Self-consistent field theory for the interactions between keratin intermediate filaments.

Authors:
Anna Akinshina
Anna Akinshina
The University of Manchester
United Kingdom
Patrick B Warren
Patrick B Warren
Unilever R&D Port Sunlight
Birkenhead | United Kingdom
Massimo G Noro
Massimo G Noro
King's College London
United Kingdom

BMC Biophys 2013 Sep 5;6(1):12. Epub 2013 Sep 5.

Unilever R&D Port Sunlight, Quarry Road East, Bebington, Wirral, CH63 3JW, UK.

Background: Keratins are important structural proteins found in skin, hair and nails. Keratin Intermediate Filaments are major components of corneocytes, nonviable horny cells of the Stratum Corneum, the outermost layer of skin. It is considered that interactions between unstructured domains of Keratin Intermediate Filaments are the key factor in maintaining the elasticity of the skin.

Results: We have developed a model for the interactions between keratin intermediate filaments based on self-consistent field theory. The intermediate filaments are represented by charged surfaces, and the disordered terminal domains of the keratins are represented by charged heteropolymers grafted to these surfaces. We estimate the system is close to a charge compensation point where the heteropolymer grafting density is matched to the surface charge density. Using a protein model with amino acid resolution for the terminal domains, we find that the terminal chains can mediate a weak attraction between the keratin surfaces. The origin of the attraction is a combination of bridging and electrostatics. The attraction disappears when the system moves away from the charge compensation point, or when excess small ions and/or NMF-representing free amino acids are added.

Conclusions: These results are in concordance with experimental observations, and support the idea that the interaction between keratin filaments, and ultimately in part the elastic properties of the keratin-containing tissue, is controlled by a combination of the physico-chemical properties of the disordered terminal domains and the composition of the medium in the inter-filament region.

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http://dx.doi.org/10.1186/2046-1682-6-12DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3848802PMC
September 2013
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