A multi-scale numerical approach to study monoclonal antibodies in solution
Polimeni, Marco LU ; Zaccarelli, Emanuela ; Gulotta, Alessandro LU ; Lund, Mikael LU
; Stradner, Anna
LU
and Schurtenberger, Peter
LU
(2024)
In APL Bioengineering
8(1).
- Abstract
Developing efficient and robust computational models is essential to improve our understanding of protein solution behavior. This becomes particularly important to tackle the high-concentration regime. In this context, the main challenge is to put forward coarse-grained descriptions able to reduce the level of detail, while retaining key features and relevant information. In this work, we develop an efficient strategy that can be used to investigate and gain insight into monoclonal antibody solutions under different conditions. We use a multi-scale numerical approach, which connects information obtained at all-atom and amino-acid levels to bead models. The latter has the advantage of reproducing the properties of interest while being... (More)
Developing efficient and robust computational models is essential to improve our understanding of protein solution behavior. This becomes particularly important to tackle the high-concentration regime. In this context, the main challenge is to put forward coarse-grained descriptions able to reduce the level of detail, while retaining key features and relevant information. In this work, we develop an efficient strategy that can be used to investigate and gain insight into monoclonal antibody solutions under different conditions. We use a multi-scale numerical approach, which connects information obtained at all-atom and amino-acid levels to bead models. The latter has the advantage of reproducing the properties of interest while being computationally much faster. Indeed, these models allow us to perform many-protein simulations with a large number of molecules. We can, thus, explore conditions not easily accessible with more detailed descriptions, perform effective comparisons with experimental data up to very high protein concentrations, and efficiently investigate protein-protein interactions and their role in phase behavior and protein self-assembly. Here, a particular emphasis is given to the effects of charges at different ionic strengths.
(Less)
- author
- Polimeni, Marco
LU
; Zaccarelli, Emanuela
; Gulotta, Alessandro
LU
; Lund, Mikael
LU
; Stradner, Anna
LU
and Schurtenberger, Peter
LU
- organization
- publishing date
- 2024-03-01
- type
- Contribution to journal
- publication status
- published
- subject
- in
- APL Bioengineering
- volume
- 8
- issue
- 1
- article number
- 016111
- publisher
- American Institute of Physics (AIP)
- external identifiers
-
- pmid:38425712
- scopus:85186120541
- ISSN
- 2473-2877
- DOI
- 10.1063/5.0186642
- language
- English
- LU publication?
- yes
- id
- 75b998f4-a5db-47d4-8cfa-8a1cb4dfecb4
- date added to LUP
- 2024-03-15 14:41:05
- date last changed
- 2024-04-26 12:03:57
@article{75b998f4-a5db-47d4-8cfa-8a1cb4dfecb4,
abstract = {{<p>Developing efficient and robust computational models is essential to improve our understanding of protein solution behavior. This becomes particularly important to tackle the high-concentration regime. In this context, the main challenge is to put forward coarse-grained descriptions able to reduce the level of detail, while retaining key features and relevant information. In this work, we develop an efficient strategy that can be used to investigate and gain insight into monoclonal antibody solutions under different conditions. We use a multi-scale numerical approach, which connects information obtained at all-atom and amino-acid levels to bead models. The latter has the advantage of reproducing the properties of interest while being computationally much faster. Indeed, these models allow us to perform many-protein simulations with a large number of molecules. We can, thus, explore conditions not easily accessible with more detailed descriptions, perform effective comparisons with experimental data up to very high protein concentrations, and efficiently investigate protein-protein interactions and their role in phase behavior and protein self-assembly. Here, a particular emphasis is given to the effects of charges at different ionic strengths.</p>}},
author = {{Polimeni, Marco and Zaccarelli, Emanuela and Gulotta, Alessandro and Lund, Mikael and Stradner, Anna and Schurtenberger, Peter}},
issn = {{2473-2877}},
language = {{eng}},
month = {{03}},
number = {{1}},
publisher = {{American Institute of Physics (AIP)}},
series = {{APL Bioengineering}},
title = {{A multi-scale numerical approach to study monoclonal antibodies in solution}},
url = {{http://dx.doi.org/10.1063/5.0186642}},
doi = {{10.1063/5.0186642}},
volume = {{8}},
year = {{2024}},
}