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Crosslinking and Self-Crosslinking in Keratin Fibers

  • K. Ziegler
Chapter

Abstract

In recent years much attention has been directed toward the elucidation of a variety of bonds and interactions that exist between the protein molecules in wool fibers. It is argued that these forces are responsible for maintaining the stable structure of the fiber and that many of its mechanical and chemical properties can be explained by them. One of the prominent features of wool is the complete insolubility in polar solvents which results from crosslinking. The most thoroughly characterized crosslinks in wool are the covalent disulfide bonds which stem from the incorporation of cystine residues. As in other proteins, a number of noncovalent bonds also occur in sufficient quantities as to have additional effects. It was observed in the course of wool processing that disulfide bonds tend to become labile, and therefore much research work was aimed at the introduction of additional crosslinks or the replacement of some already present by those more able to resist chemical attack. “Crosslinks” are here defined as those covalent bonds which join two neighboring peptide chains through functional amino acid side-chain groups being sufficiently close to participate in a crosslinkage. When additional crosslinks are to be introduced into the molecule it is now considered useful, for the sake of clarification, to differentiate further with regard to the mode of reaction, that is, to indicate whether crosslinking has been achieved (a) by the incorporation of a foreign residue of the reagent applied, or (b) by coupling of protein side-chain groups by a special treatment with agents which themselves do not become part of the molecule. The latter type of reaction is termed a “self-crosslinking” reaction, the former being referred to as “crosslinking.”

Keywords

Crosslinking Reaction Wool Fiber Wool Textile Solubility Test Noncovalent Bond 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • K. Ziegler
    • 1
  1. 1.Deutsches WollforschungsinstitutAachenWest Germany

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