Enzyme mimics based on self-assembled peptides for di(2-ethylhexyl)phthalate degradation. Issue 41 (2nd October 2020)
- Record Type:
- Journal Article
- Title:
- Enzyme mimics based on self-assembled peptides for di(2-ethylhexyl)phthalate degradation. Issue 41 (2nd October 2020)
- Main Title:
- Enzyme mimics based on self-assembled peptides for di(2-ethylhexyl)phthalate degradation
- Authors:
- Li, Xia
Li, Jianpeng
Hao, Sijia
Han, Ailing
Yang, Yayu
Luo, Xiaoyu
Fang, Guozhen
Liu, Jifeng
Wang, Shuo - Abstract:
- Abstract : Enzyme mimics inspired by serine proteases are developed through self-assembled peptides to degrade di(2-ethylhexyl)phthalate (DEHP). Abstract : Enzyme mimics have been developed by imitating and incorporating specific features of native enzymes to achieve catalytic activity, and are expectedly comparable to that of native enzymes. Here, inspired by the "catalytic triad" in serine proteases, a series of peptide-based enzyme mimics were designed to follow the rational design principle of peptides via self-assembly, and were further applied in the degradation of di(2-ethylhexyl)phthalate (DEHP). The relationship of the structure of enzyme mimics with their degradation activity was analyzed by transmission electron microscopy, fluorescence spectroscopy, circular dichroism, Raman spectroscopy, X-ray diffraction spectroscopy, and computational modeling. These results show that the hydrophobic skeleton, amino acid sequence, species, and periodic distribution have important effects on the structure of the peptide sequence and the number of hydrogen bonds; in addition, pH can also affect the self-assembly characteristics of peptides and the formation of stable fibers, which are all closely linked to the catalytic activity of the enzyme mimics. The self-assembled peptides had a stable fibrous morphology and secondary structure after the DEHP degradation assay. The enzyme mimics with high catalytic activity constructed from the self-assembled peptides may provide guidanceAbstract : Enzyme mimics inspired by serine proteases are developed through self-assembled peptides to degrade di(2-ethylhexyl)phthalate (DEHP). Abstract : Enzyme mimics have been developed by imitating and incorporating specific features of native enzymes to achieve catalytic activity, and are expectedly comparable to that of native enzymes. Here, inspired by the "catalytic triad" in serine proteases, a series of peptide-based enzyme mimics were designed to follow the rational design principle of peptides via self-assembly, and were further applied in the degradation of di(2-ethylhexyl)phthalate (DEHP). The relationship of the structure of enzyme mimics with their degradation activity was analyzed by transmission electron microscopy, fluorescence spectroscopy, circular dichroism, Raman spectroscopy, X-ray diffraction spectroscopy, and computational modeling. These results show that the hydrophobic skeleton, amino acid sequence, species, and periodic distribution have important effects on the structure of the peptide sequence and the number of hydrogen bonds; in addition, pH can also affect the self-assembly characteristics of peptides and the formation of stable fibers, which are all closely linked to the catalytic activity of the enzyme mimics. The self-assembled peptides had a stable fibrous morphology and secondary structure after the DEHP degradation assay. The enzyme mimics with high catalytic activity constructed from the self-assembled peptides may provide guidance for the future degradation of DEHP in food packaging or water treatment, and also give insights into the design of enzyme mimics in other related fields. … (more)
- Is Part Of:
- Journal of materials chemistry. Volume 8:Issue 41(2020)
- Journal:
- Journal of materials chemistry
- Issue:
- Volume 8:Issue 41(2020)
- Issue Display:
- Volume 8, Issue 41 (2020)
- Year:
- 2020
- Volume:
- 8
- Issue:
- 41
- Issue Sort Value:
- 2020-0008-0041-0000
- Page Start:
- 9601
- Page End:
- 9609
- Publication Date:
- 2020-10-02
- Subjects:
- Materials -- Periodicals
Chemistry, Analytic -- Periodicals
Biomedical materials -- Research -- Periodicals
543.0284 - Journal URLs:
- http://pubs.rsc.org/en/journals/journalissues/tb# ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/d0tb01931c ↗
- Languages:
- English
- ISSNs:
- 2050-750X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5012.205200
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 14748.xml