ArticleBiomacromolecules2022
Charge-Modulated Accessibility of Tyrosine Residues for Silk-Elastin Copolymer Cross-Linking.
Article in Biomacromolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 7 citations in OpenAlex.
- Effects of Mini-Spidroin Repeat Region on the Mechanical Properties of Artificial Spider Silk Fibers.ACS omega · 2024Article
- Cross-Linking Methods of the Silk Protein Hydrogel in Oral and Craniomaxillofacial Tissue Regeneration.Tissue engineering and regenerative medicine · 2024Review
- Genetically Fusing Order-Promoting and Thermoresponsive Building Blocks to Design Hybrid Biomaterials.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The modulation of reaction kinetics with horseradish peroxidase (HRP)-catalyzed cross-linking of proteins remains a useful strategy to modulate hydrogel formation. Here, we demonstrate that the presence of positively charged lysines in silk-elastin-like polymers impacts the thermal transition temperature of these proteins, while the location in the primary sequence modulates the reactivity of the tyrosines. The positively charged lysine side chains decreased π-π interactions among the tyrosines and reduced the rate of formation and number of HRP-mediated dityrosine bonds, dependent on the proximity of the charged group to the tyrosine. The results suggest that the location of repulsive charges can be used to tailor the reaction kinetics for enzymatic cross-linking, providing further control of gelation rates for
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