Switchable Hydrolase Based on Reversible Formation of Supramolecular Catalytic Site Using a Self‐Assembling Peptide

Zhang, Chunqiu; Shafi, Ramim; Lampel, Ayala; MacPherson, Douglas; Pappas, Charalampos G.; Narang, V.; Wang, Tong; Maldarelli, Charles; Ulijn, Rein V.

doi:10.1002/ange.201708036

Cited by 129 publications

(36 citation statements)

References 33 publications

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“…There are a few reportson the histidine containing short peptide based hydrogelatorswith esterase activity [54][55][56][57][58] . Korendovychand coworkers have reported a Zn 2+ ion stabilized amyloid fibril with esterase acivity, whose catalytic activity drops several times in absence of the metal ion 59 .Therefore, it is of great interest to make amino acid/peptide based molecules with a ligating group that can bind with a suitable metal ion like Fe 3+ , Hg 2+ , Cu 2+ , Zn 2+ and any of these metal complexes can eventually self-associate by using various non-covalent interactions to form either gels or soluble aggregates.…”

Section: Introductionmentioning

confidence: 99%

Amino-Acid-Based Metallo-Hydrogel That Acts Like an Esterase

Gayen

Basu

Bairagi

et al. 2018

ACS Appl. Bio Mater.

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A histidine based amphiphile containing a C14 fatty acyl chain, N-histidyl N-myristry ethyl amine (AM1, 14.7mM) forms hydrogels in the presence of Fe 3+ (within the range 1.47 to 4.41mM) and Hg 2+ (within the range 3.67 to 11.02 mM) ions in aqueous dispersions at pH 6.6 (27C). The imidazole ring of the histidine residue plays a vital role to interact with these metalions. The thermal and mechanical stability of these metallo-hydrogels can be tuned by changing the proportion of amphiphile to metal ion ratio (1:0.1 to 1:0.3 for Fe 3+ containing gel and 1:0.25 to 1:0.75 for Hg 2+ containing gel). The metallo-hydrogels were characterized by different spectroscopic and microscopic techniques, low-and wide-angle powder X-ray diffraction and small-angle X-ray scattering studies. FT-IR and NMR spectroscopic studies indicate the participation of the imidazole ring in metal-ion binding. Low-and wide-angle powder X-ray diffraction and small-angle X-ray scattering data are in favour of a layered structure of the supramolecular assembly of the AM1 in presence of metal-ions. Both, the amphiphiles and the metal ion induced hydrogels reveal catalytic activity of p-nitrophenyl esters hydrolysis for the acetyl, n-butyl and n-octyl esters. Ferric ion containing metallo-hydrogel exhibits higher catalytic activity than the corresponding AM1 aggregate in the absence of metal-ions.

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Section: Introductionmentioning

confidence: 99%

Amino-Acid-Based Metallo-Hydrogel That Acts Like an Esterase

Gayen

Basu

Bairagi

et al. 2018

ACS Appl. Bio Mater.

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“…As shown in Figure 4f, Fmoc-YL, Fmoc-Y, and Fmoc-YY-NH 2 showed a positive peak at 190-200 nm and a negative peak at ∼ 205 nm, illustrating the predominantly β-sheet arranged secondary structure. 45 Collectively, this research has instructive significance for the regulation of peptide sequences, secondary structure, morphology, and mechanical property of peptide self-assembled hydrogels with precise design and control by thermolysin at the molecular level. [46][47][48]…”

Section: Dipeptide Sequence Modification By a Thermolysin-catalyzed Tmentioning

confidence: 97%

Role of Thermolysin in Catalytic-Controlled Self-Assembly of Fmoc-Dipeptides

et al. 2020

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In recent years, short peptide self-assembled materials, prepared under the control of the thermolysin catalyst, have been investigated extensively and shown to acquire various morphologies and functions as building blocks for a wide range of biomaterials and device applications. However, the role played by thermolysin in this enzymatically triggered peptide self-assembly is still ambiguous. Herein, we designed a series of Fmoc-dipeptide amphiphiles to explore the catalytic role of thermolysin. The results from our experiments and computational simulations showed that hydrophobicity and amino acid sequences of substrates have a significant correlation with thermolysin actions, including the binding capacity and catalytic efficiency. Specifically, thermolysin favors a specific substrate pattern with a hydrophilic amino acid in the first residue and hydrophobic amino acid in the second residue. Moreover, thermolysin catalyzed reactions are bidirectional and could move toward hydrolysis or condensation based on the design of its diverse substrates (peptides). However, the specificity of the enzyme action lies in the major site of its cleavage, which is the terminal hydrophobic or bulky amino side chains. We designed a two-step reaction, taking advantage of the bidirectional catalytic actions of thermolysin, to modify the sequence of N α-fluorenylmethoxycarbonyl (Fmoc)-dipeptide from Fmoc-YL-COOH to Fmoc-YY-NH 2 and treated with thermolysin, which resulted in the enzyme-catalyzed gel-sol-gel transition. This work has an instructive significance in the regulation of peptide sequences, secondary amino acid structures, morphology, and the mechanical property of self-assembled hydrogels with precise design and control at the molecular level via thermolysin catalysis.

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“…We also provide a perspective on the potential of ENS and hope this review is useful for scientists who develop supramolecular soft matter to address societal needs at various frontiers. We would like to apologize to researchers whose work [9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25] is not discussed in more detail due to space limitations.…”

Section: Progress and Potentialmentioning

confidence: 99%

Enzymatic Noncovalent Synthesis of Supramolecular Soft Matter for Biomedical Applications

Shy

Kim

2019

Matter

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Enzymatic noncovalent synthesis (ENS), a process that integrates enzymatic reactions and supramolecular (i.e., noncovalent) interactions for spatial organization of higher-order molecular assemblies, represents an emerging research area at the interface of physical and biological sciences. This review provides a few representative examples of ENS in the context of supramolecular soft matter. After a brief comparison of enzymatic covalent and noncovalent synthesis, we discuss ENS of man-made molecules for generating supramolecular nanostructures (e.g., supramolecular hydrogels) in cell-free conditions. Then, we introduce ENS in a cellular environment. To illustrate the unique merits for applications, we discuss intercellular, peri-or intracellular, and subcellular ENS for cell morphogenesis, molecular imaging, cancer therapy, and targeted delivery. Finally, we provide an outlook on the potential of ENS. We hope that this review offers a new perspective for scientists who develop supramolecular soft matter to address societal needs at various frontiers.

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Switchable Hydrolase Based on Reversible Formation of Supramolecular Catalytic Site Using a Self‐Assembling Peptide

Cited by 129 publications

References 33 publications

Amino-Acid-Based Metallo-Hydrogel That Acts Like an Esterase

Amino-Acid-Based Metallo-Hydrogel That Acts Like an Esterase

Role of Thermolysin in Catalytic-Controlled Self-Assembly of Fmoc-Dipeptides

Enzymatic Noncovalent Synthesis of Supramolecular Soft Matter for Biomedical Applications

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