Microfluidics
Microfluidic devices are very useful tools with a wide range of applications including environmental sensing, medical diagnostics, drug discovery, drug delivery, microscale chemical production, combinatorial synthesis and assays and artificial organs. Various microfluidic devices can be designed, fabricated and validated at the Macquarie University node of CNBP, depending on applications. We have one ISO Class 7 clean room for semiconductor processing and device fabrication. Fabricated microdevices can be used by connecting to a three channel outlet pressure controller system. They can also be coupled with flow sensors which offer a range of flow rates depending on your needs.
Microfluidic devices fabricated for biomarker isolation and detection (courtesy Dr Lianmei Jiang)The clean room contains essential fabrication and testing equipment for processing photoresist, spin coating materials, 3D printing, depositing metals, etching (chemically & plasma) and analysing the results (profiler, microscope and film thickness measurements). Microfluidic devices for various chemical and biological applications can be fabricated here.
Potential Uses and Applications
- Microfluidic devices for biomarker isolation and detection
- Microfluidic droplets based cell assay / chemical synthesis
- Organ on a chip
- 3D cell culture
- High throughput screening
- Sensing devices integrated with SERS, electrochemical detection, etc.
Contacts
Dr Yuling Wang: yuling.wang@mq.edu.au
Dr Lianmei Jiang: lianmei.jiang@mq.edu.au
Dr David Inglis: david.inglis@mq.edu.au
Key publications
- Liu HR, Li M, Wang Y, Piper J, Jiang LM (2020) ‘Improving single-cell encapsulation efficiency and reliability through neutral buoyancy of suspension’. Micromachines, 11: 94-98. DOI:3390/mi11010094
- Feng SL, Liu GZ, Jiang LM, Zhu YG, Goldys EM, Inglis DW (2017) ‘A Microfluidic needle for sampling and delivery of chemical signals by segmented flows’. Applied Physics Letters, 11: 183702. DOI:1063/1.4995657
Proteomics, Glycomics and Glycoproteomics
MProtein glycosylation and glycoconjugates in general are of particular interest due to their fundamental role in cell function. More than 50% of known human proteins are in fact glycoproteins. Dysfunctions in the glycosylation machinery have been associated with a variety of diseases such as chronic inflammatory conditions, cancer, neurodegenerative and cardiovascular diseases as well as reproduction. Glycosylation is also a crucial factor in bacterial and viral infections and the immune response. This makes glycoconjugates extremely interesting diagnostic, therapeutic and prognostic target molecules. In the CNBP we have developed, applied and pioneered Proteomics, Glycomics and Glycoproteomics technologies and translated this knowledge to discover new glyco-features that can be targeted by nanoparticles for diagnosis and drug delivery.
These proteomics, glycomics and glycoproteomics mass spectrometry-based workflows and technologies are used to capture and unravel the identity, quantity and specific glycosylation features of proteins in health and disease of humans and animals.
N-glycan structures can differentiate different tissue regions in ovarian cancer.Potential Uses and Applications
- Understanding mechanisms of glycan-involvement in pain perception
- Unravelling the glycosylation events around the pathogenesis of arterial plaque
- Determining glycosylation features associated with the success of in vitro fertilisation
- Identifying novel glyco-signatures to increase specificity and sensitivity for early stage cancer detection
- Improve functionalisation of nanoparticles for biological applications
- Discovery of new glycosylation targets for biotherapeutics
- Improved imaging of tissues and cells based on precise location of specific glycan structure mass profiles
Contacts
Prof. Nicki Packer: nicki.packer@mq.edu.au
A/Prof. Daniel Kolarich: d.kolarich@griffith.edu.au
Key publications
- Structural analysis of N- and O-glycans released from glycoproteins. Jensen PH, Karlsson NG, Kolarich D, Packer NH. Nat Protoc. 2012 Jun 7;7(7):1299-310. doi: 10.1038/nprot.2012.063. PMID: 2267843320
- Determination of site-specific glycan heterogeneity on glycoproteins. Kolarich D, Jensen PH, Altmann F, Packer NH. Nat Protoc. 2012 Jun 7;7(7):1285-98. doi: 10.1038/nprot.2012.062.
- Enabling Sensitive Phenotypic Profiling of Cancer-Derived Small Extracellular Vesicles Using Surface-Enhanced Raman Spectroscopy Nanotags. Zhang W, Jiang L, Diefenbach RJ, Campbell DH, Walsh BJ, Packer NH, Wang Y. ACS Sens. 2020 Mar 27;5(3):764-771. doi: 10.1021/acssensors.9b02377.
- Biochimica et Biophysica Acta (BBA) – Reviews on Cancer. doi.org/10.1016/j.bbcan.2020.188422
- https://www.sciencedirect.com/science/article/abs/pii/S0304419X20301414 Mohammad Rasheduzzaman, Arutha Kulasinghe, Riccardo Dolcetti, Liz Kenny, Newell W. Johnson, Daniel Kolarich, Chamindie Punyadeera
