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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: [email protected])
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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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