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Novelcross-Linking Agents for Hydrogelation of Biological Polymers

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Abstract:

Cross-linking agents are useful for investigating the biological functions of biological polymers. Here we would like to report the preparation of a 4-hydroxyphenyldimethyl-sulfoniummethlysulfate (DSP) activated cross-linker that can cross-link proteins as a novel cross-linking agents. By using this cross-linker, gelatin can be cross-linked both in the sol-state at 40 degree centigrade and in the gel-state at 2 degree centigrade. The chemically cross-linked gelatin gels by DSP-activated esters that were obtained in gel-state and sol-state at a gelatin concentration greater than 1percent and 5percent, respectively. The fixed conformation of the folding structure seen with this physical cross-linking system is thought to result from the structure of the native protein. In addition, the urea concentration dependence of the swelling ration indicates that the hydrogen bonds are much more stable in the gel prepared from the gel state of gelatin than those in the gel prepared from the sol state of gelatin. As result, these novel bifunctional agents of the hydrogelation of biological polymers are expected application in studying intermolecular interaction.

Keywords: Cross Linking Agents; Hydrogelation; amino acid; gelatin

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/0929866013409481

Publication date: June 1, 2001

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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