Engineering Hydrogels for Affinity-Based Release of Therapeutic Proteins

Teal, Carter J.; Lu, Sophia P.; Shoichet, Molly S.

doi:10.1021/acs.chemmater.3c02242

Cited by 4 publications

(3 citation statements)

References 300 publications

(540 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Affinity-based release modalities have been employed to prolong drug release from hydrogels, including complementary electrostatic interactions, guest-host binding, hydrogen bonding, hydrophobic interactions, and dynamic covalent interactions. 17–21 Dynamic covalent interactions are stronger than electrostatic or hydrophobic interactions and form in dynamic equilibrium under physiologically relevant conditions, allowing for drug release. 22 Dynamic covalent bonding between diol and boronic acid (BAs) motifs forms boronate esters and has been leveraged in the design of drug delivery systems.…”

Section: Mainmentioning

confidence: 99%

Enhanced dynamic covalent chemistry for the controlled release of small molecules and biologics from a nanofibrous peptide hydrogel platform

Pogostin,

Wu,

Swierczynski

et al. 2024

Preprint

View full text Add to dashboard Cite

Maintaining safe and potent pharmaceutical drug levels is often challenging. Multidomain peptides (MDPs) assemble into supramolecular hydrogels with a well-defined, highly porous nanostructure that makes them attractive for drug delivery, yet their ability to extend release is typically limited by rapid drug diffusion. To overcome this challenge, we developed self-assembling boronate ester release (SABER) MDPs capable of engaging in dynamic covalent bonding with payloads containing boronic acids (BAs). As examples, we demonstrate that SABER hydrogels can prolong the release of five BA-containing small-molecule drugs as well as BA-modified insulin and antibodies. Pharmacokinetic studies revealed that SABER hydrogels extended the therapeutic effect of ganfeborole from days to weeks, preventing Mycobacterium tuberculosis growth better than repeated oral administration in an infection model. Similarly, SABER hydrogels extended insulin activity, maintaining normoglycemia for six days in diabetic mice after a single injection. These results suggest that SABER hydrogels present broad potential for clinical translation.

show abstract

Section: Mainmentioning

confidence: 99%

Enhanced dynamic covalent chemistry for the controlled release of small molecules and biologics from a nanofibrous peptide hydrogel platform

Pogostin,

Wu,

Swierczynski

et al. 2024

Preprint

View full text Add to dashboard Cite

show abstract

“…By integrating smart materials into one of these delivery systems, the systems gain the ability to respond to external stimuli like temperature or pH, enabling an even more precise control over the release of proteins and reducing side effects and, thereby, patient non-compliance [164]. For example, certain multilayered scaffolds and hydrogels can release different active molecules when the body indicates a certain healing phase or immune response; however, success with a polymer-based stimuli-responsive smart biomaterial is still a much more novel idea, as a far deeper understanding of the human body, diseases/stimuli, and interactions between human immune cells and biomaterials [42,165,166].…”

Section: Advancements In Biomaterials Fabrication Technologiesmentioning

confidence: 99%

Biomaterials for Protein Delivery: Opportunities and Challenges to Clinical Translation

Gorantla,

Hall,

Troidle

et al. 2024

Micromachines

View full text Add to dashboard Cite

The development of biomaterials for protein delivery is an emerging field that spans materials science, bioengineering, and medicine. In this review, we highlight the immense potential of protein-delivering biomaterials as therapeutic options and discuss the multifaceted challenges inherent to the field. We address current advancements and approaches in protein delivery that leverage stimuli-responsive materials, harness advanced fabrication techniques like 3D printing, and integrate nanotechnologies for greater targeting and improved stability, efficacy, and tolerability profiles. We also discuss the demand for highly complex delivery systems to maintain structural integrity and functionality of the protein payload. Finally, we discuss barriers to clinical translation, such as biocompatibility, immunogenicity, achieving reliable controlled release, efficient and targeted delivery, stability issues, scalability of production, and navigating the regulatory landscape for such materials. Overall, this review summarizes insights from a survey of the current literature and sheds light on the interplay between innovation and the practical implementation of biomaterials for protein delivery.

show abstract

“…Capable of moderating biological activities and cellular pathways in which small molecular drugs may not be able to, protein therapeutics have been intensively investigated. 28 One of the biggest challenges in this area is achieving a high loading efficiency while not destabilizing the unique structures of proteins. 29 To address this issue, considerable efforts have been made to encapsulate protein via different techniques.…”

Section: Introductionmentioning

confidence: 99%

Polydopamine-Coated Polymer Nanofibers for In Situ Protein Loading and Controlled Release

Zhang,

Dop,

Zhang

2024

ACS Omega

View full text Add to dashboard Cite

Nanofibrous polymeric materials, combined with protein therapeutics, play a significant role in biomedical and pharmaceutical applications. However, the upload of proteins into nanofibers with a high yield and controlled release has been a challenging issue. Here, we report the in situ loading of a model protein (bovine serum albumin) into hydrophilic poly(vinyl alcohol) nanofibers via ice-templating, with a 100% protein drug loading efficiency. These protein-loaded nanofibers were further coated by polydopamine in order to improve the nanofiber stability and achieve a controlled protein release. The mass ratio between poly(vinyl alcohol) and bovine serum albumin influenced the percentage of proteins in composite nanofibers and fiber morphology. More particles and less nanofibers were formed with an increasing percentage of bovine serum albumin. By varying the coating conditions, it was possible to produce a uniform polydopamine coating with tunable thickness, which acted as an additional barrier to reduce burst release and achieve a more sustained release profile.

show abstract

Engineering Hydrogels for Affinity-Based Release of Therapeutic Proteins

Cited by 4 publications

References 300 publications

Enhanced dynamic covalent chemistry for the controlled release of small molecules and biologics from a nanofibrous peptide hydrogel platform

Enhanced dynamic covalent chemistry for the controlled release of small molecules and biologics from a nanofibrous peptide hydrogel platform

Biomaterials for Protein Delivery: Opportunities and Challenges to Clinical Translation

Polydopamine-Coated Polymer Nanofibers for In Situ Protein Loading and Controlled Release

Contact Info

Product

Resources

About