Menu Search

Cristiano Dias

Dias, Cristiano Luis
Associate Professor, Physics
481 Tiernan Hall
About me

(Check the Dias lab at

Cristiano is an Associate Professor in the Department of Physics at NJIT where he runs the Dias lab in computational biophysics. The lab uses multiscale models that can bridge atomistic and mesoscopic length scales to provide a better understanding of biological systems and diseases. Enhanced sampling methods as well as brute force molecular dynamics simulations are used to study these systems. The lab also develops new simulation methods whenever needed.

‚ÄčMain research interests: (i) the structure of amyloid proteins and their aggregation into oligomers and fibrils related to senile plaques in the brain of Alzheimer's patients, (ii) effect of organic molecules/drugs on the structure and aggregation of amyloid proteins, (iii) interactions of amyloid fibrils and lipid bilayers, (iv) allosteric effects in enzymes, and (v) formation of methane clathrates at the atomic level.

Several of the research projects in the Dias lab are performed in collaboration with experimental and theoretical partners. Thus, do not hesitate to contact us if you are interested in collaboration.

Post-doc, Physics, Freie Universistat Berlin (Volkswagen Fellow)
Post-doc, Biochemistry, University of Toronto
Post-doc, Applied Mathematics, Western Ontario
PhD, Physics, McGill University.
MSc, Physics, Universite de Montreal.
Bsc, Physics, Universidade de Brasilia.

Research Interests

Dr. Dias uses theory and computer simulations to understand emerging phenomena at the interface of Physics, Biology, and Chemistry. His group uses all-atom models and develops coarse-grained models to study equilibrium and non-equilibrium phenomena in molecular Bio-Physics. Dr. Dias seeks to decipher: (i) microscopic mechanisms accounting for the aggregation of peptides into amyloid fibrils, (ii) how these fibrils interact with each other accounting for the bulk properties of biomaterials, and (iii) how they interact with micelles/cells. These efforts are of paramount importance for the design of new drugs to treat diseases that result from misfolding and/or aggregation, to understand biological and cellular functions at the molecular level, and to design new biomaterials.

Selected Publications

(Check the Dias lab at

Zhaoqian Su, Gopal Ravindhran, and Cristiano Dias, Effects of Trimethylamine-N-oxide (TMAO) on hydrophobic and charged interactions, J. Phys. Chem. B 122, 5557 (2018).

Zhaoqian Su, Farbod Mahmoudinobar, and Cristiano Dias, Role of TMAO on the conformation of peptides and its implication for proteins, Phys. Rev. Letters 119, 108102 (2017).

Zhaoqian Su and Cristiano L. Dias, Molecular mechanism of protein unfolding by urea, Journal of Molecular Liquids 228, 168-175 (2017).

Srinivasa R. Jampani, Farbood Mahmoudinobar, Zhaoqian Su and Cristiano L. Dias, Thermodynamics of Abeta16-21 dissociation from a fibril, PROTEIN: Structure, Function, and Bioinformatics 83, 1963 (2015).

Cristiano L. Dias and Hue Sun Chan. Pressure-Dependence Properties of Elementary Hydrophobic Interactions: Ramifications for Activation Properties of Protein Folding. J. Phys. Chem. B 118, 7488 (2014).

Chitra Narayanan and Cristiano L. Dias. Hydrophobic interactions and hydrogen bonds in beta-sheet formation. J. Chem. Phys. 139, 115103 (2013).

Cristiano L. Dias. Unifying microscopic mechanism for pressure and cold denaturations of proteins, Physical Review letter 109, 048104 (2012)

Teemu Hynninen, Vili Heinonen, Cristiano L. Dias, Mikko Karttunen, Adam S. Foster and Tapio Ala-Nissila. Cutting Ice: Nanowire Regelation, Physical Review Letters 105, 086102 (2010).

Jirasak Wong-Ekkabut, M. Miettinen, Cristiano L. Dias and Mikko Kartunnen. Static charges cannot drive a continuous flow of water molecules through a carbon nanotube, Nature Nanotechnology 5, 555 (2010).

Cristiano L. Dias, Tapio Ala-Nissila, Martin Grant and Mikko Karttunen. Three-dimensional "Mercedes-Benz" model for water. Journal of Chemical Physics 131, 054505, 2009.

Cristiano L. Dias, Tapio Ala-Nissila, Mikko Karttunen, Ilpo Vattulainen, and Martin Grant. Microscopic mechanism for cold denaturation. Physical Review Letters 100, 118101, 2008.

(check my website for a full list of publications)