Molecularly imprinted peptide-based enzyme mimics with enhanced activity and specificity

Li, Jingyi; Zhu, Mingjie; Wang, Mengfan; Qi, Wei; Su, Rongxin; He, Zhimin

doi:10.1039/d0sm00635a

Cited by 27 publications

(24 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A similar research was reported by Chen et al who developed homovanillic acid-imprinted hemin-containing catalyst as peroxidase-mimic system in a form of nanogels [12]. An interesting approach to the preparation of peroxidase-mimic catalysts was recently published by Li et al [13]. The authors used Fmoc-tripeptide and hemin for self-assembling monomers and template (2,2 -azinobis -(3-ethylbenzthiazoline-6-sulfonate)) to form the catalytic centers.…”

Section: Introductionmentioning

confidence: 63%

See 1 more Smart Citation

Flow-Through Macroporous Polymer Monoliths Containing Artificial Catalytic Centers Mimicking Chymotrypsin Active Site

et al. 2020

View full text Add to dashboard Cite

Synthetic catalysts that could compete with enzymes in term of the catalytic efficiency but surpass them in stability have a great potential for the practical application. In this work, we have developed a novel kind of organic catalysts based on flow-through macroporous polymer monoliths containing catalytic centers that mimic the catalytic site of natural enzyme chymotrypsin. It is known that chymotrypsin catalytic center consists of L-serine, L-histidine, and L-aspartic acid and has specificity to C-terminal residues of hydrophobic amino acids (L-phenylalanine, L-tyrosine, and L-tryptophan). In this paper, we have prepared the macroporous polymer monoliths bearing grafted polymer layer on their surface. The last one was synthesized via copolymerization of N-methacryloyl-L-serine, N-methacryloyl-L-histidine, and N-methacryloyl-L-aspartic acid. The spatial orientation of amino acids in the polymer layer, generated on the surface of monolithic framework, was achieved by coordinating amino acid-polymerizable derivatives with cobalt (II) ions without substrate-mimicking template and with its use. The conditions for the preparation of mimic materials were optimized to achieve a mechanically stable system. Catalytic properties of the developed systems were evaluated towards the hydrolysis of ester bond in a low molecular substrate and compared to the results of using chymotrypsin immobilized on the surface of a similar monolithic framework. The effect of flow rate increase and temperature elevation on the hydrolysis efficiency were evaluated for both mimic monolith and column with immobilized enzyme.

show abstract

Section: Introductionmentioning

confidence: 63%

“…The preparation of artificial enzyme-mimic catalysts by molecular imprinting (molecularly imprinted catalysts, MICs) and their study have been reported in a number of original papers [11][12][13][14] and some reviews [4,15]. Among the mimicking enzymes, metalloproteinases [12,16] and hydrolases [14,17] can be mentioned.…”

Section: Introductionmentioning

confidence: 99%

Flow-Through Macroporous Polymer Monoliths Containing Artificial Catalytic Centers Mimicking Chymotrypsin Active Site

et al. 2020

View full text Add to dashboard Cite

show abstract

“…Pragmatic design of biomimetic synthetic enzyme systems to explore the catalytic activities of artificial systems circumventing the limitations of natural enzymes viz. denaturation, non‐compatibility with organic chemical and solvents are of particular interest in synthetic biology [36,37] . Although several attempts have been initiated to develop high‐efficiency enzyme mimics, the complicated synthesis protocols, low yields and structural incompatibility are some of the major issues to be addressed.…”

Section: Biosensing and Catalysismentioning

confidence: 99%

Molecular Architectonics‐guided Design of Biomaterials

Moorthy

Datta

Govindaraju

2021

Chemistry An Asian Journal

View full text Add to dashboard Cite

The quest for mastering the controlled engineering of dynamic molecular assemblies is the basis of molecular architectonics. The rational use of noncovalent interactions to programme the molecular assemblies allow the construction of diverse molecular and material architectures with novel functional properties and applications. Understanding and controlling the assembly of molecular systems are daunting tasks owing to the complex factors that govern at the molecular level. Molecular architectures depend on the design of functional molecular modules through the judicious selection of functional core and auxiliary units to guide the precise molecular assembly and co‐assembly patterns. Biomolecules with built‐in information for molecular recognition are the ultimate examples of evolutionary guided molecular recognition systems that define the structure and functions of living organisms. Explicit use of biomolecules as auxiliary units to command the molecular assemblies of functional molecules is an intriguing exercise in the scheme of molecular architectonics. In this minireview, we discuss the implementation of the principles of molecular architectonics for the development of novel biomaterials with functional properties and applications ranging from sensing, drug delivery to neurogeneration and tissue engineering. We present the molecular designs pioneered by our group owing to the requirement and scope of the article while acknowledging the designs pursued by several research groups that befit the concept.

show abstract

“…Major advantages are related to the fact that the building blocks of peptides are amino acids that work as catalytic groups, assemble, and form supramolecular structures through noncovalent interactions, all traits of natural enzymes [ 73 ]. Based on this approach, many artificial enzymes have been constructed, such as hydrolases, aldolase, oxidoreductase, among others [ 73 , 74 , 75 ]. As for other synthetic alternatives, lower catalytic activity and substrate specificity are still challenging, and molecular imprinting can contribute to improving those features.…”

Section: Molecular Imprinting Technologymentioning

confidence: 99%

“…Another example is the work of Li et al, 2020, who developed a peroxidase-like enzyme by the co-assembly of Hemin and Fmoc-FFH, combined with an imprinted polymer of the substrate ABTS. Since the polymer components can be easily adjusted, the addition of a cationic monomer further enhanced the catalytic activity because the electrostatic interaction created a synergistic effect [ 73 ].…”

Section: Molecular Imprinting Technologymentioning

confidence: 99%

Molecular Imprinting on Nanozymes for Sensing Applications

et al. 2021

View full text Add to dashboard Cite

As part of the biomimetic enzyme field, nanomaterial-based artificial enzymes, or nanozymes, have been recognized as highly stable and low-cost alternatives to their natural counterparts. The discovery of enzyme-like activities in nanomaterials triggered a broad range of designs with various composition, size, and shape. An overview of the properties of nanozymes is given, including some examples of enzyme mimics for multiple biosensing approaches. The limitations of nanozymes regarding lack of selectivity and low catalytic efficiency may be surpassed by their easy surface modification, and it is possible to tune specific properties. From this perspective, molecularly imprinted polymers have been successfully combined with nanozymes as biomimetic receptors conferring selectivity and improving catalytic performance. Compelling works on constructing imprinted polymer layers on nanozymes to achieve enhanced catalytic efficiency and selective recognition, requisites for broad implementation in biosensing devices, are reviewed. Multimodal biomimetic enzyme-like biosensing platforms can offer additional advantages concerning responsiveness to different microenvironments and external stimuli. Ultimately, progress in biomimetic imprinted nanozymes may open new horizons in a wide range of biosensing applications.

show abstract

Molecularly imprinted peptide-based enzyme mimics with enhanced activity and specificity

Abstract:
We herein report the construction of peroxidase (POD)-mimicking catalysts based on the strategy of peptide assembly and molecular imprinting. Upon the co-assembly of Fmoc-FFH and hemin, we firstly fabricated the...

Cited by 27 publications

References 46 publications

Flow-Through Macroporous Polymer Monoliths Containing Artificial Catalytic Centers Mimicking Chymotrypsin Active Site

Flow-Through Macroporous Polymer Monoliths Containing Artificial Catalytic Centers Mimicking Chymotrypsin Active Site

Molecular Architectonics‐guided Design of Biomaterials

Molecular Imprinting on Nanozymes for Sensing Applications

Contact Info

Product

Resources

About

Molecularly imprinted peptide-based enzyme mimics with enhanced activity and specificity

Abstract: We herein report the construction of peroxidase (POD)-mimicking catalysts based on the strategy of peptide assembly and molecular imprinting. Upon the co-assembly of Fmoc-FFH and hemin, we firstly fabricated the...

Cited by 27 publications

References 46 publications

Flow-Through Macroporous Polymer Monoliths Containing Artificial Catalytic Centers Mimicking Chymotrypsin Active Site

Flow-Through Macroporous Polymer Monoliths Containing Artificial Catalytic Centers Mimicking Chymotrypsin Active Site

Molecular Architectonics‐guided Design of Biomaterials

Molecular Imprinting on Nanozymes for Sensing Applications

Contact Info

Product

Resources

About

Abstract:
We herein report the construction of peroxidase (POD)-mimicking catalysts based on the strategy of peptide assembly and molecular imprinting. Upon the co-assembly of Fmoc-FFH and hemin, we firstly fabricated the...