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Molecular Mobility in Keratin-Rich Materials Monitored by Nuclear Magnetic Resonance : A Tool for the Evaluation of Structure-Giving Properties

Gunnarsson, Maria LU ; Larsson, Sandra LU ; Malak, Monika ; Ericson, Marica B. ; Topgaard, Daniel LU and Sparr, Emma LU (2023) In Biomacromolecules 24(6). p.2661-2673
Abstract

Keratins are structural proteins that are abundant in human skin, nails, and hair, where they provide mechanical strength. In the present study, we investigate the molecular mobilities and structures of three keratin-rich materials with clearly different mechanical properties: nails, stratum corneum (upper layer of epidermis), and keratinocytes (from lower layer of epidermis). We use solid-state NMR on natural-abundance 13C to characterize small changes in molecular dynamics in these biological materials with close to atomistic resolution. One strong advantage of this method is that it detects small fractions of mobile components in a molecularly complex material while it simultaneously gives information on the rigid components in the... (More)

Keratins are structural proteins that are abundant in human skin, nails, and hair, where they provide mechanical strength. In the present study, we investigate the molecular mobilities and structures of three keratin-rich materials with clearly different mechanical properties: nails, stratum corneum (upper layer of epidermis), and keratinocytes (from lower layer of epidermis). We use solid-state NMR on natural-abundance 13C to characterize small changes in molecular dynamics in these biological materials with close to atomistic resolution. One strong advantage of this method is that it detects small fractions of mobile components in a molecularly complex material while it simultaneously gives information on the rigid components in the very same sample. The molecular mobility can be linked to mechanical material properties in different conditions, including hydration or exposure to osmolytes or organic solvents. Importantly, the study revealed that the response to both hydration and addition of urea is clearly different for the nail keratin compared to the stratum corneum keratin. The comparative examination of these materials may provide a better understanding of skin diseases originating from keratin malfunction and contributes to the design and development of new materials.

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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biomacromolecules
volume
24
issue
6
pages
13 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • pmid:37199647
  • scopus:85160713744
ISSN
1525-7797
DOI
10.1021/acs.biomac.3c00131
language
English
LU publication?
yes
id
16d8995f-7fff-491b-9f9f-ce0bf375c483
date added to LUP
2023-08-28 14:23:27
date last changed
2024-04-20 02:05:57
@article{16d8995f-7fff-491b-9f9f-ce0bf375c483,
  abstract     = {{<p>Keratins are structural proteins that are abundant in human skin, nails, and hair, where they provide mechanical strength. In the present study, we investigate the molecular mobilities and structures of three keratin-rich materials with clearly different mechanical properties: nails, stratum corneum (upper layer of epidermis), and keratinocytes (from lower layer of epidermis). We use solid-state NMR on natural-abundance 13C to characterize small changes in molecular dynamics in these biological materials with close to atomistic resolution. One strong advantage of this method is that it detects small fractions of mobile components in a molecularly complex material while it simultaneously gives information on the rigid components in the very same sample. The molecular mobility can be linked to mechanical material properties in different conditions, including hydration or exposure to osmolytes or organic solvents. Importantly, the study revealed that the response to both hydration and addition of urea is clearly different for the nail keratin compared to the stratum corneum keratin. The comparative examination of these materials may provide a better understanding of skin diseases originating from keratin malfunction and contributes to the design and development of new materials.</p>}},
  author       = {{Gunnarsson, Maria and Larsson, Sandra and Malak, Monika and Ericson, Marica B. and Topgaard, Daniel and Sparr, Emma}},
  issn         = {{1525-7797}},
  language     = {{eng}},
  month        = {{06}},
  number       = {{6}},
  pages        = {{2661--2673}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Biomacromolecules}},
  title        = {{Molecular Mobility in Keratin-Rich Materials Monitored by Nuclear Magnetic Resonance : A Tool for the Evaluation of Structure-Giving Properties}},
  url          = {{http://dx.doi.org/10.1021/acs.biomac.3c00131}},
  doi          = {{10.1021/acs.biomac.3c00131}},
  volume       = {{24}},
  year         = {{2023}},
}