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Strong electrostatic attraction drives milk heteroprotein complex coacervation

Vinterbladh, Isabel LU orcid ; Soussi, Rima Hachfi ; Forsman, Jan LU ; Bouhallab, Said and Lund, Mikael LU orcid (2025) In International Journal of Biological Macromolecules 286.
Abstract

Coacervates of oppositely charged milk proteins are used in functional food development, mainly to encapsulate bioactives. To uncover the driving forces behind coacervates formation, we study the association of lactoferrin and β−lactoglobulin at amino-acid level detail, using molecular simulations. Our findings show that inter-protein electrostatic interactions dominate and are, surprisingly, equally divided between an isotropic part, due to monopole-monopole attraction of the oppositely charged proteins, and an anisotropic part due to uneven surface charge distributions. In good agreement with recent experimental association constants, the calculated protein-protein interaction free energy is strongly dependent on pH and salt... (More)

Coacervates of oppositely charged milk proteins are used in functional food development, mainly to encapsulate bioactives. To uncover the driving forces behind coacervates formation, we study the association of lactoferrin and β−lactoglobulin at amino-acid level detail, using molecular simulations. Our findings show that inter-protein electrostatic interactions dominate and are, surprisingly, equally divided between an isotropic part, due to monopole-monopole attraction of the oppositely charged proteins, and an anisotropic part due to uneven surface charge distributions. In good agreement with recent experimental association constants, the calculated protein-protein interaction free energy is strongly dependent on pH and salt concentration. In addition to thermodynamics, we also investigate amino acid contacts in microstates of trimeric and pentameric protein complexes, and identify interaction hot-spots that drive heteroprotein complex coacervation process.

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author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Coacervates, Heteroprotein complex coacervation, Lactoferrin, Metropolis-Hastings Monte Carlo, Milk proteins, Parallel tempering, β-lactoglobulin
in
International Journal of Biological Macromolecules
volume
286
article number
137790
publisher
Elsevier
external identifiers
  • pmid:39603294
  • scopus:85211212453
ISSN
0141-8130
DOI
10.1016/j.ijbiomac.2024.137790
language
English
LU publication?
yes
id
849c8ca3-77c3-4b1f-a321-89347fe7cb45
date added to LUP
2025-03-04 15:35:32
date last changed
2025-07-09 02:34:04
@article{849c8ca3-77c3-4b1f-a321-89347fe7cb45,
  abstract     = {{<p>Coacervates of oppositely charged milk proteins are used in functional food development, mainly to encapsulate bioactives. To uncover the driving forces behind coacervates formation, we study the association of lactoferrin and β−lactoglobulin at amino-acid level detail, using molecular simulations. Our findings show that inter-protein electrostatic interactions dominate and are, surprisingly, equally divided between an isotropic part, due to monopole-monopole attraction of the oppositely charged proteins, and an anisotropic part due to uneven surface charge distributions. In good agreement with recent experimental association constants, the calculated protein-protein interaction free energy is strongly dependent on pH and salt concentration. In addition to thermodynamics, we also investigate amino acid contacts in microstates of trimeric and pentameric protein complexes, and identify interaction hot-spots that drive heteroprotein complex coacervation process.</p>}},
  author       = {{Vinterbladh, Isabel and Soussi, Rima Hachfi and Forsman, Jan and Bouhallab, Said and Lund, Mikael}},
  issn         = {{0141-8130}},
  keywords     = {{Coacervates; Heteroprotein complex coacervation; Lactoferrin; Metropolis-Hastings Monte Carlo; Milk proteins; Parallel tempering; β-lactoglobulin}},
  language     = {{eng}},
  publisher    = {{Elsevier}},
  series       = {{International Journal of Biological Macromolecules}},
  title        = {{Strong electrostatic attraction drives milk heteroprotein complex coacervation}},
  url          = {{http://dx.doi.org/10.1016/j.ijbiomac.2024.137790}},
  doi          = {{10.1016/j.ijbiomac.2024.137790}},
  volume       = {{286}},
  year         = {{2025}},
}