journal article·2018-10

Crosslinked fibroin nanoparticles using EDC or PEI for drug delivery: physicochemical properties, crystallinity and structure

Duy Toan Pham, Nuttawut Saelim, Waree Tiyaboonchai

Journal of Materials Science· Volume 53· Issue 20
Publisher page

Abstract

A new silk fibroin-based nanoparticles (FNPs) have been successfully developed utilizing crosslinker EDC (EDC-FNPs) or cationic polymer poly(ethyleneimine) (PEI-FNPs). All developed crosslinked FNPs show a similar spherical particle size of ~ 300 nm. Depending on the amount of EDC or the addition of PEI, the zeta potential could be controlled favorably and range from − 15 mV to + 30 mV. Particle structures and crystallinity index are determined and compared using different techniques; X-ray diffraction (XRD), Fourier-transformed infrared spectroscopy (FT-IR), differential scanning calorimetry and nuclear magnetic resonance (NMR). The most reliable crystallinity calculation methods are based on FT-IR and NMR. The degree of fibroin crystallinity increases with increasing EDC content, whereas PEI reduces it. Exceptionally, XRD shows a reverse order of crystallinity due to the inability to detect short-range ordered structures. Proposed schematic particle structures match all experimental data. In conclusion, the crosslinked fibroin-based nanoparticle properties could be manipulated by using carbodiimide or PEI crosslinkers. In addition, both EDC-FNPs and PEI-FNPs showed high potential as a drug delivery system.
Source: openaire · Quality: candidate unverified · Source record ↗

Research context

OpenAlex topics: Silk-based biomaterials and applications · Polymer Surface Interaction Studies · Electrospun Nanofibers in Biomedical Applications

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

References (46)

Show source-provided references
1. Martínez-Mora C et al (2012) Fibroin and sericin from Bombyx mori silk stimulate cell migration through upregulation and phosphorylation of c-jun. PLoS ONE 7:e42271. https://doi.org/10.1371/journal.pone.004227110.1371/journal.pone.0042271 ↗
2. Zaoming W, Codina R, Fernández-Caldas E, Lockey RF (1996) Partial characterization of the silk allergens in mulberry silk extract. J Investig Allergol Clin Immunol 6:237–241
3. Altman GH et al (2003) Silk-based biomaterials. Biomaterials 24:401–416. https://doi.org/10.1016/S0142-9612(02)00353-810.1016/S0142-9612(02)00353-8 ↗
4. Numata K, Kaplan DL (2010) Silk-based delivery systems of bioactive molecules. Adv Drug Deliv Rev 62:1497–1508. https://doi.org/10.1016/j.addr.2010.03.00910.1016/j.addr.2010.03.009 ↗
5. Sharma S et al (2016) Silk fibroin nanoparticles support in vitro sustained antibiotic release and osteogenesis on titanium surface. Nanomedicine 12:1193–1204. https://doi.org/10.1016/j.nano.2015.12.38510.1016/j.nano.2015.12.385 ↗
6. Lozano-Pérez AA et al (2014) Silk fibroin nanoparticles constitute a vector for controlled release of resveratrol in an experimental model of inflammatory bowel disease in rats. Int J Nanomed 9:4507–4520. https://doi.org/10.2147/IJN.S6852610.2147/IJN.S68526 ↗
7. Zhang YQ et al (2006) Synthesis of silk fibroin-insulin bioconjugates and their characterization and activities in vivo. J Biomed Mater Res B Appl Biomater 79:275–283. https://doi.org/10.1002/jbm.b.3053910.1002/jbm.b.30539 ↗
8. Gupta V, Aseh A, Ríos CN, Aggarwal BB, Mathur AB (2009) Fabrication and characterization of silk fibroin-derived curcumin nanoparticles for cancer therapy. Int J Nanomed 4:115–12210.2147/IJN.S5581 ↗
9. Seib FP, Jones GT, Rnjak-Kovacina J, Lin Y, Kaplan DL (2013) pH-dependent anticancer drug release from silk nanoparticles. Adv Healthc Mater 2:1606–1611. https://doi.org/10.1002/adhm.20130003410.1002/adhm.201300034 ↗
10. Subia B, Chandra S, Talukdar S, Kundu SC (2014) Folate conjugated silk fibroin nanocarriers for targeted drug delivery. Integr Biol (Camb) 6:203–214. https://doi.org/10.1039/c3ib40184g10.1039/C3IB40184G ↗
11. Vepari C, Kaplan DL (2007) Silk as a biomaterial. Prog Polym Sci 32:991–1007. https://doi.org/10.1016/j.progpolymsci.2007.05.01310.1016/j.progpolymsci.2007.05.013 ↗
12. Park S, Baker JO, Himmel ME, Parilla PA, Johnson DK (2010) Cellulose crystallinity index: measurement techniques and their impact on interpreting cellulase performance. Biotechnol Biofuels. https://doi.org/10.1186/1754-6834-3-1010.1186/1754-6834-3-10 ↗
13. Jin HJ, Fridrikh SV, Rutledge GC, Kaplan DL (2002) Electrospinning Bombyx mori silk with poly(ethylene oxide). Biomacromol 3:1233–1239. https://doi.org/10.1021/bm025581u10.1021/bm025581u ↗
14. Lu Q et al (2010) Water-insoluble silk films with silk I structure. Acta Biomater 6:1380–1387. https://doi.org/10.1016/j.actbio.2009.10.04110.1016/j.actbio.2009.10.041 ↗
15. Lammel A, Hu X, Park S-H, Kaplan DL, Scheibel T (2010) Controlling silk fibroin particle features for drug delivery. Biomaterials 31:4583–4591. https://doi.org/10.1016/j.biomaterials.2010.02.02410.1016/j.biomaterials.2010.02.024 ↗
16. Hofmann S et al (2006) Silk fibroin as an organic polymer for controlled drug delivery. J Control Release 111:219–227. https://doi.org/10.1016/j.jconrel.2005.12.00910.1016/j.jconrel.2005.12.009 ↗
17. Wang X et al (2007) Silk microspheres for encapsulation and controlled release. J Control Release 117:360–370. https://doi.org/10.1016/j.jconrel.2006.11.02110.1016/j.jconrel.2006.11.021 ↗
18. Mottaghitalab F, Farokhi M, Shokrgozar MA, Atyabi F, Hosseinkhani H (2015) Silk fibroin nanoparticle as a novel drug delivery system. J Control Release 206:161–176. https://doi.org/10.1016/j.jconrel.2015.03.02010.1016/j.jconrel.2015.03.020 ↗
19. Bhat NV, Nadiger GS (1980) Crystallinity in silk fibers: partial acid hydrolysis and related studies. J Appl Polym Sci 25:921–932. https://doi.org/10.1002/app.1980.07025051810.1002/app.1980.070250518 ↗
20. Cebe P et al (2017) Silk I and silk II studied by fast scanning calorimetry. Acta Biomater 55:323–332. https://doi.org/10.1016/j.actbio.2017.04.00110.1016/j.actbio.2017.04.001 ↗
21. Kamalha E, Zheng Y, Zeng Y (2013) Analysis of the secondary crystalline structure of regenerated Bombyx mori fibroin. Res Rev Biosci 7:76–83
22. Um IC, Kweon HY, Park YH, Hudson S (2001) Structural characteristics and properties of the regenerated silk fibroin prepared from formic acid. Int J Biol Macromol 29:91–97. https://doi.org/10.1016/S0141-8130(01)00159-310.1016/S0141-8130(01)00159-3 ↗
23. Zhao Z, Li Y, Xie M-B (2015) Silk fibroin-based nanoparticles for drug delivery. Int J Mol Sci 16:4880–4903. https://doi.org/10.3390/ijms1603488010.3390/ijms16034880 ↗
24. Kundu J, Chung Y-I, Kim YH, Tae G, Kundu SC (2010) Silk fibroin nanoparticles for cellular uptake and control release. Int J Pharm 388:242–250. https://doi.org/10.1016/j.ijpharm.2009.12.05210.1016/j.ijpharm.2009.12.052 ↗
25. Shi P, Goh JCH (2011) Release and cellular acceptance of multiple drugs loaded silk fibroin particles. Int J Pharm 420:282–289. https://doi.org/10.1016/j.ijpharm.2011.08.05110.1016/j.ijpharm.2011.08.051 ↗
26. Min BM et al (2004) Electrospinning of silk fibroin nanofibers and its effect on the adhesion and spreading of normal human keratinocytes and fibroblasts in vitro. Biomaterials 25:1289–1297. https://doi.org/10.1016/j.biomaterials.2003.08.04510.1016/j.biomaterials.2003.08.045 ↗
27. Bertran MS, Dale BE (1986) Determination of cellulose accessibility by differential scanning calorimetry. J Appl Polym Sci 32:4241–4253. https://doi.org/10.1002/app.1986.07032033510.1002/app.1986.070320335 ↗
28. Magoshi J, Magoshi Y (1975) Physical properties and structure of silk. II. Dynamic mechanical and dielectric properties of silk fibroin. J Polym Sci Polym Phys 13:1347–1351. https://doi.org/10.1002/pol.1975.18013070710.1002/pol.1975.180130707 ↗
29. Wunderlich B (2003) Reversible crystallization and the rigid–amorphous phase in semicrystalline macromolecules. Prog Polym Sci 28:383–450. https://doi.org/10.1016/S0079-6700(02)00085-010.1016/S0079-6700(02)00085-0 ↗
30. Asakura T, Yao J, Yamane T, Umemura K, Ulrich AS (2002) Heterogeneous structure of silk fibers from Bombyx mori resolved by 13C solid-state NMR spectroscopy. J Am Chem Soc 124:8794–8795. https://doi.org/10.1021/ja020244e10.1021/ja020244e ↗
31. Kimura H, Kishi S, Shoji A, Sugisawa H, Deguchi K (2000) Characteristic 1H chemical shifts of silk fibroins determined by 1H CRAMPS NMR. Macromolecules 33:9682–9687. https://doi.org/10.1021/ma001167f10.1021/ma001167f ↗
32. Asakura T, Suita K, Kameda T, Afonin S, Ulrich AS (2004) Structural role of tyrosine in Bombyx mori silk fibroin, studied by solid-state NMR and molecular mechanics on a model peptide prepared as silk I and II. Magn Reson Chem 42:258–266. https://doi.org/10.1002/mrc.133710.1002/mrc.1337 ↗
33. Asakura T et al (2005) Possible implications of serine and tyrosine residues and intermolecular interactions on the appearance of silk I structure of Bombyx mori silk fibroin-derived synthetic peptides: high-resolution 13C cross-polarization/magic-angle spinning NMR study. Biomacromol 6:468–474. https://doi.org/10.1021/bm049487k10.1021/bm049487k ↗
34. Hermans PH, Weidinger A (1948) Quantitative X-Ray investigations on the crystallinity of cellulose fibers. A background analysis. J Appl Phys 19:491–506. https://doi.org/10.1063/1.169816210.1063/1.1698162 ↗
35. Wu P et al (2013) Facile preparation of paclitaxel loaded silk fibroin nanoparticles for enhanced antitumor efficacy by locoregional drug delivery. ACS Appl Mater Interfaces 5:12638–12645. https://doi.org/10.1021/am403992b10.1021/am403992b ↗
36. Zhang Y-Q et al (2007) Formation of silk fibroin nanoparticles in water-miscible organic solvent and their characterization. J Nanopart Res 9:885–900. https://doi.org/10.1007/s11051-006-9162-x10.1007/s11051-006-9162-x ↗
37. Koperska MA et al (2014) Degradation markers of fibroin in silk through infrared spectroscopy. Polym Degrad Stab 105:185–196. https://doi.org/10.1016/j.polymdegradstab.2014.04.00810.1016/j.polymdegradstab.2014.04.008 ↗
38. Murphy AR, Kaplan DL (2009) Biomedical applications of chemically-modified silk fibroin. J Mater Chem 19:6443–6450. https://doi.org/10.1039/b905802h10.1039/b905802h ↗
39. Kemp PD, Cavallaro JF, Hastings DN (1995) Effects of carbodiimide crosslinking and load environment on the remodeling of collagen scaffolds. Tissue Eng 1:71–79. https://doi.org/10.1089/ten.1995.1.7110.1089/ten.1995.1.71 ↗
40. Hu X, Kaplan D, Cebe P (2006) Determining beta-sheet crystallinity in fibrous proteins by thermal analysis and infrared spectroscopy. Macromolecules 39:6161–6170. https://doi.org/10.1021/ma061010910.1021/ma0610109 ↗
41. Freddi G, Pessina G, Tsukada M (1999) Swelling and dissolution of silk fibroin (Bombyx mori) in N-methyl morpholine N-oxide. Int J Biol Macromol 24:251–263. https://doi.org/10.1016/S0141-8130(98)00087-710.1016/S0141-8130(98)00087-7 ↗
42. Asai M, Tsuboi M, Shimanouchi T, Mizushima S-I (1955) Infrared spectra of polypeptides and related compounds. I. J Phys Chem 59:322–325. https://doi.org/10.1021/j150526a01110.1021/j150526a011 ↗
43. Motta A, Fambri L, Migliaresi C (2002) Regenerated silk fibroin films: thermal and dynamic mechanical analysis. Macromol Chem Phys 203:1658–1665. https://doi.org/10.1002/1521-3935%28200207%29203%3A10/11%3C1658%3A%3AAID-MACP1658%3E3.0.CO%3B2-310.1002/1521-3935(200207)203:10/11<1658::AID-MACP1658>3.0.CO;2-3 ↗
44. Sashina ES, Janowska G, Zaborski M, Vnuchkin AV (2007) Compatibility of fibroin/chitosan and fibroin/cellulose blends studied by thermal analysis. J Therm Anal Calorim 89:887–891. https://doi.org/10.1007/s10973-006-7676-110.1007/s10973-006-7676-1 ↗
45. Lawrence BD et al (2010) Effect of hydration on silk film material properties. Macromol Biosci 10:393–403. https://doi.org/10.1002/mabi.20090029410.1002/mabi.200900294 ↗
46. Jin HJ, Kaplan DL (2003) Mechanism of silk processing in insects and spiders. Nature 424:1057–1061. https://doi.org/10.1038/nature0180910.1038/nature01809 ↗