Submitted to: American Chemical Society National Meeting
Publication Type: Abstract Only
Publication Acceptance Date: 6/1/2004
Publication Date: 8/23/2004
Citation: Barone, J.R., Schmidt, W.F. 2004. Physical modification of the keratin network to produce new polymer blends [abstract]. American Chemical Society National Meeting. Philadelphia, PA, Aug. 23-27, 2004. Paper No. CELL 78. Interpretive Summary:
Technical Abstract: Biological evolution has demonstrated that keratin persists in hair and feathers, hooves, and horns because it is tough, strong, and lightweight. The origin of the unusual properties of keratin is the high amount of the amino acid cysteine (C) that it contains relative to other proteins. Cysteine has the ability to form inter-molecular bonds, known as cystine bonds or cross-links, with other cysteine molecules. The cross-linked network imparts toughness to the protein. Analysis of the amino acid sequence of keratin derived from poultry feathers shows that the amount of the -OH containing amino acids serine (S), threonine (T), and tyrosine (Y) is high relative to the C content, resulting in a ratio of [-OH]/[C]=(S+T+Y)/C=3. A process developed in this laboratory exploits this unique feature of feather keratin to make polymer blends that can have a range of properties depending on the mole percentage of -OH in the second phase.