Enhancing the substrate selectivity of enzyme mimetics in biosensing and bioassay: Novel approaches

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216305%3A26620%2F24%3APU152475" target="_blank" >RIV/00216305:26620/24:PU152475 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/67985882:_____/24:00588276 RIV/62156489:43210/24:43925274 RIV/CZ______:_____/24:N0000053

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S0001868624001568?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0001868624001568?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.cis.2024.103233" target="_blank" >10.1016/j.cis.2024.103233</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Enhancing the substrate selectivity of enzyme mimetics in biosensing and bioassay: Novel approaches

Popis výsledku v původním jazyce

A substantial development in nanoscale materials possessing catalytic activities comparable with natural enzymes has been accomplished. Their advantages were owing to the excellent sturdiness in an extreme environment, possibilities of their large-scale production resulting in higher profitability, and easy manipulation for modification. Despite these advantages, the main challenge for artificial enzyme mimetics is the lack of substrate selectivity where natural enzymes flourish. This review addresses this vital problem by introducing substrate selectivity strategies to three classes of artificial enzymes: molecularly imprinted polymers, nanozymes (NZs), and DNAzymes. These rationally designed strategies enhance the substrate selectivity and are discussed and exemplified throughout the review. Various functional mechanisms associated with applying enzyme mimetics in biosensing and bioassays are also given. Eventually, future directives toward enhancing the substrate selectivity of biomimetics and related challenges are discussed and evaluated based on their efficiency and convenience in biosensing and bioassays.

Název v anglickém jazyce

Enhancing the substrate selectivity of enzyme mimetics in biosensing and bioassay: Novel approaches

Popis výsledku anglicky

A substantial development in nanoscale materials possessing catalytic activities comparable with natural enzymes has been accomplished. Their advantages were owing to the excellent sturdiness in an extreme environment, possibilities of their large-scale production resulting in higher profitability, and easy manipulation for modification. Despite these advantages, the main challenge for artificial enzyme mimetics is the lack of substrate selectivity where natural enzymes flourish. This review addresses this vital problem by introducing substrate selectivity strategies to three classes of artificial enzymes: molecularly imprinted polymers, nanozymes (NZs), and DNAzymes. These rationally designed strategies enhance the substrate selectivity and are discussed and exemplified throughout the review. Various functional mechanisms associated with applying enzyme mimetics in biosensing and bioassays are also given. Eventually, future directives toward enhancing the substrate selectivity of biomimetics and related challenges are discussed and evaluated based on their efficiency and convenience in biosensing and bioassays.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10610 - Biophysics

Projekt

<a href="/cs/project/EF16_025%2F0007314" target="_blank" >EF16_025/0007314: Multioborový výzkum pro zvýšení aplikačního potenciálu nanomateriálů v zemědělské praxi</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2024

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

ADVANCES IN COLLOID AND INTERFACE SCIENCE

ISSN

0001-8686

e-ISSN

1873-3727

Svazek periodika

331

Číslo periodika v rámci svazku

103233

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

21

Strana od-do

„“-„“

Kód UT WoS článku

001261318200001

EID výsledku v databázi Scopus

2-s2.0-85196733658