Gianluca GRENCI
Research Assistant Professor, Department of Biomedical Engineering, National University of Singapore
Facility Manager, Nano and Microfabrication Core
mbigg@nus.edu.sg
Level 10 T-Lab
National University of Singapore
5A Engineering Drive 1
Singapore 117411
Geetika Chouhan
Research Fellow, Dye Group
Seeking Research Assistant for project with MBI Fellow Dr. Tee Yee Han at the Mechanobiology Institute, NUS
The Mechanobiology Institute, NUS seeks to recruit a Research Assistant to work with MBI Fellow Dr. Tee Yee Han.
Seeking Research Fellow in the group of Prof. Alexander Bershadsky at the Mechanobiology Institute, NUS
The Mechanobiology Institute, NUS seeks to recruit a Research Fellow in the group of Prof. Alexander Bershadsky at the MBI, NUS.
Vaishnavi Rangaraj
Research Assistant, Holle Group
Liu Haoqiu
Research Fellow, Michelot Group
Seeking Postdoctoral Research Fellow for collaborative project between Dr. Yin Loon Lee and Prof. Alexander Bershadsky at the Mechanobiology Institute, NUS
The Mechanobiology Institute, NUS seeks to recruit a Postdoctoral Research Fellow for a collaborative project between Dr. Yin Loon Lee (A*STAR) and Prof. Alexander Bershadsky.
Gianluca Grenci
Research Assistant Professor, Facility Manager
Research Interests
Microfluidics, Micro-optical systems for live cell imaging
Our laboratory is primarily interested in the application of micro/nano fabrication technology to biological science. We exploit standard and advanced micro-fabrication tools in order to design and produce systems and devices for cell culturing and imaging. Examples of such devices are: topographically and/or chemically micro-textured environments, microfluidic devices, micro-optical systems and more.
We are also interested in developing microfluidic devices for FTIR spectromicroscopy of living cells. FTIR is an imaging technique that is intrinsically label-free and requires minimal sample preparation; when coupled with microscopy and high brilliance IR sources it allows the acquisition of chemical maps at a resolution which is diffraction limited. Absorption of IR photons induces very low or no damage at all, therefore it is in principle possible to observe for prolonged time the behaviour of living cells. Our research activity is intended to develope microfludic platforms suitable for FTIR (key parameters are optical transparency and low IR absorption) while keeping cells alive and healthy; a beneficial feature provided by micro-fabrication approach is the possibility to control of the chemical environment at the micro-scale.
Research Areas
Micro/nano engineering, microfluidic, FTIR
Biography
Dr Gianluca Grenci joined MBI in 2012 as a research fellow and head of the Micro Fabrication Core facility. Previously he was employed at the LILIT micro/nano fabrication group (IOM-CNR, Trieste, IT) for a total of 6 years, during which he was mainly involved in the design and fabrication of microfluidic devices for synchrotron-light related spectroscopic techniques, such as SAXS and FTIR. He thus developed extensive practical knowledge on all the major lithographic technologies (UV and EB lithography, wet/dry etching, soft-lithography, thin films deposition), plus some less usual and/or more advanced technique, such as X-ray Lithography and LIGA.
He did his PhD in the field of applied superconductivity, in a project aimed to develop a current cryo-comparator (CCC) using high critical temperature superconductors of the cuprate family (YBCO) in the form of a thick film deposited onto a large area, complex shaped silver substrate.
Education
PhD Polytechnic of Torino, DISPEA
Recent Publications
- Zhang Z, Canela A, Kurisu J, Zou P, Kawaue T, Nakazawa N, Takeda N, Saeki M, Utsunomiya M, Bilgic M, Ishidate F, Grenci G, Furuta T, Kishi Y, Sasanuma H, and Kengaku M. Confined migration induces non-lethal DNA damage in developing neurons. Nature 2026;. [PMID: 42310452]
- Gandin A, Torresan V, Panciera T, Grenci G, Vanni G, Citron A, Marchionni M, Battilana G, Pelosin M, Busetto R, Piccolo S, and Brusatin G. Flexible high-resolution ECM micropatterning. Nat Protoc 2026;. [PMID: 42129485]
- Dunsing-Eichenauer V, Hummert J, Chardès C, Schönau T, Guignard L, Galland R, Grenci G, Tillmann M, Koberling F, Nock C, Sibarita J, Viasnoff V, Antolovic IM, Erdmann R, and Lenne P. Fast volumetric fluorescence lifetime imaging of multicellular systems using single-objective light-sheet microscopy. Commun Biol 2025;. [PMID: 41315677]
- Jiang X, Xu P, Feng F, Grenci G, and Saw TB. Revealing Electromechanical Control of Tissue Homeostasis Using a Two-Layer Microfluidic Device. J Vis Exp 2025;(223). [PMID: 41052031]
- Cabillic M, Forriere H, Bettarel L, Butler C, Neuhaus A, Idrissi I, Sambrano-Lopez ME, Rossbroich J, Müller L, Ries J, Grenci G, Viasnoff V, Levet F, Sibarita J, and Galland R. In-depth single molecule localization microscopy using adaptive optics and single objective light-sheet microscopy. Nat Commun 2025; 16(1):8362. [PMID: 40993142]
- Mu B, Rutkowski DM, Grenci G, Vavylonis D, and Zhang D. Ca2+-dependent vesicular and non-vesicular lipid transfer controls hypoosmotic plasma membrane expansion. BMC Biol 2025; 23(1):207. [PMID: 40629316]
- Ong HT, Karatas E, Poquillon T, Grenci G, Furlan A, Dilasser F, Mohamad Raffi SB, Blanc D, Drimaracci E, Mikec D, Galisot G, Johnson BA, Liu AZ, Thiel C, Ullrich O, , Racine V, and Beghin A. Digitalized organoids: integrated pipeline for high-speed 3D analysis of organoid structures using multilevel segmentation and cellular topology. Nat Methods 2025;. [PMID: 40369245]
- Arora A, Rizvi MS, Grenci G, Dilasser F, Fu C, Ganguly M, Vaishnavi S, Paramsivam K, Budnar S, Noordstra I, Yap AS, and Viasnoff V. Viscous dissipation in the rupture of cell-cell contacts. Nat Mater 2025;. [PMID: 40355570]
- Nakazawa N, Grenci G, Kameo Y, Takeda N, Sawada T, Kurisu J, Zhang Z, Toma K, Adachi T, Nonomura K, and Kengaku M. PIEZO1-dependent mode switch of neuronal migration in heterogeneous microenvironments in the developing brain. Cell Rep 2025; 44(3):115405. [PMID: 40053456]
- Suryana M, Produit T, Yang H, Birarda G, Shanmugar JV, Krivitsky L, Paterova A, and Grenci G. Infrared imaging with visible light in microfluidic devices: the water absorption barrier. Analyst 2024;. [PMID: 39692693]
Selected Publications
- Mona Suryana, Jegan V. Shanmugarajah, Sivakumar M. Maniam, Gianluca Grenci. Soft Lithographic Procedure for Producing Plastic Microfluidic Devices with View-ports Transparent to Visible and Infrared Light
- Mohammed Ashraf, Sree V. Sundararajan, Gianluca Grenci. Low-power, low-pressure reactive-ion etching process for silicon etching with vertical and smooth walls for mechanobiology application
Lab Members
What factors regulate actin filament polymerization?
What factors regulate actin filament polymerization? Nucleation Promoting Factors (NPFs) (e.g. WASP, Scar/WAVE) modulate actin filament nucleation by bringing together actin monomers and pre-existing actin filaments, for example, during filopodial initiation where they recruit [...]
What is the steady state phase of actin polymerization?
What is the steady state phase of actin polymerization? In the steady state phase, the filament dynamics enter a state of equilibrium where monomer disassembly from the (-) end and polymerization at the (+) [...]
Actin Crosslinking
Actin Crosslinking Crosslinking of actin filaments is a critical step in cell motility and is a fundamental process in filopodia protrusion and lamellipodia formation. Smaller cross-linking proteins that are more globular (e.g. fascin) [...]
How are intermediate filaments assembled?
How are intermediate filaments assembled? The soluble subunit for creating intermediate filaments is a tetramer. The tetramer is created from monomers in a stepwise fashion (as reviewed in [1]). First, two monomers associate via [...]
Alpha-actinin
Alpha-actinin α-actinin is an actin-binding protein [1] and component of the actin crosslinking functional modules; it lacks G-actin binding activity and lacks actin initiation/nucleation activity [2]. α-actinin is an important organizer of the cytoskeleton [...]
Fascin
Fascin Fascin is the major actin crosslinking protein found in a wide range of filopodia [1][2][3]. This protein has been shown to work in concert with other cross linkers such as α-actinin to produce [...]
Filamin
Filamin The filamin family of proteins bind to both actin and a number of signaling molecules including Rho GTPases. Evidence for this was shown with the loss of Filamin-A in M2 Melanoma cells, which [...]
Fimbrin
Fimbrin Fimbrin (aka plastin homologue, accumentin) is an actin binding protein that was originally identified in microvilli [1][2]. This schematic diagram illustrates the molecular organization of fimbrin as depicted in this resource, and [...]
What are microtubules?
What are microtubules? Microtubules are hollow cylinders [1] that are approximately 25nm in diameter [2] and vary in length from 200 nm to 25 μm. They are formed by the lateral association of between [...]
What is capping protein?
What is capping protein? Capping protein is involved in actin filament assembly and disassembly Capping proteins control access to the free barbed ends of actin filaments and is therefore a major factor affecting actin [...]
What are intermediate filaments?
What are intermediate filaments? Intermediate filaments are a primary component of the cytoskeleton, although they are not found in all eukaryotes, and are absent in fungi and plants [1]. These filaments, which extend throughout [...]
I-BAR and Other Proteins/Factors
I-BAR and Other Proteins/Factors Proteins containing I-BAR (inverted Bin/amphiphysin/Rvs i.e. IRSp53 Missing-in-metastasis homology Domain or IMD) cooperate with various components of actin filament assembly, to promote filopodia protrusion, via several mechanisms including the stimulation [...]
Former Lab Members
What factors regulate actin filament polymerization?
What factors regulate actin filament polymerization? Nucleation Promoting Factors (NPFs) (e.g. WASP, Scar/WAVE) modulate actin filament nucleation by bringing together actin monomers and pre-existing actin filaments, for example, during filopodial initiation where they recruit [...]
What is the steady state phase of actin polymerization?
What is the steady state phase of actin polymerization? In the steady state phase, the filament dynamics enter a state of equilibrium where monomer disassembly from the (-) end and polymerization at the (+) [...]
Actin Crosslinking
Actin Crosslinking Crosslinking of actin filaments is a critical step in cell motility and is a fundamental process in filopodia protrusion and lamellipodia formation. Smaller cross-linking proteins that are more globular (e.g. fascin) [...]
How are intermediate filaments assembled?
How are intermediate filaments assembled? The soluble subunit for creating intermediate filaments is a tetramer. The tetramer is created from monomers in a stepwise fashion (as reviewed in [1]). First, two monomers associate via [...]
Alpha-actinin
Alpha-actinin α-actinin is an actin-binding protein [1] and component of the actin crosslinking functional modules; it lacks G-actin binding activity and lacks actin initiation/nucleation activity [2]. α-actinin is an important organizer of the cytoskeleton [...]
Fascin
Fascin Fascin is the major actin crosslinking protein found in a wide range of filopodia [1][2][3]. This protein has been shown to work in concert with other cross linkers such as α-actinin to produce [...]
Filamin
Filamin The filamin family of proteins bind to both actin and a number of signaling molecules including Rho GTPases. Evidence for this was shown with the loss of Filamin-A in M2 Melanoma cells, which [...]
Fimbrin
Fimbrin Fimbrin (aka plastin homologue, accumentin) is an actin binding protein that was originally identified in microvilli [1][2]. This schematic diagram illustrates the molecular organization of fimbrin as depicted in this resource, and [...]
What are microtubules?
What are microtubules? Microtubules are hollow cylinders [1] that are approximately 25nm in diameter [2] and vary in length from 200 nm to 25 μm. They are formed by the lateral association of between [...]
What is capping protein?
What is capping protein? Capping protein is involved in actin filament assembly and disassembly Capping proteins control access to the free barbed ends of actin filaments and is therefore a major factor affecting actin [...]
What are intermediate filaments?
What are intermediate filaments? Intermediate filaments are a primary component of the cytoskeleton, although they are not found in all eukaryotes, and are absent in fungi and plants [1]. These filaments, which extend throughout [...]
I-BAR and Other Proteins/Factors
I-BAR and Other Proteins/Factors Proteins containing I-BAR (inverted Bin/amphiphysin/Rvs i.e. IRSp53 Missing-in-metastasis homology Domain or IMD) cooperate with various components of actin filament assembly, to promote filopodia protrusion, via several mechanisms including the stimulation [...]
