Skip to content
DraconiticResearch
Search Sources API
197,768 studies31 sourcesUpdated 29 min ago
Peer-reviewedCC BY 4.0Nature Communications

Reaction enhancement via product scavenging and phase separation-driven pathway canalization

  • Byunghwa Kang1,2
  • Heonjoon Lee3
  • Eli Kengmana2
  • Jie Yi Yea4
  • Dong Woo Kim4
  • Rebecca Schulman1,2,4,5
5 affiliations
  1. 1Institute for Nanobiotechnology, Johns Hopkins University, Baltimore, Maryland USA
  2. 2Chemistry-Biology Interface Program, Johns Hopkins University, Baltimore, Maryland USA
  3. 3Department of Biomedical Engineering, Johns Hopkins University, Baltimore, Maryland USA
  4. 4Department of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, Maryland USA
  5. 5Department of Computer Science, Johns Hopkins University, Baltimore, Maryland USA
Read full textPDFDOICite

Abstract

Targeted biomolecular modification requires recognizing and binding to extended sequence domains, which can limit product dissociation rates and, therefore, catalytic efficiency. Product removal by downstream enzymes or condensates, common in biological catalysis, pushes catalytic reactions toward product formation, but cannot overcome intrinsically low product off-rates. Here, we demonstrate that designed affinity reagents, termed scavengers, can actively displace a product from an enzyme. Designed scavengers for three nucleic acid enzymes increase catalytic turnover up to 39-fold. Additionally, co-localizing enzymes and substrates, but not scavengers, within a biomolecular condensate further enhances >6-fold in catalytic rate by biasing productive substrate-enzyme interaction over inhibitory substrate-scavenger complexation. Scavenging and colocalization can be combined into a single generalizable and programmable framework, multiphase-controlled product scavenging (MCPS). By enabling rapid and exquisitely specific biomolecular modification, MCPS could lead to the development of potent nucleic acid enzyme therapeutics or efficient, controllable pathways for biomolecular modification, cleavage, and synthesis.

Related

  1. Targeted intestinal ROS scavenging alleviated rheumatoid arthritis by microbial metabolite kynurenic acid mediated Treg/Th17 balance through AhR pathway activation.
    Zhiguo Ling, Tingwen Xiang, Chuan Yang +10
    Gut microbesPeer-reviewedCC BY-NCFull textMolecular biology & gene regulationEurope PMC
  2. Osteoporosis treatment via programmed delivery of IRF5 siRNA to macrophages in bone tissue combined with ROS scavenging.
    Zining Chen, Jinjin Wu, Yunyan Zhu +5
    Bioactive materialsPeer-reviewedCC BY-NC-NDFull textMolecular biology & gene regulationEurope PMC
  3. Metabolic flux enhancement from the translational fusion of terpene synthases is linked to terpene synthase accumulation
    Li Chen Cheah, Lian Liu, Terra Stark +6
    Metabolic EngineeringPeer-reviewedLicence not statedFull text62 citedMolecular biology & gene regulationHAL
  4. Nascent RNA-mediated recruitment and R-loop suppression underlie FUS-driven enhancement of transcription
    Nilimesh Das, Yingda Ge, Fahad Rashid +8
    Nature CommunicationsPeer-reviewedCC BY-NC-ND 4.0Full textMolecular biology & gene regulationCrossref
  5. The intrinsically disordered N-terminal region of eIF5B nucleates RNA-driven phase separation
    B. K. Bodley-Gomes, M. T. Marr
    bioRxivPreprintAll rights reservedFull textGeneral biochemistrybioRxiv

Cite

BibTeXRIS
BibTeX
@article{kang2026reaction,
  title = {{Reaction enhancement via product scavenging and phase separation-driven pathway canalization}},
  author = {Byunghwa Kang and Heonjoon Lee and Eli Kengmana and Jie Yi Yea and Dong Woo Kim and Rebecca Schulman},
  journal = {Nature Communications},
  year = {2026},
  month = sep,
  doi = {10.1038/s41467-026-77899-x},
  url = {https://doi.org/10.1038/s41467-026-77899-x},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Reaction enhancement via product scavenging and phase separation-driven pathway canalization
AU  - Byunghwa Kang
AU  - Heonjoon Lee
AU  - Eli Kengmana
AU  - Jie Yi Yea
AU  - Dong Woo Kim
AU  - Rebecca Schulman
PY  - 2026
DA  - 2026/09/28
JO  - Nature Communications
DO  - 10.1038/s41467-026-77899-x
UR  - https://doi.org/10.1038/s41467-026-77899-x
AB  - Targeted biomolecular modification requires recognizing and binding to extended sequence domains, which can limit product dissociation rates and, therefore, catalytic efficiency. Product removal by downstream enzymes or condensates, common in biological catalysis, pushes catalytic reactions toward product formation, but cannot overcome intrinsically low product off-rates. Here, we demonstrate that designed affinity reagents, termed scavengers, can actively displace a product from an enzyme. Designed scavengers for three nucleic acid enzymes increase catalytic turnover up to 39-fold. Additionally, co-localizing enzymes and substrates, but not scavengers, within a biomolecular condensate further enhances >6-fold in catalytic rate by biasing productive substrate-enzyme interaction over inhibitory substrate-scavenger complexation. Scavenging and colocalization can be combined into a single generalizable and programmable framework, multiphase-controlled product scavenging (MCPS). By enabling rapid and exquisitely specific biomolecular modification, MCPS could lead to the development of potent nucleic acid enzyme therapeutics or efficient, controllable pathways for biomolecular modification, cleavage, and synthesis.
SN  - 2041-1723
ER  -