The University of Queensland

Endothelial leakiness elicited by amyloid protein aggregation

Li, Yuhuan, Ni, Nengyi, Lee, Myeongsang, Wei, Wei, Andrikopoulos, Nicholas, Kakinen, Aleksandr, Davis, Thomas P., Song, Yang, Ding, Feng, Leong, David Tai and Ke, Pu Chun (2024). Endothelial leakiness elicited by amyloid protein aggregation. Nature Communications, 15 (1) 613, 613. doi: 10.1038/s41467-024-44814-1

Alzheimer's progenitor amyloid‐β targets and dissolves microbial amyloids and impairs biofilm function

Ali, Syed Aoun, Chung, Ka Hang Karen, Forgham, Helen, Olsen, William P., Kakinen, Aleksandr, Balaji, Arunpandian, Otzen, Daniel E., Davis, Thomas Paul and Javed, Ibrahim (2023). Alzheimer's progenitor amyloid‐β targets and dissolves microbial amyloids and impairs biofilm function. Advanced Science, 10 (29) 2301423, e2301423. doi: 10.1002/advs.202301423

Keeping up with the COVID's—Could siRNA‐based antivirals be a part of the answer?

Forgham, Helen, Kakinen, Aleksandr, Qiao, Ruirui and Davis, Thomas P. (2022). Keeping up with the COVID's—Could siRNA‐based antivirals be a part of the answer?. Exploration, 00 (6) 20220012, 20220012. doi: 10.1002/exp.20220012

Graphene quantum dots obstruct the membrane axis of Alzheimer's amyloid beta

Tang, Huayuan, Li, Yuhuan, Kakinen, Aleksandr, Andrikopoulos, Nicholas, Sun, Yunxiang, Kwak, Eunbi, Davis, Thomas P., Ding, Feng and Ke, Pu Chun (2022). Graphene quantum dots obstruct the membrane axis of Alzheimer's amyloid beta. Physical Chemistry Chemical Physics, 24 (1), 86-97. doi: 10.1039/d1cp04246g

Dynamic protein corona of gold nanoparticles with an evolving morphology

Nandakumar, Aparna, Wei, Wei, Siddiqui, Ghizal, Tang, Huayuan, Li, Yuhuan, Kakinen, Aleksandr, Wan, Xulin, Koppel, Kairi, Lin, Sijie, Davis, Thomas P., Leong, David T., Creek, Darren J., Ding, Feng, Song, Yang and Ke, Pu Chun (2021). Dynamic protein corona of gold nanoparticles with an evolving morphology. ACS Applied Materials and Interfaces, 13 (48), 58238-58251. doi: 10.1021/acsami.1c19824

Structure dependent differential modulation of Aβ fibrillization by selenadiazole-based inhibitors

Kalsoom, Umme, Alazmi, Meshari, Farrukh, Hafiz Syed Usama Bin, Chung, Ka Hang Karen, Alshammari, Nawaf, Kakinen, Aleksandr, Chotana, Ghayoor Abbas, Javed, Ibrahim, Davis, Thomas Paul and Saleem, Rahman Shah Zaib (2021). Structure dependent differential modulation of Aβ fibrillization by selenadiazole-based inhibitors. ACS Chemical Neuroscience, 12 (20), 3806-3817. doi: 10.1021/acschemneuro.1c00478

A framework of paracellular transport via nanoparticles‐induced endothelial leakiness

Lee, Myeongsang, Ni, Nengyi, Tang, Huayuan, Li, Yuhuan, Wei, Wei, Kakinen, Aleksandr, Wan, Xulin, Davis, Thomas P., Song, Yang, Leong, David Tai, Ding, Feng and Ke, Pu Chun (2021). A framework of paracellular transport via nanoparticles‐induced endothelial leakiness. Advanced Science, 8 (21) 2102519, e2102519. doi: 10.1002/advs.202102519

Inhibition of amyloid aggregation and toxicity with Janus iron oxide nanoparticles

Andrikopoulos, Nicholas, Song, Zhiyuan, Wan, Xulin, Douek, Alon M., Javed, Ibrahim, Fu, Changkui, Xing, Yanting, Xin, Fangyun, Li, Yuhuan, Kakinen, Aleksandr, Koppel, Kairi, Qiao, Ruirui, Whittaker, Andrew K., Kaslin, Jan, Davis, Thomas P., Song, Yang, Ding, Feng and Ke, Pu Chun (2021). Inhibition of amyloid aggregation and toxicity with Janus iron oxide nanoparticles. Chemistry of Materials, 33 (16) acs.chemmater.1c01947, 6484-6500. doi: 10.1021/acs.chemmater.1c01947

Nanotoxicology and nanomedicine: The Yin and Yang of nano-bio interactions for the new decade

Bondarenko, Olesja, Mortimer, Monika, Kahru, Anne, Feliu, Neus, Javed, Ibrahim, Kakinen, Aleksandr, Lin, Sijie, Xia, Tian, Song, Yang, Davis, Thomas P., Lynch, Iseult, Parak, Wolfgang J., Leong, David Tai, Ke, Pu Chun, Chen, Chunying and Zhao, Yuliang (2021). Nanotoxicology and nanomedicine: The Yin and Yang of nano-bio interactions for the new decade. Nano Today, 39 101184, 101184. doi: 10.1016/j.nantod.2021.101184

Ultrasmall molybdenum disulfide quantum dots cage Alzheimer’s amyloid beta to restore membrane fluidity

Li, Yuhuan, Tang, Huayuan, Zhu, Houjuan, Kakinen, Aleksandr, Wang, Di, Andrikopoulos, Nicholas, Sun, Yunxiang, Nandakumar, Aparna, Kwak, Eunbi, Davis, Thomas P., Leong, David Tai, Ding, Feng and Ke, Pu Chun (2021). Ultrasmall molybdenum disulfide quantum dots cage Alzheimer’s amyloid beta to restore membrane fluidity. ACS Applied Materials and Interfaces, 13 (25) acsami.1c06478, 29936-29948. doi: 10.1021/acsami.1c06478

Spontaneous formation of β-sheet nano-barrels during the early aggregation of Alzheimer’s amyloid beta

Sun, Yunxiang, Kakinen, Aleksandr, Wan, Xulin, Moriarty, Niamh, Hunt, Cameron P.J., Li, Yuhuan, Andrikopoulos, Nicholas, Nandakumar, Aparna, Davis, Thomas P., Parish, Clare L., Song, Yang, Ke, Pu Chun and Ding, Feng (2021). Spontaneous formation of β-sheet nano-barrels during the early aggregation of Alzheimer’s amyloid beta. Nano Today, 38 101125, 101125. doi: 10.1016/j.nantod.2021.101125

In vitro and in vivo models for anti-amyloidosis nanomedicines

Kakinen, Aleksandr, Javed, Ibrahim, Davis, Thomas P. and Ke, Pu Chun (2021). In vitro and in vivo models for anti-amyloidosis nanomedicines. Nanoscale Horizons, 6 (2), 95-119. doi: 10.1039/d0nh00548g

Amyloid aggregation under the lens of liquid–liquid phase separation

Xing, Yanting, Nandakumar, Aparna, Kakinen, Aleksandr, Sun, Yunxiang, Davis, Thomas P., Ke, Pu Chun and Ding, Feng (2020). Amyloid aggregation under the lens of liquid–liquid phase separation. The Journal of Physical Chemistry Letters, 12 (1), 368-378. doi: 10.1021/acs.jpclett.0c02567

The membrane axis of Alzheimer's nanomedicine

Li, Yuhuan, Tang, Huayuan, Andrikopoulos, Nicholas, Javed, Ibrahim, Cecchetto, Luca, Nandakumar, Aparna, Kakinen, Aleksandr, Davis, Thomas P., Ding, Feng and Ke, Pu Chun (2020). The membrane axis of Alzheimer's nanomedicine. Advanced NanoBiomed Research, 1 (1), 2000040. doi: 10.1002/anbr.202000040

Human plasma protein corona of Aβ amyloid and its impact on islet amyloid polypeptide cross-seeding

Nandakumar, Aparna, Xing, Yanting, Aranha, Ritchlynn R., Faridi, Ava, Kakinen, Aleksandr, Javed, Ibrahim, Koppel, Kairi, Pilkington, Emily H., Purcell, Anthony Wayne, Davis, Thomas P., Faridi, Pouya, Ding, Feng and Ke, Pu Chun (2020). Human plasma protein corona of Aβ amyloid and its impact on islet amyloid polypeptide cross-seeding. Biomacromolecules, 21 (2), 988-998. doi: 10.1021/acs.biomac.9b01650

Single-Molecular Heteroamyloidosis of Human Islet Amyloid Polypeptide

Kakinen, Aleksandr, Xing, Yanting, Hegoda Arachchi, Nuwan, Javed, Ibrahim, Feng, Lei, Faridi, Ava, Douek, Alon M., Sun, Yunxiang, Kaslin, Jan, Davis, Thomas P., Higgins, Michael J., Ding, Feng and Ke, Pu Chun (2019). Single-Molecular Heteroamyloidosis of Human Islet Amyloid Polypeptide. Nano Letters, 19 (9), 6535-6546. doi: 10.1021/acs.nanolett.9b02771

Inhibition of amyloid beta toxicity in zebrafish with a chaperone-gold nanoparticle dual strategy

Javed, Ibrahim, Peng, Guotao, Xing, Yanting, Yu, Tianyu, Zhao, Mei, Kakinen, Aleksandr, Faridi, Ava, Parish, Clare L., Ding, Feng, Davis, Thomas P., Ke, Pu Chun and Lin, Sijie (2019). Inhibition of amyloid beta toxicity in zebrafish with a chaperone-gold nanoparticle dual strategy. Nature Communications, 10 (1) 3780, 3780. doi: 10.1038/s41467-019-11762-0

Amphiphilic surface chemistry of fullerenols is necessary for inhibiting the amyloid aggregation of alpha-synuclein NACore

Sun, Yunxiang, Kakinen, Aleksandr, Zhang, Chi, Yang, Ye, Faridi, Ava, Davis, Thomas P., Cao, Weiguo, Ke, Pu Chun and Ding, Feng (2019). Amphiphilic surface chemistry of fullerenols is necessary for inhibiting the amyloid aggregation of alpha-synuclein NACore. Nanoscale, 11 (24), 11933-11945. doi: 10.1039/c9nr02407g

Mitigation of amyloidosis with nanomaterials

Ke, Pu Chun, Pilkington, Emily H., Sun, Yunxiang, Javed, Ibrahim, Kakinen, Aleksandr, Peng, Guotao, Ding, Feng and Davis, Thomas P. (2019). Mitigation of amyloidosis with nanomaterials. Advanced Materials, 32 (18) 1901690, 1901690. doi: 10.1002/adma.201901690

Amyloid self-assembly of hIAPP8-20 via the accumulation of helical oligomers, α-helix to β-sheet transition, and formation of β-barrel intermediates

Sun, Yunxiang, Kakinen, Aleksandr, Xing, Yanting, Faridi, Pouya, Nandakumar, Aparna, Purcell, Anthony W., Davis, Thomas P., Ke, Pu Chun and Ding, Feng (2019). Amyloid self-assembly of hIAPP8-20 via the accumulation of helical oligomers, α-helix to β-sheet transition, and formation of β-barrel intermediates. Small, 15 (18) 1805166, 1805166. doi: 10.1002/smll.201805166

Probing the aggregation and immune response of human islet amyloid polypeptides with ligand-stabilized gold nanoparticles

Javed, Ibrahim, He, Jiacheng, Kakinen, Aleksandr, Faridi, Ava, Yang, Wen, Davis, Thomas P., Ke, Pu Chun and Chen, Pengyu (2019). Probing the aggregation and immune response of human islet amyloid polypeptides with ligand-stabilized gold nanoparticles. ACS Applied Materials and Interfaces, 11 (11), 10462-10471. doi: 10.1021/acsami.8b19506

Nucleation of β-rich oligomers and β-barrels in the early aggregation of human islet amyloid polypeptide

Sun, Yunxiang, Kakinen, Aleksandr, Xing, Yanting, Pilkington, Emily H., Davis, Thomas P., Ke, Pu Chun and Ding, Feng (2019). Nucleation of β-rich oligomers and β-barrels in the early aggregation of human islet amyloid polypeptide. Biochimica et Biophysica Acta - Molecular Basis of Disease, 1865 (2), 434-444. doi: 10.1016/j.bbadis.2018.11.021

Physical and toxicological profiles of human IAPP amyloids and plaques

Kakinen, Aleksandr, Sun, Yunxiang, Javed, Ibrahim, Faridi, Ava, Pilkington, Emily H., Faridi, Pouya, Purcell, Anthony W., Zhou, Ruhong, Ding, Feng, Lin, Sijie, Ke, Pu Chun and Davis, Thomas P. (2019). Physical and toxicological profiles of human IAPP amyloids and plaques. Science Bulletin, 64 (1), 26-35. doi: 10.1016/j.scib.2018.11.012

Graphene quantum dots rescue protein dysregulation of pancreatic β-cells exposed to human islet amyloid polypeptide

Faridi, Ava, Sun, Yunxiang, Mortimer, Monika, Aranha, Ritchlynn R., Nandakumar, Aparna, Li, Yuhuan, Javed, Ibrahim, Kakinen, Aleksandr, Fan, Qingqing, Purcell, Anthony W., Davis, Thomas P., Ding, Feng, Faridi, Pouya and Ke, Pu Chun (2019). Graphene quantum dots rescue protein dysregulation of pancreatic β-cells exposed to human islet amyloid polypeptide. Nano Research, 12 (11), 2827-2834. doi: 10.1007/s12274-019-2520-7

Mitigating human IAPP amyloidogenesis in vivo with chiral silica nanoribbons

Faridi, Ava, Sun, Yunxiang, Okazaki, Yutaka, Peng, Guotao, Gao, Jie, Kakinen, Aleksandr, Faridi, Pouya, Zhao, Mei, Javed, Ibrahim, Purcell, Anthony W., Davis, Thomas P., Lin, Sijie, Oda, Reiko, Ding, Feng and Ke, Pu Chun (2018). Mitigating human IAPP amyloidogenesis in vivo with chiral silica nanoribbons. Small, 14 (47) 1802825, 1802825. doi: 10.1002/smll.201802825

In vivo mitigation of amyloidogenesis through functional–pathogenic double-protein coronae

Javed, Ibrahim, Yu, Tianyu, Peng, Guotao, Sánchez-Ferrer, Antoni, Faridi, Ava, Kakinen, Aleksandr, Zhao, Mei, Mezzenga, Raffaele, Davis, Thomas P., Lin, Sijie and Ke, Pu Chun (2018). In vivo mitigation of amyloidogenesis through functional–pathogenic double-protein coronae. Nano Letters, 18 (9), 5797-5804. doi: 10.1021/acs.nanolett.8b02446

Serum albumin impedes the amyloid aggregation and hemolysis of human islet amyloid polypeptide and alpha synuclein

Kakinen, Aleksandr, Javed, Ibrahim, Faridi, Ava, Davis, Thomas P. and Ke, Pu Chun (2018). Serum albumin impedes the amyloid aggregation and hemolysis of human islet amyloid polypeptide and alpha synuclein. Biochimica Et Biophysica Acta-Biomembranes, 1860 (9), 1803-1809. doi: 10.1016/j.bbamem.2018.01.015

Nanoscale inhibition of polymorphic and ambidextrous IAPP amyloid aggregation with small molecules

Kakinen, Aleksandr, Adamcik, Jozef, Wang, Bo, Ge, Xinwei, Mezzenga, Raffaele, Davis, Thomas P., Ding, Feng and Ke, Pu Chun (2018). Nanoscale inhibition of polymorphic and ambidextrous IAPP amyloid aggregation with small molecules. Nano Research, 11 (7), 3636-3647. doi: 10.1007/s12274-017-1930-7

Profiling the serum protein corona of fibrillar human islet amyloid polypeptide

Pilkington, Emily H., Gustafsson, Ove J. R., Xing, Yanting, Hernandez-Fernaud, Juan, Zampronio, Cleidi, Kakinen, Aleksandr, Faridi, Ava, Ding, Feng, Wilson, Paul, Ke, Pu Chun and Davis, Thomas P. (2018). Profiling the serum protein corona of fibrillar human islet amyloid polypeptide. ACS Nano, 12 (6), 6066-6078. doi: 10.1021/acsnano.8b02346

Uptake and transcytosis of functionalized superparamagnetic iron oxide nanoparticles in an in vitro blood brain barrier model

Ivask, Angela, Pilkington, Emily H., Blin, Thomas, Käkinen, Aleksandr, Vija, Heiki, Visnapuu, Meeri, Quinn, John F., Whittaker, Michael R., Qiao, Ruirui, Davis, Thomas P., Ke, Pu Chun and Voelcker, Nicolas H. (2018). Uptake and transcytosis of functionalized superparamagnetic iron oxide nanoparticles in an in vitro blood brain barrier model. Biomaterials Science, 6 (2), 314-323. doi: 10.1039/c7bm01012e

Graphene quantum dots against human IAPP aggregation and toxicity in vivo

Wang, Miaoyi, Sun, Yunxiang, Cao, Xueying, Peng, Guotao, Javed, Ibrahim, Kakinen, Aleksandr, Davis, Thomas P., Lin, Sijie, Liu, Jingquan, Ding, Feng and Ke, Pu Chun (2018). Graphene quantum dots against human IAPP aggregation and toxicity in vivo. Nanoscale, 10 (42), 19995-20006. doi: 10.1039/c8nr07180b

Nanoparticle–proteome in vitro and in vivo

Wang, Miaoyi, Gustafsson, Ove J. R., Pilkington, Emily H., Kakinen, Aleksandr, Javed, Ibrahim, Faridi, Ava, Davis, Thomas P. and Ke, Pu Chun (2018). Nanoparticle–proteome in vitro and in vivo. Journal of Materials Chemistry B, 6 (38), 6026-6041. doi: 10.1039/c8tb01634h

Cofibrillization of pathogenic and functional amyloid proteins with gold nanoparticles against amyloidogenesis

Javed, Ibrahim, Sun, Yunxiang, Adamcik, Jozef, Wang, Bo, Kakinen, Aleksandr, Pilkington, Emily H., Ding, Feng, Mezzenga, Raffaele, Davis, Thomas P. and Ke, Pu Chun (2017). Cofibrillization of pathogenic and functional amyloid proteins with gold nanoparticles against amyloidogenesis. Biomacromolecules, 18 (12), 4316-4322. doi: 10.1021/acs.biomac.7b01359

Lysophosphatidylcholine modulates the aggregation of human islet amyloid polypeptide

Xing, Yanting, Pilkington, Emily H., Wang, Miaoyi, Nowell, Cameron J., Kakinen, Aleksandr, Sun, Yunxiang, Wang, Bo, Davis, Thomas P., Ding, Feng and Ke, Pu Chun (2017). Lysophosphatidylcholine modulates the aggregation of human islet amyloid polypeptide. Physical Chemistry Chemical Physics, 19 (45), 30627-30635. doi: 10.1039/c7cp06670h

Star polymers reduce islet amyloid polypeptide toxicity via accelerated amyloid aggregation

Pilkington, Emily H., Lai, May, Ge, Xinwei, Stanley, William J., Wang, Bo, Wang, Miaoyi, Kakinen, Aleksandr, Sani, Marc-Antonie, Whittaker, Michael R., Gurzov, Esteban N., Ding, Feng, Quinn, John F., Davis, Thomas P. and Ke, Pu Chun (2017). Star polymers reduce islet amyloid polypeptide toxicity via accelerated amyloid aggregation. Biomacromolecules, 18 (12), 4249-4260. doi: 10.1021/acs.biomac.7b01301

Implications of peptide assemblies in amyloid diseases

Ke, Pu Chun, Sani, Marc-Antonie, Ding, Feng, Kakinen, Aleksandr, Javed, Ibrahim, Separovic, Frances, Davis, Thomas P. and Mezzenga, Raffaele (2017). Implications of peptide assemblies in amyloid diseases. Chemical Society Reviews, 46 (21), 6492-6531. doi: 10.1039/c7cs00372b

Plasma proteome association and catalytic activity of stealth polymer-grafted iron oxide nanoparticles

Wang, Miaoyi, Siddiqui, Ghizal, Gustafsson, Ove J. R., Kakinen, Aleksandr, Javed, Ibrahim, Voelcker, Nicolas H., Creek, Darren J., Ke, Pu Chun and Davis, Thomas P. (2017). Plasma proteome association and catalytic activity of stealth polymer-grafted iron oxide nanoparticles. Small, 13 (36) 1701528, 1701528. doi: 10.1002/smll.201701528

Zinc-coordination and C-peptide complexation: a potential mechanism for the endogenous inhibition of IAPP aggregation

Ge, Xinwei, Kakinen, Aleksandr, Gurzov, Esteban N., Yang, Wen, Pang, Lokman, Pilkington, Emily H., Govindan-Nedumpully, Praveen, Chen, Pengyu, Separovic, Frances, Davis, Thomas P., Ke, Pu Chun and Ding, Feng (2017). Zinc-coordination and C-peptide complexation: a potential mechanism for the endogenous inhibition of IAPP aggregation. Chemical Communications, 53 (68), 9394-9397. doi: 10.1039/c7cc04291d

NanoEHS beyond toxicity - focusing on biocorona

Lin, Sijie, Mortimer, Monika, Chen, Ran, Kakinen, Aleksandr, Riviere, Jim E., Davis, Thomas P., Ding, Feng and Ke, Pu Chun (2017). NanoEHS beyond toxicity - focusing on biocorona. Environmental Science-Nano, 4 (7), 1433-1454. doi: 10.1039/c6en00579a

Effects of Protein Corona on IAPP Amyloid Aggregation, Fibril Remodelling, and Cytotoxicity

Pilkington, Emily H., Xing, Yanting, Wang, Bo, Kakinen, Aleksandr, Wang, Miaoyi, Davis, Thomas P., Ding, Feng and Ke, Pu Chun (2017). Effects of Protein Corona on IAPP Amyloid Aggregation, Fibril Remodelling, and Cytotoxicity. Scientific Reports, 7 (1) 2455. doi: 10.1038/s41598-017-02597-0

Differential effects of silver and iron oxide nanoparticles on IAPP amyloid aggregation

Wang, Miaoyi, Kakinen, Aleksandr, Pilkington, Emily H., Davis, Thomas P. and Ke, Pu Chun (2017). Differential effects of silver and iron oxide nanoparticles on IAPP amyloid aggregation. Biomaterials Science, 5 (3), 485-493. doi: 10.1039/c6bm00764c

Solubility-driven toxicity of CuO nanoparticles to Caco2 cells and Escherichia coli: effect of sonication energy and test environment

Käkinen, Aleksandr, Kahru, Anne, Nurmsoo, Helen, Kubo, Anna-Liisa and Bondarenko, Olesja M. (2016). Solubility-driven toxicity of CuO nanoparticles to Caco2 cells and Escherichia coli: effect of sonication energy and test environment. Toxicology in Vitro, 36, 172-179. doi: 10.1016/j.tiv.2016.08.004

Inhibition of hIAPP amyloid aggregation and pancreatic beta-cell toxicity by OH-terminated PAMAM dendrimer

Gurzov, Esteban N., Wang, Bo, Pilkington, Emily H., Chen, Pengyu, Kakinen, Aleksandr, Stanley, William J., Litwak, Sara A., Hanssen, Eric G., Davis, Thomas P., Ding, Feng and Ke, Pu Chun (2016). Inhibition of hIAPP amyloid aggregation and pancreatic beta-cell toxicity by OH-terminated PAMAM dendrimer. Small, 12 (12), 1615-1626. doi: 10.1002/smll.201502317

Pancreatic beta-Cell Membrane Fluidity and Toxicity Induced by Human Islet Amyloid Polypeptide Species

Pilkington, Emily H., Gurzov, Esteban N., Kakinen, Aleksandr, Litwak, Sara A., Stanley, William J., Davis, Thomas P. and Ke, Pu Chun (2016). Pancreatic beta-Cell Membrane Fluidity and Toxicity Induced by Human Islet Amyloid Polypeptide Species. Scientific Reports, 6 (1) 21274. doi: 10.1038/srep21274

An interlaboratory comparison of nanosilver characterisation and hazard identification: harmonising techniques for high quality data

Jemec, Anita, Kahru, Anne, Potthoff, Annegret, Drobne, Damjana, Heinlaan, Margit, Böhme, Steffi, Geppert, Mark, Novak, Sara, Schirmer, Kristin, Rekulapally, Rohit, Singh, Shashi, Aruoja, Villem, Sihtmäe, Mariliis, Juganson, Katre, Käkinen, Aleksandr and Kühnel, Dana (2016). An interlaboratory comparison of nanosilver characterisation and hazard identification: harmonising techniques for high quality data. Environment International, 87, 20-32. doi: 10.1016/j.envint.2015.10.014

Stabilizing off-pathway oligomers by polyphenol nanoassemblies for IAPP aggregation inhibition

Nedumpully-Govindan, Praveen, Kakinen, Aleksandr, Pilkington, Emily H., Davis, Thomas P., Ke, Pu Chun and Ding, Feng (2016). Stabilizing off-pathway oligomers by polyphenol nanoassemblies for IAPP aggregation inhibition. Scientific Reports, 6 (1) 19463. doi: 10.1038/srep19463

Brushed polyethylene glycol and phosphorylcholine for grafting nanoparticles against protein binding

Wang, Bo, Blin, Thomas, Kakinen, Aleksandr, Ge, Xinwei, Pilkington, Emily H., Quinn, John F., Whittaker, Michael R., Davis, Thomas P., Ke, Pu Chun and Ding, Feng (2016). Brushed polyethylene glycol and phosphorylcholine for grafting nanoparticles against protein binding. Polymer Chemistry, 7 (45), 6875-6879. doi: 10.1039/c6py01480a

Synthesis and in vitro properties of iron oxide nanoparticles grafted with brushed phosphorylcholine and polyethylene glycol

Blin, Thomas, Kakinen, Aleksandr, Pilkington, Emily H., Ivask, Angela, Ding, Feng, Quinn, John F., Whittaker, Michael R., Ke, Pu Chun and Davis, Thomas P. (2016). Synthesis and in vitro properties of iron oxide nanoparticles grafted with brushed phosphorylcholine and polyethylene glycol. Polymer Chemistry, 7 (10), 1931-1944. doi: 10.1039/c5py02024g

Dissolution of CuO nanoparticles and their in vitro toxicity to Caco-2 cells and bacteria Escherichia coli depends on CuO ultrasonication protocol

Bondarenko, O., Käkinen, A., Nurmsoo, H. and Kahru, A. (2015). Dissolution of CuO nanoparticles and their in vitro toxicity to Caco-2 cells and bacteria Escherichia coli depends on CuO ultrasonication protocol. Toxicology Letters, 238 (2), S210-S210. doi: 10.1016/j.toxlet.2015.08.624

Toxicity of 11 metal oxide nanoparticles to three mammalian cell types in vitro

Ivask, Angela, Titma, Tiina, Visnapuu, Meeri, Vija, Heiki, Kaekinen, Aleksandr, Sihtmaee, Mariliis, Pokhrel, Suman, Maedler, Lutz, Heinlaan, Margit, Kisand, Vambola, Shimmo, Ruth and Kahru, Anne (2015). Toxicity of 11 metal oxide nanoparticles to three mammalian cell types in vitro. Current Topics in Medicinal Chemistry, 15 (18), 1914-1929. doi: 10.2174/1568026615666150506150109

Size-dependent toxicity of silver nanoparticles to bacteria, yeast, algae, crustaceans and mammalian cells in vitro

Ivask, Angela, Kurvet, Imbi, Kasemets, Kaja, Blinova, Irina, Aruoja, Villem, Suppi, Sandra, Vija, Heiki, Kaekinen, Aleksandr, Titma, Tiina, Heinlaan, Margit, Visnapuu, Meeri, Koller, Dagmar, Kisand, Vambola and Kahru, Anne (2014). Size-dependent toxicity of silver nanoparticles to bacteria, yeast, algae, crustaceans and mammalian cells in vitro. PLoS One, 9 (7) e102108. doi: 10.1371/journal.pone.0102108

Selective performance of sol-gel synthesised titanium dioxide photocatalysts in aqueous oxidation of various-type organic pollutants

Klauson, Deniss, Budarnaja, Olga, Stepanova, Kristina, Krichevskaya, Marina, Dedova, Tatjana, Käkinen, Aleksandr and Preis, Sergei (2014). Selective performance of sol-gel synthesised titanium dioxide photocatalysts in aqueous oxidation of various-type organic pollutants. Kinetics and Catalysis, 55 (1), 47-55. doi: 10.1134/s0023158414010030

Aqueous photocatalytic oxidation of prednisolone

Klauson, Deniss, Pilnik-Sudareva, Jana, Pronina, Natalja, Budarnaja, Olga, Krichevskaya, Marina, Käkinen, Aleksandr, Juganson, Katre and Preis, Sergei (2013). Aqueous photocatalytic oxidation of prednisolone. Central European Journal of Chemistry, 11 (10), 1620-1633. doi: 10.2478/s11532-013-0290-8

Interaction of firefly luciferase and silver nanoparticles and its impact on enzyme activity

Kaekinen, Aleksandr, Ding, Feng, Chen, Pengyu, Mortimer, Monika, Kahru, Anne and Ke, Pu Chun (2013). Interaction of firefly luciferase and silver nanoparticles and its impact on enzyme activity. Nanotechnology, 24 (34) 345101. doi: 10.1088/0957-4484/24/34/345101

Competitive binding of natural amphiphiles with graphene derivatives

Radic, Slaven, Geitner, Nicholas K., Podila, Ramakrishna, Kaekinen, Aleksandr, Chen, Pengyu, Ke, Pu Chun and Ding, Feng (2013). Competitive binding of natural amphiphiles with graphene derivatives. Scientific Reports, 3 (1) 2273. doi: 10.1038/srep02273

Particle-cell contact enhances antibacterial activity of silver nanoparticles

Bondarenko, Olesja, Ivask, Angela, Kaekinen, Aleksandr, Kurvet, Imbi and Kahru, Anne (2013). Particle-cell contact enhances antibacterial activity of silver nanoparticles. PLoS One, 8 (5) e64060. doi: 10.1371/journal.pone.0064060

Toxicity of two types of silver nanoparticles to aquatic crustaceans Daphnia magna and Thamnocephalus platyurus

Blinova, Irina, Niskanen, Jukka, Kajankari, Paula, Kanarbik, Liina, Kaekinen, Aleksandr, Tenhu, Heikki, Penttinen, Olli-Pekka and Kahru, Anne (2013). Toxicity of two types of silver nanoparticles to aquatic crustaceans Daphnia magna and Thamnocephalus platyurus. Environmental Science and Pollution Research, 20 (5), 3456-3463. doi: 10.1007/s11356-012-1290-5

Sub-toxic effects of CuO nanoparticles on bacteria: Kinetics, role of Cu ions and possible mechanisms of action

Bondarenko, Olesja, Ivask, Angela, Kaekinen, Aleksandr and Kahru, Anne (2012). Sub-toxic effects of CuO nanoparticles on bacteria: Kinetics, role of Cu ions and possible mechanisms of action. Environmental Pollution, 169, 81-89. doi: 10.1016/j.envpol.2012.05.009

Environmental hazard of oil shale combustion fly ash

Blinova, Irina, Bityukova, Liidia, Kasemets, Kaja, Ivask, Angela, Kaekinen, Aleksandr, Kurvet, Imbi, Bondarenko, Olesja, Kanarbik, Liina, Sihtmaee, Mariliis, Aruoja, Villem, Schvede, Hedi and Kahru, Anne (2012). Environmental hazard of oil shale combustion fly ash. Journal of Hazardous Materials, 229, 192-200. doi: 10.1016/j.jhazmat.2012.05.095

The effect of composition of different ecotoxicological test media on free and bioavailable copper from CuSO4 and CuO nanoparticles: comparative evidence from a Cu-selective electrode and a Cu-biosensor

Kaekinen, Aleksandr, Bondarenko, Olesja, Ivask, Angela and Kahru, Anne (2011). The effect of composition of different ecotoxicological test media on free and bioavailable copper from CuSO4 and CuO nanoparticles: comparative evidence from a Cu-selective electrode and a Cu-biosensor. Sensors, 11 (11), 10502-10521. doi: 10.3390/s111110502

Mesoscopic properties and molecular mechanisms of IAPP amyloid inhibition and remodeling with small molecules

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