2018
DOI: 10.1002/adem.201700961
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Chemically Modified Silk Proteins

Abstract: Silks are of central importance as smart natural biomaterials and are attracting increasing attention for their biomimetic potential due to their sophisticated molecular structure, self‐assembly mechanism, impressive mechanical properties, biocompatibility, and biodegradability. The versatility of silk proteins (SP) allows the chemical modification of silk‐based materials with diverse morphologies under harsh conditions. The chemical modification of amino acids within SP enables the expanded generation of new … Show more

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Cited by 52 publications
(44 citation statements)
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“…Coupling reactions are mainly used to immobilize peptides, molecules and polymers in fiber proteins. Copper-catalyzed azide-alkyne cycloaddition reactions, cyanuric chloride, carbodiimide and glutaraldehyde are very effective coupling agents [58,59]. The amino acid modifications are made through arginine masking, which is used to regulate the surface charge, sulfation/oxidation of tyrosine, which causes the hydrolysis of the fiber protein [58], and azo-modified tyrosine that can be used to install small molecules into fiber protein, resulting in hydrophobic and hydrophilic derivatives [60].…”
Section: Chemical Treatments In Animal Fibersmentioning
confidence: 99%
“…Coupling reactions are mainly used to immobilize peptides, molecules and polymers in fiber proteins. Copper-catalyzed azide-alkyne cycloaddition reactions, cyanuric chloride, carbodiimide and glutaraldehyde are very effective coupling agents [58,59]. The amino acid modifications are made through arginine masking, which is used to regulate the surface charge, sulfation/oxidation of tyrosine, which causes the hydrolysis of the fiber protein [58], and azo-modified tyrosine that can be used to install small molecules into fiber protein, resulting in hydrophobic and hydrophilic derivatives [60].…”
Section: Chemical Treatments In Animal Fibersmentioning
confidence: 99%
“…Silk sutures have been FDA‐approved for use in surgery, and silk materials have been developed as effective extracellular matrix analogs for cell growth and direction . Silk can be chemically modified in a variety of ways to produce materials with additional functionalities, including with azobenzene functional groups, via the tyrosine residues on silk fibroin that can be chemically modified to form azobenzene derivatives on the silk through diazonium coupling ( Figure a) . 5.3% of the amino acids composing silk fibroin are tyrosine, which is distributed through the silk fibroin protein sequence, and this azobenzene postmodified silk fibroin is then referred to as “azosilk” or “optosilk.” This diazonium coupling method, developed by Murphy and Kaplan, can be performed in mild conditions and results in a relatively high conversion of tyrosine residues to azobenzene residues (≈40%) .…”
Section: Interfacing Azo To Bio: An Eye Toward Influencing Living Sysmentioning
confidence: 99%
“…Due to the nature of silk fibroin is degraded by enzymes, controlling the availability and content of enzymes becomes very important in managing the degradation rate [87,76,85]. It has also been reported that degradation behavior can be controlled through chemical modification [88][89][90].…”
Section: Factors Affecting Silk Fibroin Degradationmentioning
confidence: 99%
“…The degradation behavior of silk fibroin is often facilitated by other object responses [111,112], and does not lead to an immunogenic response. In many literatures, degradation of silk fibroin is reported to be enzymatically degraded [113][114][115]89] because of the dominant role of enzymes in the degradation process of silk fibroin. Based on this fact, the enzymatic degradation process can be divided into two steps, namely enzyme adsorption on the substrate surface, and ester bond hydrolysis [115,89].…”
Section: Degradation Behavior By Enzymesmentioning
confidence: 99%
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