{"id":183,"date":"2021-04-16T21:54:13","date_gmt":"2021-04-16T21:54:13","guid":{"rendered":"http:\/\/dlab.clemson.edu\/?p=183"},"modified":"2025-04-25T21:12:50","modified_gmt":"2025-04-25T21:12:50","slug":"interactions-between-nanomaterials-and-biomolecules-at-the-nano-bio-interface","status":"publish","type":"post","link":"https:\/\/dlab.clemson.edu\/?p=183","title":{"rendered":"Interactions between nanomaterials and biomolecules at the Nano-Bio interface"},"content":{"rendered":"\n<p>Recent advances in Nanotechnology allow sophisticated synthesis of nanomaterials with well-defined composition, aspect ratio, size, surface chemistry and functionalization. Biomedical applications of engineered nanomaterials or nanomedine include imaging, sensing, targeting, drug and gene delivery, and therapeutics in diagnosis, prognosis, and treatment of human diseases. Upon entering biological media such as the bloodstream, a nanoparticle forms molecular complexes with encountered proteins, termed as the protein corona. The protein-nanoparticle complex instead of the original nanoparticle dictates its biological identity and function. In addition, proteins in the corona can undergo conformational changes, resulting into either lost or gain of functions. Hence, understanding the structure and dynamics of a nanoparticle\u2013protein corona is essential for predicting the fate, transport, and toxicity of nanomaterials in living systems and for enabling the vast applications of nanomedicine.<\/p>\n\n\n<p><img decoding=\"async\" src=\"img\/TOC.jpeg\"><\/p>\n<p>Our group is the first to demonstrate the formation of protein-nanoparticle corona at both atomic and molecule levels in silico using multiscale discrete molecular dynamics (DMD) simulations. Computational results of the ubiquitin-silver nanoparticle (AgNP) corona agreed with high-resolution NMR experiments of the binding between ubiquitin and AgNP, the stretched exponential binding kinetics, and the secondary structure changes of ubiquitin in the corona. Over the years, we have been expanding the capability of DMD to model various types of nanomaterials ranging from carbon-based and polymeric to metal and metal oxide nanoparticles. Using DMD simulations, we have been studying the fundamental interactions between nanoparticles and biomolecules, and trying to uncover the physicochemical determinants of nanoparticles on the self-assembly of biomolecules in the corona.<\/p>\n<p>52. X. Liang, G. Huang, Y. Wang, N. Andrikopoulos, H. Tang, F. Ding*, Y. Li*, P.C. Ke*, \u201cPolystyrene Nanoplastics Hitch-Hike the Gut-Brain Axis to Exacerbate Parkinson\u2019s Pathology\u201d, ACS Nano, 19(5): 5475\u20135492 (2025) doi: 10.1021\/acsnano.4c13914<\/p>\n<p>51. A. Nandakumar, H. Tang, N. Andrikopoulos, J. F. Quinn, F. Ding,* P. C. Ke* and Y. Li*, \u201cControlling nanoparticle-induced endothelial leakiness with the protein corona\u201d, Nanoscale, 6(19):9348-9360 (2024) doi:10.1039\/D4NR01311E<\/p>\n<p>50. Y. Wang, X. Liang, N. Andrikopoulos, H. Tang, F. He, X. Yin, Y. Li, F. Ding, G. Peng, M. Mortimer, P.C. Ke, \u201cRemediation of Metal Oxide Nanotoxicity with a Functional Amyloid\u201d, Advanced Science, 11(23):2310314 (2024) doi:10.1002\/advs.202310314<\/p>\n<p>49. X. Liang, N. Andrikopoulos, H. Tang, Y. Wang, F. Ding* and P.C. Ke*, \u201cNanoplastic stimulates the amyloidogenesis of Parkinson\u2019s alpha-synuclein NACore\u201d, Small, in press (2023) doi:10.1002\/smll.202308753<\/p>\n<p>48. Andrikopoulos N., Li Y., Nandakumar A., Quinn J., Davis T., Ding F.*, Saikia N.*, Ke P.C.*, \u201cZinc-Epigallocatechin-3-gallate Network-Coated Nanocomposites against the Pathogenesis of Amyloid-Beta\u201d, ACS Applied Materials &amp; Interfaces, 15, 6, 7777\u20137792 (2023) doi:10.1021\/acsami.2c20334<\/p>\n<p>47. J. He, L. Zhou, G. Huang, J. Shen, W. Chen, C. Wang, A. Kim, Z. Zhang, W. Cheng, S. Dai, F. Ding,* and P. Chen*, \u201cEnhanced Label-Free Nanoplasmonic Cytokine Detection in SARS-CoV-2 Induced Inflammation Using Rationally Designed Peptide Aptamer\u201d, ACS Applied Materials &amp; Interfaces, 14, 43, 48464\u201348475 doi:10.1021\/acsami.2c14748 (2022)<\/p>\n<p> 46. W. Wei, Y. Li, M. Lee, N. Andrikopoulos, S. Lin, C. Chen, D. Leong, F. Ding, Y. Song, and P. Ke, \u201cAnionic Nanoplastic Exposure Induces Endothelial Leakiness\u201d, Nature Communications, 13: 4757, doi:10.1038\/s41467-022-32532-5 (2022)<\/p>\n<p> 45.  J. Ren, K. Velonia, N. Andrikopoulos, H. Tang, F. Ding, P. C. Ke, C. Chen, \u201cChemical and Biophysical Signatures of the Protein Corona in Nanomedicine\u201d, Journal of The American Chemical Society, 144(21): 9184\u20139205 (2022) doi:10.1021\/jacs.2c02277<\/p>\n<p>44.  H. Tang, Y. Li, A. Kakinen, N. Andrikopoulos, Y. Sun, E. Kwak, T. P. Davis, F. Ding* and P. C. Ke*, \u201cGraphene Quantum Dots Obstruct the Membrane Axis of Alzheimer\u2019s Amyloid Beta\u201d, Physical Chemistry Chemical Physics, 24, 86-97 (2022) doi: 10.1039\/D1CP04246G<\/p>\n<p>43. A. Nandakumar, W. Wei , G. Siddiqui, H. Tang, Y. Li , A. Kakinen, X. Wan, K. Koppel, S. Lin, T. Davis, D. Leong, D. Creek, F. Ding, Y. Song, P. C. Ke, \u201cDynamic Protein Corona of Gold Nanoparticles with An Evolving Morphology\u201d, ACS Appl. Mater. Interfaces, 13, 48, 58238\u201358251 (2021) doi: 10.1021\/acsami.1c19824<\/p>\n<p>42. M. Lee,\u2020 N. Ni,\u2020 H. Tang,\u2020 Y. Li,\u2020 W. Wei, A. Kakinen, X. Wan, T. P. Davis, Y. Song,* D. T. Leong,* F. Ding* and P. C. Ke*, \u201cA Framework of Paracellular Transport via Nanoparticles-Induced Endothelial Leakiness\u201d, Advanced Science, 2102519 (2021) doi:10.1002\/advs.202102519<\/p>\n<p>41. &nbsp;H. Tang, Y. Li, A. Kakinen, N. Andrikopoulos, Y. Sun, E. Kwak, T. P. Davis, F. Ding* and P. C. Ke*, \u201cGraphene Quantum Dots Obstruct the Membrane Axis of Alzheimer\u2019s Amyloid Beta\u201d, Physical Chemistry Chemical Physics, in press (2021)&nbsp;<a href=\"https:\/\/pubs.rsc.org\/en\/content\/articlelanding\/2021\/CP\/D1CP04246G#!divAbstract\">doi: 10.1039\/D1CP04246G<\/a><\/p>\n<p>40. A. Nandakumar, W. Wei , G. Siddiqui, H. Tang, Y. Li , A. Kakinen, X. Wan, K. Koppel, S. Lin, T. Davis, D. Leong, D. Creek, F. Ding, Y. Song, P. C. Ke, \u201cDynamic Protein Corona of Gold Nanoparticles with An Evolving Morphology\u201d, ACS Appl. Mater. Interfaces, in press (2021)&nbsp;<a href=\"https:\/\/pubs.acs.org\/doi\/full\/10.1021\/acsami.1c19824\">doi: 10.1021\/acsami.1c19824<\/a><\/p>\n<p>39. M. Lee,\u2020 N. Ni,\u2020 H. Tang,\u2020 Y. Li,\u2020 W. Wei, A. Kakinen, X. Wan, T. P. Davis, Y. Song,* D. T. Leong,* F. Ding* and P. C. Ke*, \u201cA Framework of Paracellular Transport via Nanoparticles-Induced Endothelial Leakiness\u201d, Advanced Science, 2102519 (2021)&nbsp;<a href=\"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/advs.202102519\">doi:10.1002\/advs.202102519<\/a><\/p>\n<p>38. N. Andrikopoulos, Z. Song, X. Wan, A. Douek, I. Javed, C. Fu, X. Changkui, Y. Xing, F. Xin, Y. Li, A. Kakinen, K. Koppel, R. Qiao, A. Whittaker, J. Kaslin, T. Davis*, Y. Song*, F. Ding*, P.C. Ke*, \u201cInhibition of Amyloid Aggregation and Toxicity with Janus Iron Oxide Nanoparticles\u201d, Chem. Mater., 33, 16, 6484\u20136500 (2021)&nbsp;<a href=\"https:\/\/pubs.acs.org\/doi\/abs\/10.1021\/acs.chemmater.1c01947\">doi: 10.1021\/acs.chemmater.1c01947<\/a><\/p>\n<p>37. Y. Li, H. Tang, H. Zhu, A. Kakinen, D. Wang, N. Andrikopoulos, Y. Sun, A. Nandakumar, E. Kwak, T. Davis, D. Leong, F. Ding, P. C. Ke, \u201cUltrasmall Molybdenum Disulfide Quantum Dots Cage Alzheimer\u2019s Amyloid Beta to Restore Membrane Fluidity\u201d, ACS Appl. Mater. Interfaces, 13(25): 29936\u201329948 (2021)&nbsp;<a href=\"https:\/\/pubs.acs.org\/doi\/full\/10.1021\/acsami.1c06478\">doi: 10.1021\/acsami.1c06478<\/a><\/p>\n<p>36. Chen P, Ding F, Cai R, Javed I, Yang W, Zhang Z, Li Y, Davis TP, Ke PC, Chen C., \u201cAmyloidosis Inhibition, a New Frontier of the Protein Corona\u201d, Nano Today, 35:100937 (2020)&nbsp;<a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S1748013220301067\">doi: 10.1016\/j.nantod.2020.100937<\/a><\/p>\n<p>35. Koppel K, Tang H, Javed I, Parsa M, Mortimer M, Davis TP, Lin S, Chaffee AL, Ding F and Ke P, \u201cElevated Amyloidoses of Human IAPP and Amyloid Beta by Lipopolysaccharide and Their Mitigation by Carbon Quantum Dots\u201d, Nanoscale, in press (2020)<\/p>\n<p>34. Y. Xing, Y. Sun, B. Wang, &amp; F. Ding, \u201cMorphological Determinants of Carbon Nanomaterial-Induced Amyloid Peptide Self-Assembly\u201d, Frontiers in Chemistry, in press (2020)<\/p>\n<p>33. Z Huma,I Javed, Z Zhang, H Bilal, Y Sun, SZ Hussain, TP Davis, DE Otzen, CB Landersdorfer, F Ding, I Hussain and PC Ke, \u201cNano Silver Mitigates Biofilm Formation via FapC Amyloidosis Inhibition\u201d, Small, 1906674-1906683 (2019) DOI: 10.1002\/smll.201906674<\/p>\n<p>32. A Faridi, Y Sun, M Mortimer, RR Aranha, A Nandakumar, Y Li, I Javed, A Kakinen, Q Fan, AW Purcell, TP Davis,* F Ding,* P Faridi,* and P Ke*, \u201cGraphene quantum dots rescue protein dysregulation of pancreatic \u03b2-cells exposed to human islet amyloid polypeptide\u201d, Nano Research, in press (2019)<\/p>\n<p>31. I Javed, G Peng, Y Xing, T Yu, M Zhao, A Kakinen, A Faridi, CL Parish, F Ding*, TP Davis*, P Ke* and S Lin*, \u201cInhibition of Amyloid Beta Toxicity in Zebrafish with A Chaperone-Gold Nanoparticle Dual Strategy\u201d, Nature Commun, in press (2019)<\/p>\n<p>30. Y. Sun, A. Kakinen, C. Zhang, Y. Yang, A. Faridi, T. P. Davis, W. Cao, P. C. Ke and F. Ding, \u201cAmphiphilic Surface Chemistry of Fullerenols Is Necessary for Inhibiting the Amyloid Aggregation of Alpha-Synuclein NACore\u201d, Nanoscale, in press, (2019)<\/p>\n<p>29. P. C. Ke, E. H. Pilkington, Y. Sun, I. Javed, A. Kakinen, G. Peng, F. Ding, . P. Davisa, \u201cMitigation of Amyloidosis with Nanomaterials\u201d, Advanced Materials, in press, (2019)<\/p>\n<p>28. M. Wang, Y. Sun, X. Cao, G. Peng, I. Javed, A. Kakinen, T.P. Davis, S. Lin, J. Liu, F. Ding, and P. Ke, \u201cGraphene Quantum Dots against Human IAPP Aggregation and Toxicity in Vivo\u201d, Nanoscale 10, 19995, <a href=\"https:\/\/pubs.rsc.org\/en\/Content\/ArticleLanding\/2018\/NR\/C8NR07180B?utm_source=feedburner&amp;utm_medium=feed&amp;utm_campaign=Feed%3A+rss%2FNR+%28RSC+-+Nanoscale+latest+articles%29#!divAbstract\">DOI: 10.1039\/C8NR07180B <\/a> (2018)<\/p>\n<p>27. A. Faridi,Y. Sun, Y. Okazaki, G. Peng, J. Gao, A. Kakinen, P. Faridi, M. Zhao, I. Javed, A.W. Purcell, T.P. Davis, S. Lin, R. Oda, F. Ding, P. Ke, \u201cMitigating Human IAPP Amyloidogenesis in Vivo with Chiral Silica Nanoribbons\u201d, Small, 14, 1802825, <a href=\"https:\/\/onlinelibrary.wiley.com\/doi\/full\/10.1002\/smll.201802825\">DOI: 10.1002\/smll.201802825 <\/a>(2018)<\/p>\n<p>26. B. Wang, Y. Sun, T. Davis, P.C. Ke, Y. Wu, and F. Ding, \u201cUnderstanding the Effects of PAMAM Dendrimer Size and Surface Chemistry on Serum Protein Binding with Discrete Molecular Dynamics Simulations\u201d, ACS Sustainable Chemistry &amp; Engineering, 6 (9),11704\u201311715, <a href=\"https:\/\/pubs.acs.org\/doi\/10.1021\/acssuschemeng.8b01959\">DOI: 10.1021\/acssuschemeng.8b01959 <\/a>, (2018)<\/p>\n<p>25. Pilkington E.P., Gustafsson O.J.R., Xing Y., Hernandez-Fernaud J., Zampronio C., Kakinen A., Faridi A., Ding F., Wilson P., Ke P.C. and Davis T.P., \u201cProfiling the Serum Protein Corona of Fibrillar Human Islet Amyloid Polypeptide\u201d, ACS Nano, 12, 6066\u22126078 (2018) <a href=\"https:\/\/pubs.acs.org\/doi\/10.1021\/acsnano.8b02346\">DOI: 10.1021\/acsnano.8b02346<\/a><br>-Featured as Journal Front <a href=\"https:\/\/pubs.acs.org\/subscribe\/covers\/ancac3\/ancac3_v012i006.jpg?0.5236079398209994\">Cover <\/a>.<\/p>\n<p>24. A. Kakinen, J. Adamcik, B. Wang, X. Ge, R. Mezzenga, T.P. Davis, F. Ding, and P. Ke, \u201cNanoscale inhibition of polymorphic and ambidextrous IAPP amyloid aggregation with small molecules\u201d, Nano Research, 11(7): 3636\u20133647 (2017)<a href=\"Papers\/kawgmddk-2017.pdf\">[download]<\/a>DOI: 10.1007\/s12274-017-1930-7<\/p>\n<p>23. I. Javed, Y. Sun, J. Adamcik, B. Wang, A. Kakinen, E. Pilkington, F. Ding, R. Mezzenga, T. Davis, Thomas; P. Ke, \u201cCo-fibrillization of pathogenic and functional amyloid proteins with gold nanoparticles against amyloidogenesis\u201d, Biomacromolecules, in press (2017) DOI: 10.1021\/acs.biomac.7b01359<\/p>\n<p>22. E. Pilkington, M. Lai, X. Ge, W. Stanley, B. Wang, M. Wang, A. Kakinen, M. Sani, M. Whittaker, E. Gurzov, F. Ding, J. Quinn, T. Davis, P. Ke, \u201cStar Polymers Reduce IAPP Toxicity via Accelerated Amyloid Aggregation\u201d, Biomacromolecules, in press (2017)<\/p>\n<p>21. J. Yang, B. Wang, Y. You, W. Chang, K. Tang, Y. Wang, W. Zhang, F. Ding, S. Gunasekaran, \u201cProbing the modulated formation of gold nanoparticle-beta lactoglobulin corona complexes and its applications\u201d, Nanoscale, in press (2017) <a href=\"http:\/\/pubs.rsc.org\/en\/content\/articlelanding\/2017\/nr\/c7nr02999c\">[link]<\/a><\/p>\n<p>20. B. Wang, E.H. Pilkington, Y. Sun, T.P. Davis, P.C. Ke and F. Ding, Modulating protein amyloid aggregation with nanomaterials, Environmental Science Nano, in press (2017)<\/p>\n<p>19. N.K. Geitner, W. Zhao, F. Ding, W. Chen, M. R. Wiesner, \u201cMechanistic Insights from Discrete Molecular Dynamics Simulations of PesticideNanoparticle Interactions\u201d, Environmental Science &amp; Technology, in press (2017) <a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/acs.est.7b01674\">[link]<\/a><\/p>\n<p>18. S. Lin, M. Mortimer, R. Chen, A. Kakinen, J.E. Riviere, T.P. Davis, F. Ding,* and P. C. Ke*, \u201cNanoEHS beyond Toxicity \u2013 Focusing on Biocorona\u201d, Env. Sci. Nano, in press (2017)<a href=\"http:\/\/pubs.rsc.org\/en\/Content\/ArticleLanding\/2017\/EN\/C6EN00579A#!divAbstract\"> [link]<\/a><\/p>\n<p>17. Pilkington E.H., Xing Y., Wang B., Kakinen A., Wang M., Davis T.P., Ding F., Ke P.C., \u201cEffects of Protein Corona on IAPP Amyloid Aggregation, Fibril Remodelling, and Cytotoxicity\u201d, Scientific Reports, in press (2017)<\/p>\n<p>16. B. Wang,T. Blin, A. K\u00e4kinen, X. Ge, E.H. Pilkington, J.F. Quinn, M.R. Whittaker, T.P. Davis, P.C. Ke and F. Ding, \u201cBrushed polyethylene glycol and phosphorylcholine for grafting nanoparticles against protein binding\u201d, Polymer Chemistry, in press (2016)<\/p>\n<p>15. T. Blin, A. Kakinen, E.H. Pilkington, A. Ivask, F. Ding, J.F. Quinn. M.R. Whittaker, P.C. Ke and T.P. Davis, \u201cSynthesis and In Vitro Properties of Iron Oxide Nanoparticles Grafted with Brushed Phosphorylcholine and Polyethylene Glycol\u201d, Polymer Chemistry, in press (2016)<\/p>\n<p>14. E.N. Gurzov, B. Wang, E.H. Pilkington, P. Chen,A. Kakinen, W.J. Stanley, S.A. Litwak, E.G. Hanssen,T.P. Davis, F. Ding, and P.Chun Ke, \u201cInhibition of hIAPP Amyloid Aggregation and Pancreatic \u03b2-cell Toxicity by OH-terminated PAMAM Dendrimer\u201d, Small, in press (2016)<\/p>\n<p>13. S. Radic, T.P. Davis, P.C. Ke and F. Ding, \u201cContrasting effects of nanoparticle-protein attraction on amyloid aggregation\u201d, RSC Advances, in press (2015)<\/p>\n<p>12. P. Nedumpully-Govindan, E.N. Gurzov, P. Chen, E.H. Pilkington, W.J. Stanley, S.A. Litwak, T.P. Davis, P.C. Ke, and F. Ding, \u201cGraphene Oxide Inhibits hIAPP Amyloid Fibrillation and Toxicity in Insulin-Producing NIT-1 Cells\u201d, PCCP, in press (2015)<\/p>\n<p>11. Wang B, Geitner NK, Davis TP, Ke PC, Ladner DL and Ding F, \u201cDeviation from the Unimolecular Micelle Paradigm of PAMAM Dendrimers Induced by Strong Inter-Ligand Interactions\u201d, Journal of Physical Chemistry C, in press (2015)<\/p>\n<p>10. Ge XW, Ke PC, Davis TP and Ding F, \u201cA Thermodynamics Model for the Emergence of a Stripe-like Binary SAM on a Nanoparticle Surface\u201d, Small, in press (2015)<\/p>\n<p>9. DeFever R., Geitner N., Bhattacharya P., Ding F., Ke P.C., Sarupria S., \u201cPAMAM dendrimers and graphene: Materials for removing aromatic contaminants from water\u201d, Environmental Science &amp; Technology, in press (2015)<\/p>\n<p>8. Geitner N., Wang B., Andorfer R.; Ladner D.; Ke P.K.; Ding F., \u201cThe structure-function relationship of PAMAM dendrimers as robust oil dispersants\u201d, Environmental Science &amp; Technology, 48(21):12868-75, (2014)<\/p>\n<p>7. Wang B., Seabrook S.A., Nedumpully-Govindan P., Chen P., Yin H., Waddington L., Epa V.C., Winkler D.A., Kirby J.K., Ding F., Ke P.C., \u201cThermostability and Reversibility of Silver Nanoparticle-Protein Binding\u201d, Physical Chemistry Chemical Physics, in press (2014)<\/p>\n<p>6. S. Radic, P. Nedumpully-Govindan,R. Chen, E. Salonen, J.M. Brown, P.C. Ke, and F. Ding, \u201cEffect of Fullerenol Surface Chemistry on Nanoparticle Binding-induced Protein Misfolding\u201d, Nanoscale, in press (2014)<\/p>\n<p>5. Y. Wen, N.K. Geitner, R. Chen, F. Ding, P. Chen, R.E. Andorfer, P.N. Govindan, and P.C. Ke, Binding of Cytoskeletal Proteins with Silver Nanoparticles, RSC Adcances, in press, (2013).<\/p>\n<p>4.&nbsp;EE. Salonen, F. Ding, and P.C. Ke, \u201cFate, behavior and biophysical modeling of nanoparticles in living systems\u201d in \u201cEngineered Nanoparticles and the Environment: Biophysicochemical Processes and Toxicity\u201d, Edited by B. Xing, C.D. Vecitis, &amp; N. Senesi, Wiley-IUPAC (2016) <a href=\"Papers\/c15.pdf\">[download]<\/a><\/p>\n<p>3. A. Kakinen, F. Ding, P. Chen, A. Kahru*, and P.C. Ke, \u201cInteraction of Silver Nanoparticles and Firefly Luciferase and Its Impact on Enzyme Luminescence\u201d, <em> Nanotechnology, in press. (2013)<\/em><\/p>\n<p>2. S. Radic, N. Geitner, R. Podila, A. Kakinen, P. Chen, P.C. Ke*, and F. Ding*, \u201cCompetitive Binding of Natural Amphiphiles with Graphene Derivatives\u201d, <em> Scientific Reports, in press. (2013)<\/em><\/p>\n<p>1. F. Ding*, S. Radic, R. Chen, P. Chen, J.M. Brown and P.C. Ke*, \u201cDirect observation of silver nanoparticle-ubiquitin corona formation\u201d, <em>Nanoscale, in press <\/em> (2012)<\/p>","protected":false},"excerpt":{"rendered":"<p>Recent advances in Nanotechnology allow sophisticated synthesis of nanomaterials with well-defined composition, aspect ratio, size, surface chemistry and functionalization. Biomedical applications of engineered nanomaterials or nanomedine include imaging, sensing, targeting, drug and gene delivery, and therapeutics in diagnosis, prognosis, and treatment of human diseases. Upon entering biological media such as the bloodstream, a nanoparticle forms &hellip; <\/p>\n<p><a class=\"more-link btn\" href=\"https:\/\/dlab.clemson.edu\/?p=183\">Continue reading<\/a><\/p>\n","protected":false},"author":1,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[4,2],"tags":[6,5],"class_list":["post-183","post","type-post","status-publish","format-standard","hentry","category-education","category-research","tag-education","tag-research","nodate","item-wrap"],"_links":{"self":[{"href":"https:\/\/dlab.clemson.edu\/index.php?rest_route=\/wp\/v2\/posts\/183","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/dlab.clemson.edu\/index.php?rest_route=\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/dlab.clemson.edu\/index.php?rest_route=\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/dlab.clemson.edu\/index.php?rest_route=\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/dlab.clemson.edu\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=183"}],"version-history":[{"count":21,"href":"https:\/\/dlab.clemson.edu\/index.php?rest_route=\/wp\/v2\/posts\/183\/revisions"}],"predecessor-version":[{"id":900,"href":"https:\/\/dlab.clemson.edu\/index.php?rest_route=\/wp\/v2\/posts\/183\/revisions\/900"}],"wp:attachment":[{"href":"https:\/\/dlab.clemson.edu\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=183"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/dlab.clemson.edu\/index.php?rest_route=%2Fwp%2Fv2%2Fcategories&post=183"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/dlab.clemson.edu\/index.php?rest_route=%2Fwp%2Fv2%2Ftags&post=183"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}