Velia Minicozzi
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Velia Minicozzi has a total of 7 co-authors. Here are the top co-authors by number of shared publications:
- Alessia Muroni
University of Rome Tor Vergata Via della Ricerca Scientifica 1
1 shared publication Almerinda Di Venere
Department of Experimental Medicine, University of Rome Tor Vergata, Rome, Italy
1 shared publicationFederica Sinibaldi
Department of Clinical Science and Translational Medicine, Tor Vergata University of Rome, Rome, Italy
1 shared publicationFulvio Erba
Department of Clinical Science and Translational Medicine, Tor Vergata University of Rome, Rome, Italy
1 shared publicationGiampiero Mei
Department of Experimental Medicine, University of Rome Tor Vergata, Rome, Italy
1 shared publication- Leonardo Domenichelli
Departmental Faculty of Engineering, Università Campus Bio-Medico di Roma, 00128 Rome, Italy
1 shared publication
Latest Publications
- Open Access
- 25 July 2025
- Published by Springer Nature in European Biophysics Journal
- Vol. 55 (2) , 263-273
In silico study of cytochrome-C binding to a cardiolipin-containing membrane
Cytochrome C is a key protein involved in electron transport within the mitochondrial respiratory chain and in apoptosis mechanisms. In this work, we provide a detailed theoretical analysis of the binding mechanism between cytochrome-C and a cardiolipin-containing membrane. Molecular dynamics simulations, along with protein contact network and fractal dimension analyses were employed to investigate the structural changes in cytochrome-C during the binding process. Our results suggest that cytochrome-C follows a two-step binding mechanism, starting with a rapid initial interaction, followed by slower conformational rearrangements. We identified two different cytochrome-C conformations at the membrane: a compact, native-like structure and an extended form. The latter, stabilized by Lys72, exhibits a higher binding affinity (≈ 2 kcal/mol) compared to the former. Protein extension also correlates with increased protein-membrane contact and altered heme ring orientation, suggesting that the partial unfolding of cytochrome-C could be crucial for its peroxidase activity and its role in apoptosis. These findings enhance the understanding of the cytochrome-C’s membrane interactions and its diverse functions.
- 25 July 2025
- Published by Springer Nature in European Biophysics Journal
- Vol. 55 (2) , 263-273
Open AccessIn silico study of cytochrome-C binding to a cardiolipin-containing membrane
Cytochrome C is a key protein involved in electron transport within the mitochondrial respiratory chain and in apoptosis mechanisms. In this work, we provide a detailed theoretical analysis of the binding mechanism between cytochrome-C and a cardiolipin-containing membrane. Molecular dynamics simulations, along with protein contact network and fractal dimension analyses were employed to investigate the structural changes in cytochrome-C during the binding process. Our results suggest that cytochrome-C follows a two-step binding mechanism, starting with a rapid initial interaction, followed by slower conformational rearrangements. We identified two different cytochrome-C conformations at the membrane: a compact, native-like structure and an extended form. The latter, stabilized by Lys72, exhibits a higher binding affinity (≈ 2 kcal/mol) compared to the former. Protein extension also correlates with increased protein-membrane contact and altered heme ring orientation, suggesting that the partial unfolding of cytochrome-C could be crucial for its peroxidase activity and its role in apoptosis. These findings enhance the understanding of the cytochrome-C’s membrane interactions and its diverse functions.