“Tuning” gel-forming protein molecules to increase their versatility for biomedical applications

Gene Kim Monclar, Professor of Chemical and Biomolecular Engineering. Credit: New York’s Tandon School of Engineering

Self-assembled protein molecules are versatile materials for medical applications because their ability to form gels can be accelerated or slowed by pH variations as well as changes in temperature or ionic strength. Thus, these biomaterials that respond to physiological conditions can be easily adapted for applications where their effectiveness depends on the kinetics of gelation, such as how quickly and under what stimuli they form gels.

Understanding gelation Kinetics for protein hydrogels are important for evaluating their usefulness in medical applications and future biomaterials. For example, rapid gelling systems are clinically useful for in situ gelling for drug delivery or genetic material to target cells or anatomical areas, while slow gelling systems are used for tissue engineering because of their ability to maintain cell viability and their tendency to maintain homogeneity.

To study this dynamic, NYU Tandon researchers led by Gene Kim Moncler, Professor of Chemical and Biomolecular Engineering, used passive microreology (compared to measuring flow behavior through active application of pressure) to extend previous jelly-based phase behavior studies. macromolecules. A previous study examined various environmental conditions, mainly changes in temperature – in part to determine the upper temperature point at which gels break down into constituent macromolecules.

In a new study that appears in the journal ASC Macromolecules, the team found, among other findings, that using pH near the isoelectric point of the protein minimizes electrostatic repulsion, allowing self-assembly and gelation. They found that the same effect could be caused by an increase in ionic strength to shield any electrostatic repulsions present.

“This is an important insight into the development of gel materials for tissue engineering and drug delivery because the tissue microenvironment has a certain pH and ionic strength,” said Moncler, who runs Montclare’s lab at New York’s Tandon University and co-authored the study. . author and Ph.D. candidate; Dustin Britton, PhD; Priya Kotel, doctoral student; Bonnie Lynn, undergraduate researcher; and Air Force Research Laboratory staffers Rhett L. Martino and Manish K. Gupta.

She noted that microreology can be performed with high performance to quickly assess the kinetics of self-assembly / gelation of a number of samples in parallel, as opposed to screening individual samples one after the other, which can be time consuming.

“Now this can allow biomaterials researchers to view a large number of different engineering materials to accelerate the development of biomaterials,” she said.

Self-assembly of fibrous hydrogels that respond to stimuli

Additional information:
Michael Meletis et al., High-throughput Microreology for Evaluating Protein Gelling Kinetics, Macromolecules (2022). DOI: 10.1021 / acs.macromol.1c02281

Citation: “Tuning” gel-forming protein molecules to enhance their versatility for biomedical applications (2022, February 16), obtained February 16, 2022 from protein-molecules -boost.html

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