journal article·2015-10-12

Thermally Controlled Collagen Peptide Cages for Biopolymer Delivery

Jeremy Gleaton, Jean Chmielewski

Publisher page

Abstract

The hierarchical assembly of collagen-based triple helical peptides into disks, followed by metal-promoted assembly into microcages is described. The length of the triple helix was found to correlate to the height of the disks that formed, providing mechanistic insights into their formation. The encapsulation of fluorescently labeled dextrans within the peptide microcages, and their subsequent thermal release is detailed. The half-life for thermal release of the encapsulated cargo from the cages was found to increase as the peptide triple helix stability increased, providing a means to engineer cargo delivery rates through peptide design.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Collagen: Extraction and Characterization · Silk-based biomaterials and applications · Protein Hydrolysis and Bioactive Peptides

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

Affiliations

Department of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, Indiana 47907, United States

Funding

Division of Chemistry

References (41)

Show source-provided references
1. 10.1146/annurev.biochem.77.032207.12083310.1146/annurev.biochem.77.032207.120833 ↗
2. Boyle A. L. · 2012
3. 10.1021/bi902129p10.1021/bi902129p ↗
4. 10.1073/pnas.080029110510.1073/pnas.0800291105 ↗
5. 10.1021/ja066986f10.1021/ja066986f ↗
6. 10.1073/pnas.050878310310.1073/pnas.0508783103 ↗
7. 10.1016/j.bmcl.2005.08.04110.1016/j.bmcl.2005.08.041 ↗
8. 10.1021/bm900551c10.1021/bm900551c ↗
9. 10.1021/ma051406510.1021/ma0514065 ↗
10. 10.1038/nchem.112310.1038/nchem.1123 ↗
11. 10.1021/ja075899010.1021/ja0758990 ↗
12. 10.1021/ja804942w10.1021/ja804942w ↗
13. 10.1021/ja412867z10.1021/ja412867z ↗
14. 10.1002/anie.20140378010.1002/anie.201403780 ↗
15. 10.1021/ja410654510.1021/ja4106545 ↗
16. 10.1021/ja808884510.1021/ja8088845 ↗
17. 10.1021/ja204264510.1021/ja2042645 ↗
18. 10.1021/ja103148t10.1021/ja103148t ↗
19. 10.1021/ja307651e10.1021/ja307651e ↗
20. 10.1002/anie.20090237510.1002/anie.200902375 ↗
21. 10.1016/j.biomaterials.2014.05.01910.1016/j.biomaterials.2014.05.019 ↗
22. 10.1021/bm500091e10.1021/bm500091e ↗
23. 10.1021/bm200493410.1021/bm2004934 ↗
24. 10.1111/j.1399-3011.1991.tb01418.x10.1111/j.1399-3011.1991.tb01418.x ↗
25. 10.1016/S0968-0896(98)00230-210.1016/S0968-0896(98)00230-2 ↗
26. 10.1110/ps.0350170410.1110/ps.03501704 ↗
27. 10.1016/j.peptides.2012.04.01310.1016/j.peptides.2012.04.013 ↗
28. 10.1126/science.769569910.1126/science.7695699 ↗
29. 10.1016/0022-2836(81)90252-710.1016/0022-2836(81)90252-7 ↗
30. 10.1002/(SICI)1521-3773(19980904)37:16<2201::AID-ANIE2201>3.0.CO;2-E10.1002/(SICI)1521-3773(19980904)37:16<2201::AID-ANIE2201>3.0.CO;2-E ↗
31. Kim K. K. · 2006 · 1910.1007/978-0-387-25842-3_2 ↗
32. 10.1128/AAC.01329-1010.1128/AAC.01329-10 ↗
33. 10.1016/j.abb.2012.10.01510.1016/j.abb.2012.10.015 ↗
34. 10.1146/annurev.biophys.093008.13141810.1146/annurev.biophys.093008.131418 ↗
35. 10.1126/science.121935110.1126/science.1219351 ↗
36. 10.1126/science.121936410.1126/science.1219364 ↗
37. 10.1038/nature1340410.1038/nature13404 ↗
38. 10.1126/science.123393610.1126/science.1233936 ↗
39. 10.1039/c4nr00915k10.1039/c4nr00915k ↗
40. 10.1021/nn302183h10.1021/nn302183h ↗
41. 10.1021/bm200983k10.1021/bm200983k ↗