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Amino Acid Composition of Nanofibrillar Self-assembling Peptide Hydrogels Affects Responses of Periodontal Tissue Cells in Vitro

Overview
Publisher Dove Medical Press
Specialty Biotechnology
Date 2018 Nov 15
PMID 30425485
Citations 6
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Abstract

Background: The regeneration of tissue defects at the interface between soft and hard tissue, eg, in the periodontium, poses a challenge due to the divergent tissue requirements. A class of biomaterials that may support the regeneration at the soft-to-hard tissue interface are self-assembling peptides (SAPs), as their physicochemical and mechanical properties can be rationally designed to meet tissue requirements.

Materials And Methods: In this work, we investigated the effect of two single-component and two complementary β-sheet forming SAP systems on their hydrogel properties such as nanofibrillar architecture, surface charge, and protein adsorption as well as their influence on cell adhesion, morphology, growth, and differentiation.

Results: We showed that these four 11-amino acid SAP (P11-SAP) hydrogels possessed physico-chemical characteristics dependent on their amino acid composition that allowed variabilities in nanofibrillar network architecture, surface charge, and protein adsorption (eg, the single-component systems demonstrated an ~30% higher porosity and an almost 2-fold higher protein adsorption compared with the complementary systems). Cytocompatibility studies revealed similar results for cells cultured on the four P11-SAP hydrogels compared with cells on standard cell culture surfaces. The single-component P11-SAP systems showed a 1.7-fold increase in cell adhesion and cellular growth compared with the complementary P11-SAP systems. Moreover, significantly enhanced osteogenic differentiation of human calvarial osteoblasts was detected for the single-component P11-SAP system hydrogels compared with standard cell cultures.

Conclusion: Thus, single-component system P11-SAP hydrogels can be assessed as suitable scaffolds for periodontal regeneration therapy, as they provide adjustable, extracellular matrix-mimetic nanofibrillar architecture and favorable cellular interaction with periodontal cells.

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References
1.
Kirkham J, Firth A, Vernals D, Boden N, Robinson C, Shore R . Self-assembling peptide scaffolds promote enamel remineralization. J Dent Res. 2007; 86(5):426-30. DOI: 10.1177/154405910708600507. View

2.
Kyle S, Felton S, McPherson M, Aggeli A, Ingham E . Rational molecular design of complementary self-assembling peptide hydrogels. Adv Healthc Mater. 2012; 1(5):640-5. PMC: 3607250. DOI: 10.1002/adhm.201200047. View

3.
Paul J, Hynes R . Multiple fibronectin subunits and their post-translational modifications. J Biol Chem. 1984; 259(21):13477-87. View

4.
Griffin M, Ibrahim A, Seifalian A, Butler P, Kalaskar D, Ferretti P . Chemical group-dependent plasma polymerisation preferentially directs adipose stem cell differentiation towards osteogenic or chondrogenic lineages. Acta Biomater. 2016; 50:450-461. PMC: 5331891. DOI: 10.1016/j.actbio.2016.12.016. View

5.
Sekiguchi K, Hakomori S . Topological arrangement of four functionally distinct domains in hamster plasma fibronectin: a study with combination of S-cyanylation and limited proteolysis. Biochemistry. 1983; 22(6):1415-22. DOI: 10.1021/bi00275a015. View