Elastin-based silver-binding proteins with antimicrobial capabilities

Elastin-based biomaterials have gained popularity in tissue engineering and regenerative medicine due to their well-defined chemical and physical properties. In particular, elastin-based materials have tremendous potential as wound dressing materials due to their elasticity and biocompatibility. Yet...

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Main Author: Truong, Thi Hong Anh
Other Authors: School of Materials Science & Engineering
Format: Theses and Dissertations
Language:English
Published: 2013
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Online Access:https://hdl.handle.net/10356/54874
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-548742023-03-04T16:48:27Z Elastin-based silver-binding proteins with antimicrobial capabilities Truong, Thi Hong Anh School of Materials Science & Engineering Fong Men Wei, Eileen DRNTU::Science::Biological sciences::Microbiology::Bacteria DRNTU::Science::Chemistry::Inorganic chemistry::Metals DRNTU::Science::Medicine::Biomedical engineering Elastin-based biomaterials have gained popularity in tissue engineering and regenerative medicine due to their well-defined chemical and physical properties. In particular, elastin-based materials have tremendous potential as wound dressing materials due to their elasticity and biocompatibility. Yet, elastin-based materials with antimicrobial properties have not been developed to date. In this work, we constructed novel elastin fusion proteins bearing AG3 silver-binding motifs (GPG-AG3) and their thin films. In the presence of NaCl, GPG-AG3 proteins self-assembled to form aggregates with diameters of about 100 nm. Further incubation in silver nitrate yielded silver nanoparticles on the surfaces of the protein particles and thin films. The silver nanoparticles obtained in our work had diameters of 20 – 25 nm from protein aggregates solution and 471 nm ± 178 nm on protein films. The effect of varying NaCl concentrations and pH on the size and morphology of silver particles was examined. The nucleated silver nanoparticles exhibited antibacterial properties when tested against gram-negative E. coli. In both 2xYT agar plates and culture media containing 20 g/mL of synthesized silver, or silver-coated protein films, E. coli growth was completely inhibited. Silver-coated GPG-AG3 films were able to support mammalian cell growth for up to 3 days, but displayed significant cytotoxicity after 7 days. In summary, we have developed GPG-AG3 proteins with the ability to nucleate antibacterial silver particles. In our future work, we will focus on the fabrication of silver nanowires using GPG-AG3 templates. The antibacterial properties and cytotoxicity of silver nanowires will also be examined in vitro. MASTER OF ENGINEERING (MSE) 2013-10-14T00:54:03Z 2013-10-14T00:54:03Z 2013 2013 Thesis Truong, T. H. A. (2013). Elastin-based silver-binding proteins with antimicrobial capabilities. Master’s thesis, Nanyang Technological University, Singapore. https://hdl.handle.net/10356/54874 10.32657/10356/54874 en 62 p. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic DRNTU::Science::Biological sciences::Microbiology::Bacteria
DRNTU::Science::Chemistry::Inorganic chemistry::Metals
DRNTU::Science::Medicine::Biomedical engineering
spellingShingle DRNTU::Science::Biological sciences::Microbiology::Bacteria
DRNTU::Science::Chemistry::Inorganic chemistry::Metals
DRNTU::Science::Medicine::Biomedical engineering
Truong, Thi Hong Anh
Elastin-based silver-binding proteins with antimicrobial capabilities
description Elastin-based biomaterials have gained popularity in tissue engineering and regenerative medicine due to their well-defined chemical and physical properties. In particular, elastin-based materials have tremendous potential as wound dressing materials due to their elasticity and biocompatibility. Yet, elastin-based materials with antimicrobial properties have not been developed to date. In this work, we constructed novel elastin fusion proteins bearing AG3 silver-binding motifs (GPG-AG3) and their thin films. In the presence of NaCl, GPG-AG3 proteins self-assembled to form aggregates with diameters of about 100 nm. Further incubation in silver nitrate yielded silver nanoparticles on the surfaces of the protein particles and thin films. The silver nanoparticles obtained in our work had diameters of 20 – 25 nm from protein aggregates solution and 471 nm ± 178 nm on protein films. The effect of varying NaCl concentrations and pH on the size and morphology of silver particles was examined. The nucleated silver nanoparticles exhibited antibacterial properties when tested against gram-negative E. coli. In both 2xYT agar plates and culture media containing 20 g/mL of synthesized silver, or silver-coated protein films, E. coli growth was completely inhibited. Silver-coated GPG-AG3 films were able to support mammalian cell growth for up to 3 days, but displayed significant cytotoxicity after 7 days. In summary, we have developed GPG-AG3 proteins with the ability to nucleate antibacterial silver particles. In our future work, we will focus on the fabrication of silver nanowires using GPG-AG3 templates. The antibacterial properties and cytotoxicity of silver nanowires will also be examined in vitro.
author2 School of Materials Science & Engineering
author_facet School of Materials Science & Engineering
Truong, Thi Hong Anh
format Theses and Dissertations
author Truong, Thi Hong Anh
author_sort Truong, Thi Hong Anh
title Elastin-based silver-binding proteins with antimicrobial capabilities
title_short Elastin-based silver-binding proteins with antimicrobial capabilities
title_full Elastin-based silver-binding proteins with antimicrobial capabilities
title_fullStr Elastin-based silver-binding proteins with antimicrobial capabilities
title_full_unstemmed Elastin-based silver-binding proteins with antimicrobial capabilities
title_sort elastin-based silver-binding proteins with antimicrobial capabilities
publishDate 2013
url https://hdl.handle.net/10356/54874
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