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Combined Modification of Fiber Materials by Enzymes and Metal Nanoparticles for Chemical and Biological Protection.


ABSTRACT: To obtain fiber materials with pronounced chemical-biological protection, metal (Zn or Ta) nanoparticles were jointly applied with polyelectrolyte complexes of enzymes and polypeptides being their stabilizers. Computer modeling revealed the preferences between certain polyelectrolyte partners for N-acyl-homoserine lactone acylase and hexahistidine-tagged organophosphorus hydrolase (His6-OPH) possessing the quorum quenching (QQ) behavior with bacterial cells. The combinations of metal nanoparticles and enzymes appeared to function better as compared to the combinations of the same QQ-enzymes with antibiotics (polymyxins), making it possible to decrease the applied quantities by orders of magnitude while giving the same effect. The elimination of Gram-positive and Gram-negative bacterial cells from doubly modified fiber materials notably increased (up to 2.9-fold), whereas His6-OPH retained its hydrolytic activity in reaction with organophosphorus compounds (up to 74% of initially applied activity). Materials with the certain enzyme and Zn nanoparticles were more efficient against Bacillus subtilis cells (up to 2.1-fold), and Ta nanoparticles acted preferentially against Escherichia coli (up to 1.5-fold). Some materials were proved to be more suitable for combined modification by metal nanoparticles and His6-OPH complexes as antimicrobial protectants.

SUBMITTER: Lyagin I 

PROVIDER: S-EPMC8835833 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature

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Combined Modification of Fiber Materials by Enzymes and Metal Nanoparticles for Chemical and Biological Protection.

Lyagin Ilya I   Stepanov Nikolay N   Frolov George G   Efremenko Elena E  

International journal of molecular sciences 20220125 3


To obtain fiber materials with pronounced chemical-biological protection, metal (Zn or Ta) nanoparticles were jointly applied with polyelectrolyte complexes of enzymes and polypeptides being their stabilizers. Computer modeling revealed the preferences between certain polyelectrolyte partners for <i>N</i>-acyl-homoserine lactone acylase and hexahistidine-tagged organophosphorus hydrolase (His<sub>6</sub>-OPH) possessing the quorum quenching (QQ) behavior with bacterial cells. The combinations of  ...[more]

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