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Molecular Dynamics Investigation of Self-Association of Synthetic Collagen and Spider Silk Composite System for Biomaterial Applications

Published online by Cambridge University Press:  03 January 2020

Atul Rawal ,
Kristen L. Rhinehardt  and
Ram V. Mohan
Atul Rawal*
Affiliation:
Joint School of Nanoscience & Nanoengineering, North Carolina A&T State University, Greensboro, NC 27401, U.S.A.
Kristen L. Rhinehardt
Affiliation:
Computational Science & Engineering, North Carolina A&T State University, Greensboro, NC27401 U.S.A.
Ram V. Mohan
Affiliation:
Joint School of Nanoscience & Nanoengineering, North Carolina A&T State University, Greensboro, NC 27401, U.S.A.
*
*(Email: arawal@aggies.ncat.edu)
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Abstract

Bio-composite materials with optimal mechanical and structural properties and capability of cell differentiation are crucial for tissue engineering. Synthetic collagen proteins with lengths of approximately 10 nanometers, along with natural spider silk proteins provide an opportunity for development of an optimal biomaterial for scaffolding applications in tissue engineering. This combines unique mechanical, structural and biological properties of two of the nature’s best polymer proteins, albeit the collagen used in the present work is of the synthetic nature, it mimics the properties and advantages of natural collagen itself. In the present work, we study the binding capability of these proteins at a molecular level via molecular dynamics modeling. Spider silk and synthetic collagen protein molecular models in biophysical saline conditions under standard pressure and temperature are investigated to understand if natural binding occurs between the two without any other external factors. An initial minimum separation of 10 angstroms between the proteins was used. Binding was observed between the two proteins throughout the dynamic simulation of 100 nanoseconds. The radius of gyration and minimum distance between the proteins shows a decreasing separation between the two proteins until a stable distance of 2.5 nanometers and 0.2 nanometers respectively, is achieved. Binding is further observed between the proteins via formation of strong and stable hydrogen bonds. A hydrogen bond between collagen Proline-31 and silk Serine-96 was observed to be the most stable and frequent bond between the single collagen and silk system. Results clearly indicate a self-assembly behavior of these two systems illustrating their potential as a biomaterial for tissue engineering.

Keywords

biomaterialsyntheticself-assemblymolecular
Type
Articles
Information
MRS Advances , Volume 5 , Issue 16: Soft Materials and Biomaterials , 2020 , pp. 797 - 804
Copyright
Copyright © Materials Research Society 2020

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References

REFERENCES

O’Brien, F. J., Materials Today 14 (3), 88-95 (2011).CrossRefGoogle Scholar
Dong, C. and Lv, Y., Polymers (Basel) 8 (2) (2016).CrossRefGoogle Scholar
Kaur, P. J., The City University of New York, 2017.Google Scholar
LI, Y., Dissertation The University of Florida, 2009.Google Scholar
Parenteau-Bareil, R., Gauvin, R. and Berthod, F., Materials 3 (3), 1863-1887 (2010).CrossRefGoogle Scholar
Miranda-Nieves, D. and Chaikof, E. L., ACS Biomaterials Science & Engineering 3 (5), 694-711 (2016).CrossRefGoogle Scholar
Ulery, B. D., Nair, L. S. and Laurencin, C. T., J Polym Sci B Polym Phys 49 (12), 832-864 (2011).CrossRefGoogle Scholar
Kotch, F. W. and Raines, R. T., Proceedings of National Academy of Sciences 103 (9), 9 (2006).CrossRefGoogle Scholar
Persikov, A. V., Ramshaw, J. A. and Brodsky, B., J Biol Chem 280 (19), 19343-19349 (2005).CrossRefGoogle Scholar
Persikov, A. V., Ramshaw, J. A., Kirkpatrick, A. and Brodsky, B., J Mol Biol 316 (2), 385-394 (2002).CrossRefGoogle Scholar
Kasoju, N. and Bora, U., Adv Healthc Mater 1 (4), 393-412 (2012).CrossRefGoogle Scholar
Wlodarczyk-Biegun, M. K. and Del Campo, A., Biomaterials 134, 180-201 (2017).CrossRefGoogle Scholar
Sun, K., Li, R., Jiang, W., Sun, Y. and Li, H., Biochem Biophys Res Commun 477 (4), 1085-1091 (2016).CrossRefGoogle Scholar
Wang, J., Yang, Q., Cheng, N., Tao, X., Zhang, Z., Sun, X. and Zhang, Q., Mater Sci Eng C Mater Biol Appl 61, 705-711 (2016).CrossRefGoogle Scholar
Xu, Y., Zhang, Z., Chen, X., Li, R., Li, D. and Feng, S., PLoS One 11 (1), e0147184 (2016).CrossRefGoogle Scholar
Zhu, B., Li, W., Lewis, R. V., Segre, C. U. and Wang, R., Biomacromolecules 16 (1), 202-213 (2015).CrossRefGoogle Scholar
Rhinehardt, K. L., Mohan, R. V., Srinivas, M. and Kelkar, A. D., International Journal of Bioscience, Biochemistry and Bioinformatics, 639-642 (2013).CrossRefGoogle Scholar
Allen, M. P., in Compuatational Soft Matter : From Synthetic Polymers to Proteins (John Von Neumann Institute for Computing, Julich, 2004), Vol. 23.Google Scholar
Tolman, R. C., The Principles of Statistical Mechanics (Oxford University Press England, 1938).Google Scholar
Wang, J., Cieplak, P. and Kollman, P. A., Journal of Computational Chemistry 21 (12), 1049-1074 (2000).3.0.CO;2-F>CrossRefGoogle Scholar
DePaul, A. J., Thompson, E. J., Patel, S. S., Haldeman, K. and Sorin, E. J., Nucleic Acids Res 38 (14), 4856-4867 (2010).CrossRefGoogle Scholar
Sorin, E. J. and Pande, V. S., Biophys J 88 (4), 2472-2493 (2005).CrossRefGoogle Scholar
Maier, J. A., Martinez, C., Kasavajhala, K., Wickstrom, L., Hauser, K. E. and Simmerling, C., J Chem Theory Comput 11 (8), 3696-3713 (2015).CrossRefGoogle Scholar
Berendsen, H. J. C.., Spoel, D. v. d.. and Drunen, R. v.., Computer Physics Communications 91, 13 (1995).CrossRefGoogle Scholar
Schrodinger, LLC, (2015).Google Scholar
Humphrey, W., Dalke, A. and Schulten, K., Journal of Molecular Graphics 14 (1), 33-38 (1996).CrossRefGoogle Scholar
Berendsen, H. J. C., Postma, J. P. M., van Gunsteren, W. F. and Hermans, J., in Intermolecular Forces (1981), pp. 331-342.CrossRefGoogle Scholar
Askarieh, G., Hedhammar, M., Nordling, K., Saenz, A., Casals, C., Rising, A., Johansson, J. and Knight, S. D., Nature 465 (7295), 236-238 (2010).CrossRefGoogle Scholar
Kramer, R. Z.., Bella, J.., Mayville, P.., Brodsky, B.. and Berman, H. M.., Nature Structural Biology 6 (5), 4 (1999).Google Scholar
Rawal, A. R., Mohan, K.L., , R.V. , presented at the American Society of Mechanical Engineers: Nanoengineering for Medicine and Biology Los Angeles, CA. , 2018 (unpublished).Google Scholar