Biomaterials, Biodegradables and Biomimetics Research Group

Conference Abstract -ISI Web of Science Indexed

Exploring Silk Based Biomaterials Functionalized with Antimicrobial Peptides to Prevent Surgical Site Infections


Surgical site infections (SSI) often occur after invasive surgery, which is as a serious health problem, making it important to develop new biomaterials to prevent infections. Spider silk is a natural biomaterial with excellent biocompatibility, low immunogenicity and controllable biodegradability. Through recombinant DNA technology, spider silk-based materials can be bioengineered and functionalized with antimicrobial (AM) peptides 1. The aim of this study is to develop new materials by combining spider silk chimeric proteins with AM properties and silk fibroin extracted from Bombyx mori cocoons to prevent microbial infection. Here, spider silk domains derived from the dragline sequence of the spider Nephila clavipes (6 mer and 15 mer) were fused with the AM peptides Hepcidin and Human Neutrophil peptide 1 (HNP1). The spider silk domain maintained its self-assembly features allowing the formation of beta-sheets to lock in structures without any chemical cross-linking. The AM properties of the developed chimeric proteins showed that 6 mer + HNP1 protein had a broad microbicidal activity against pathogens. The 6 mer + HNP-1 protein was then assembled with different percentages of silk fibroin into multifunctional films. In vitro cell studies with a human fibroblasts cell line (MRC5) showed nontoxic and cytocompatible behavior of the films. The positive cellular response, together with structural properties, suggests that this new fusion protein plus silk fibroin may be good candidates as multifunctional materials to prevent SSI.

Acknowledgments: This work was supported by the Portuguese Foundation for Science and Technology under the project PTDC/ BBB-BIO/0827/2012.


1. Gomes S, et al. Biomaterials 2011, 32, 4255.

Tissue Engineering Part A.
Mary Ann Liebert, Inc.
Antimicrobial peptides, cytoxicity, protein films, Spider dragline protein
Open Access
Peer Reviewed
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