Marco Buscaglia

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Associate Professor of Applied Physics (SSD FIS/07)
Department of Medical Biotechnology and Translational Medicine

My research focuses on molecular biophysics, novel optical materials and optical techniques.
I investigate the fundamental aspects leading from the weak interactions of molecular systems to their complex behavior on a larger scale. My works spans the fields of applied physics, biophysics, soft condensed matter physics, optics, material science and biotechnology.

Current research lines:

  • Label-free optical biosensors
  • Functional surfaces based on DNA-nanotechnology tools
  • Protein folding and peptide dynamics




Biosketch

Orcid ID: 0000-0001-5010-0278




Research


Optical biosensors
                 

Molecular events on the nanometer scale can be detected by visible light without the need of fluorescence or colorimetric labels. These “label-free” sensors enable the real-time monitoring of binding, hence contributing to unravel the physics beyond molecular recognition processes. This also allows the realization of novel biosensing devices characterized by ease-of-use and rapidity.

To this aim, novel optical configurations are developed and molecular layers with controlled functionality are investigated. In particular, DNA-nanotechnology tools are exploited to design self-assembled molecular structures with enhanced binding strength and responsiveness.



Phantom materials

                 

Fluorinated polymer materials can be designed to have a refractive index very close to that of water. In this condition, these plastic materials are barely visible when immersed in water and, therefore they are called “phantom”. Thin molecular layers on their surface can produce an easily detectable optical signal due to reflectance or scattering. Suitable optical models combined with kinetics and transport effects enable the quantification of the molecules adhering to the surface.

Microfluidic chips embedding different types of phantom materials, from planar prisms to micro-porous membranes or micro-beads, are designed and realized with the aim of studying the molecular interaction with the surface and to create new concepts of optical sensors.



Protein folding


Folding of simple proteins is typically a spontaneous and repeatable process. Experiments on small proteins commonly show only two populations of molecules at equilibrium: folded (native) and unfolded (denatured). Research on protein folding aims to understand which of the many possible amino acid sequences may be able to fold up and how the detailed structure of a folded protein can be predicted from its amino acid sequence. Solving the folding problem may have enormous implications: genetic diseases could be treated more effectively and exact drugs could be designed theoretically without a great deal of experimentation.

Several mechanism are presumably involved in the complex process of protein folding. One of the simplest and most fundamental events taking place during the folding of a polypeptide is the formation of contacts between two specific chain residues. Measuring the rate of contact formations between two specific amino acids of the same chain provides a tool for the characterization of the elusive unfolded state in native conditions.








Selected publication:
  1. R. Lanfranco, F. Giavazzi, M. Salina, G. Tagliabue, E. Di Nicolò, T. Bellini, and M. Buscaglia, “Selective Adsorption on Fluorinated Plastic Enables the Optical Detection of Molecular Pollutants in Water”, Physical Review Applied 5, 054012 (2016).
  2. M. Salina, F. Giavazzi, E. Ceccarello, F. Damin, M. Chiari, M. Ciuffo, G. P. Accotto, M. Buscaglia, “Multi-spot, label-free detection of viral infection in complex media by a non-reflecting surface”, Sensor and Actuators B, 223, 957-962 (2016).
  3. M. Salina, F. Giavazzi, R. Lanfranco, E. Ceccarello, L. Sola, M. Chiari, B. Chini, R. Cerbino, T. Bellini, M. Buscaglia, “Multi-spot, label-free immunoassay on reflectionless glass”, Biosens Bioelectron, 74, 539-545 (2015).
  4. F. Giavazzi, M. Salina, E. Ceccarello, A. Ilacqua, F. Damin, L. Sola, M. Chiari, B. Chini, R. Cerbino, T. Bellini, M. Buscaglia, “A fast and simple label-free immunoassay based on a smartphone”, Biosens Bioelectron, 58, 395-402 (2014).
  5. F. Giavazzi, S. Crotti, A. Speciale, F. Serra, G. Zanchetta, V. Trappe, M. Buscaglia, T. Bellini, R. Cerbino, “Viscoelasticity of nematic liquid crystals at a glance”, Soft Matter, 10, 3938-3949 (2014).
  6. F. Giavazzi, M. Salina, R. Cerbino, M. Bassi, D. Prosperi, E. Ceccarello, F. Damin, L. Sola, M. Rusnati, M. Chiari, B. Chini, T. Bellini, M. Buscaglia, “Multispot, label-free biodetection at a phantom plastic–water interface”, PNAS, 110, 9350-9355 (2013).
  7. T. Araki, M. Buscaglia, T. Bellini, H. Tanaka, "Memory and topological frustration in nematic liquid crystals confined in porous materials", Nature Materials, 10, 303309 (2011).
  8. T. Cellmer*, M. Buscaglia*, E. R. Henry, J. Hofrichter, W. A. Eaton, "Making connections between ultrafast protein folding kinetics and molecular dynamics simulations", PNAS, 108, 6103-6108 (2011).
  9. M. Buscaglia, G. Lombardo, L. Cavalli, R. Barberi, T. Bellini, "Elastic anisotropy at a glance: the optical signature of disclination lines", Soft Matter, 6, 5434-5442, (2010).
  10. A. Soranno, R. Longhi, T. Bellini, M. Buscaglia, "Kinetics of contact formation and end-to-end distance distributions of swollen dosordered peptides", Biophysical Journal, 96, 1515-1528 (2009).
  11. M. Buscaglia, T. Bellini, C. Chiccoli, F. Mantegazza, P. Pasini, M. Rotunno, C. Zannoni, "Memory effects in nematics with quenched disorder", Physical Review E, 74, 011706 (2006).
  12. M. Buscaglia, L. J. Lapidus, W. A. Eaton, J. Hofrichter, "Effects of Denaturants on the Dynamics of Loop Formation in Polypeptides", Biophysical Journal, 91, 276-288 (2006).
  13. M. Buscaglia, J. Kubelka, W. A. Eaton, J. Hofrichter, "Determination of ultrafast protein folding rates from loop formation dynamics", Journal of Molecular Biology, 347, 657-664 (2005).
  14. M. Buscaglia, B. Schuler, L. J. Lapidus, W. A. Eaton, J. Hofrichter, "Kinetics of Intramolecular Contact Formation in a Denatured Protein", Journal of Molecular Biology, 332, 9-12 (2003).

 





From 2005 teaching duties of General Physics, Optics and Digital Image Processing for various Laurea Degree of the Faculty of Medicine (Medicine and Surgery, Physiotherapy, Podology, Biomedical Laboratory Technology, Optometric and Ophthalmology Assistant). Additional duties concerned the teaching of Fluorescence Methods in Biophysics for the PhD School of Physics.




Department of Medical Biotechnology and Translational Medicine
via F.lli Cervi 93, 20090 Segrate (MI)
Università degli studi di Milano
Phone +39 02503 30352
Fax +39 02503 30365
E-mail: marco.buscaglia@unimi.it





Inquiries are welcome either for “Laurea” Thesis or PhD positions.
Feel free to contact via email at marco.buscaglia@unimi.it