Feb 2008


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


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