Jump to main content
Jump to site search

Issue 6, 2016
Previous Article Next Article

Mechanical behavior comparison of spider and silkworm silks using molecular dynamics at atomic scale

Author affiliations

Abstract

Spider and silkworm silk proteins have received much attention owing to their inherent structural stability, biodegradability, and biocompatibility. These silk protein materials have various mechanical characteristics such as elastic modulus, ultimate strength and fracture toughness. While the considerable mechanical characteristics of the core crystalline regions of spider silk proteins at the atomistic scale have been investigated through several experimental techniques and computational studies, there is a lack of comparison between spider and silkworm fibroins in the atomistic scale. In this study, we investigated the differences between the mechanical characteristics of spider and silkworm fibroin structures by applying molecular dynamics and steered molecular dynamics. We found that serine amino acids in silkworm fibroins not only increased the number of hydrogen bonds, but also altered their structural characteristics and mechanical properties.

Graphical abstract: Mechanical behavior comparison of spider and silkworm silks using molecular dynamics at atomic scale

Back to tab navigation

Publication details

The article was received on 07 Nov 2015, accepted on 12 Jan 2016 and first published on 15 Jan 2016


Article type: Paper
DOI: 10.1039/C5CP06809F
Citation: Phys. Chem. Chem. Phys., 2016,18, 4814-4821
  •   Request permissions

    Mechanical behavior comparison of spider and silkworm silks using molecular dynamics at atomic scale

    M. Lee, J. Kwon and S. Na, Phys. Chem. Chem. Phys., 2016, 18, 4814
    DOI: 10.1039/C5CP06809F

Search articles by author

Spotlight

Advertisements