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Multidimensional Decomposition and Ensemble Modeling of Histatin 1 and Its Siblings : Detailing Structure and Biological Function Using an Integrative Approach

Svensson, Oskar LU ; Gerelli, Yuri and Skepö, Marie LU orcid (2025) In Journal of Chemical Information and Modeling 65(13). p.7089-7101
Abstract

Histatins are a family of multifunctional, cationic histidine-rich saliva peptides. The most prominently represented are Histatin 1, Histatin 3, and Histatin 5. Despite considerable similarities in primary structure, the three members are known to display varied antimicrobial properties and healing abilities. This study aims to provide a detailed structural comparison of Histatin 1, Histatin 3, and Histatin 5, as well as a thorough investigation into the variation caused to the conformational ensemble of Histatin 1 upon phosphorylation. The study applies molecular dynamics simulation, small-angle X-ray scattering, circular dichroism, bioinformatics tools, and neutron reflectometry. A multidimensional decomposition technique and its... (More)

Histatins are a family of multifunctional, cationic histidine-rich saliva peptides. The most prominently represented are Histatin 1, Histatin 3, and Histatin 5. Despite considerable similarities in primary structure, the three members are known to display varied antimicrobial properties and healing abilities. This study aims to provide a detailed structural comparison of Histatin 1, Histatin 3, and Histatin 5, as well as a thorough investigation into the variation caused to the conformational ensemble of Histatin 1 upon phosphorylation. The study applies molecular dynamics simulation, small-angle X-ray scattering, circular dichroism, bioinformatics tools, and neutron reflectometry. A multidimensional decomposition technique and its connection to clustering methods are also presented. It was observed that the phosphorylation of Histatin 1 profoundly shifts the conformational ensemble and may act as a molecular switch that facilitates tooth enamel binding. Observations are provided on the killing mechanisms of Histatins concerning self-association and membrane rupturing.

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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Chemical Information and Modeling
volume
65
issue
13
pages
13 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • pmid:40600658
  • scopus:105009849566
ISSN
1549-9596
DOI
10.1021/acs.jcim.5c00854
language
English
LU publication?
yes
id
95e1e47b-7d5a-41cd-9a2b-60b438659ab4
date added to LUP
2025-12-12 13:03:23
date last changed
2025-12-13 03:00:09
@article{95e1e47b-7d5a-41cd-9a2b-60b438659ab4,
  abstract     = {{<p>Histatins are a family of multifunctional, cationic histidine-rich saliva peptides. The most prominently represented are Histatin 1, Histatin 3, and Histatin 5. Despite considerable similarities in primary structure, the three members are known to display varied antimicrobial properties and healing abilities. This study aims to provide a detailed structural comparison of Histatin 1, Histatin 3, and Histatin 5, as well as a thorough investigation into the variation caused to the conformational ensemble of Histatin 1 upon phosphorylation. The study applies molecular dynamics simulation, small-angle X-ray scattering, circular dichroism, bioinformatics tools, and neutron reflectometry. A multidimensional decomposition technique and its connection to clustering methods are also presented. It was observed that the phosphorylation of Histatin 1 profoundly shifts the conformational ensemble and may act as a molecular switch that facilitates tooth enamel binding. Observations are provided on the killing mechanisms of Histatins concerning self-association and membrane rupturing.</p>}},
  author       = {{Svensson, Oskar and Gerelli, Yuri and Skepö, Marie}},
  issn         = {{1549-9596}},
  language     = {{eng}},
  number       = {{13}},
  pages        = {{7089--7101}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Journal of Chemical Information and Modeling}},
  title        = {{Multidimensional Decomposition and Ensemble Modeling of Histatin 1 and Its Siblings : Detailing Structure and Biological Function Using an Integrative Approach}},
  url          = {{http://dx.doi.org/10.1021/acs.jcim.5c00854}},
  doi          = {{10.1021/acs.jcim.5c00854}},
  volume       = {{65}},
  year         = {{2025}},
}