journal article·2019-12-11

Coatings Releasing the Relaxin Peptide Analogue B7-33 Reduce Fibrotic Encapsulation

Nicholas G. Welch, Shayanti Mukherjee, Mohammed A. Hossain, Praveen Praveen, Jerome A. Werkmeister, John D. Wade, Ross A. D. Bathgate, David A. Winkler, Helmut Thissen

ACS Applied Materials & Interfaces· Volume 11· Issue 49
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Abstract

The development of antifibrotic materials and coatings that can resist the foreign body response (FBR) continues to present a major hurdle in the advancement of current and next-generation implantable medical devices, biosensors, and cell therapies. From an implant perspective, the most important issue associated with the FBR is the prolonged inflammatory response leading to a collagenous capsule that ultimately blocks mass transport and communication between the implant and the surrounding tissue. Up to now, most attempts to reduce the capsule thickness have focused on providing surface coatings that reduce protein fouling and cell attachment. Here, we present an approach that is based on the sustained release of a peptide drug interfering with the FBR. In this study, the biodegradable polymer poly(lactic-co-glycolic) acid (PLGA) was used as a coating releasing the relaxin peptide analogue B7-33, which has been demonstrated to reduce organ fibrosis in animal models. While in vitro protein quantification was used to demonstrate controlled release of the antifibrotic peptide B7-33 from PLGA coatings, an in vitro reporter cell assay was used to demonstrate that B7-33 retains activity against the relaxin family peptide receptor 1 (RXFP1). Subcutaneous implantation of PLGA-coated polypropylene samples in mice with and without the peptide demonstrated a marked reduction in capsule thickness (49.2%) over a 6 week period. It is expected that this novel approach will open the door to a range of new and improved implantable medical devices.
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Research context

OpenAlex topics: Pregnancy-related medical research

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

CSIRO Manufacturing, Research Way, Clayton, VIC 3168, Australia

The Ritchie Centre, Hudson Institute of Medical Research, Clayton, VIC 3168, Australia

The Florey Institute of Neuroscience and Mental Health, Parkville, VIC 3052, Australia

La Trobe Institute for Molecular Science, La Trobe University, Kingsbury Drive, Bundoora, VIC 3083, Australia

Monash Institute of Pharmaceutical Sciences, Royal Parade, Parkville, VIC 3052, Australia

School of Pharmacy, The University of Nottingham, Nottingham NG7 2RD, U.K.

Funding

National Health and Medical Research Council · Commonwealth Scientific and Industrial Research Organisation

References (40)

Show source-provided references
1. 10.1098/rsfs.2018.008910.1098/rsfs.2018.0089 ↗
2. 10.1038/nmat486610.1038/nmat4866 ↗
3. 10.1002/jbm.a.3595810.1002/jbm.a.35958 ↗
4. 10.1016/j.biomaterials.2010.02.01610.1016/j.biomaterials.2010.02.016 ↗
5. 10.1038/s41563-019-0377-510.1038/s41563-019-0377-5 ↗
6. 10.1016/j.polymer.2010.08.02210.1016/j.polymer.2010.08.022 ↗
7. 10.1016/s0142-9612(01)00334-910.1016/s0142-9612(01)00334-9 ↗
8. 10.1038/pj.2015.13710.1038/pj.2015.137 ↗
9. 10.1021/acs.biomac.8b0044410.1021/acs.biomac.8b00444 ↗
10. 10.1038/nbt.258010.1038/nbt.2580 ↗
11. 10.1021/acsbiomaterials.9b0087110.1021/acsbiomaterials.9b00871 ↗
12. 10.1002/adma.20110051310.1002/adma.201100513 ↗
13. 10.1038/s41551-018-0275-110.1038/s41551-018-0275-1 ↗
14. 10.1038/nbt.346210.1038/nbt.3462 ↗
15. 10.1038/nm.403010.1038/nm.4030 ↗
16. 10.1016/j.biomaterials.2013.08.09010.1016/j.biomaterials.2013.08.090 ↗
17. 10.1016/j.actbio.2013.12.05610.1016/j.actbio.2013.12.056 ↗
18. 10.1016/j.bios.2015.08.05910.1016/j.bios.2015.08.059 ↗
19. 10.1016/j.jconrel.2012.12.02810.1016/j.jconrel.2012.12.028 ↗
20. 10.1016/j.jconrel.2015.07.02110.1016/j.jconrel.2015.07.021 ↗
21. 10.1002/path.227710.1002/path.2277 ↗
22. 10.1016/j.matbio.2017.11.01010.1016/j.matbio.2017.11.010 ↗
23. 10.1126/scitranslmed.aao047510.1126/scitranslmed.aao0475 ↗
24. 10.1021/acs.jmedchem.8b0029410.1021/acs.jmedchem.8b00294 ↗
25. 10.1007/978-0-387-74672-2_710.1007/978-0-387-74672-2_7 ↗
26. 10.1111/bph.1352910.1111/bph.13529 ↗
27. 10.1016/j.pharmthera.2018.02.00810.1016/j.pharmthera.2018.02.008 ↗
28. 10.1002/ejhf.83010.1002/ejhf.830 ↗
29. 10.1016/S0140-6736(12)61855-810.1016/S0140-6736(12)61855-8 ↗
30. 10.1074/jbc.M111.28219410.1074/jbc.M111.282194 ↗
31. 10.1111/bph.1368410.1111/bph.13684 ↗
32. 10.1039/c5sc04754d10.1039/c5sc04754d ↗
33. 10.1039/C5TB00515A10.1039/C5TB00515A ↗
34. 10.1023/A:101890100906210.1023/A:1018901009062 ↗
35. 10.1021/ar980074410.1021/ar9800744 ↗
36. 10.1002/bms.120019110510.1002/bms.1200191105 ↗
37. 10.1096/fj.02-0449fje10.1096/fj.02-0449fje ↗
38. 10.1074/jbc.M60272820010.1074/jbc.M602728200 ↗
39. 10.1016/0042-207x(89)90272-810.1016/0042-207x(89)90272-8 ↗
40. 10.1089/ten.TEA.2014.026510.1089/ten.TEA.2014.0265 ↗