p-NN'-phenylenebismaleimide acts as a specific cross-linking agent for F-actin, joining subunits of the same long-pitched helix without introducing structural strain.
Covalent cross-links can be inserted between the subunits of F-actin by using p-NN'-phenylenebismaleimide. Cross-linking reaches its maximum value when one molecule of reagent has reacted with each actin subunit. p-NN'-Phenylenebismaleimide reacts initially with a cysteine residue on one subunit, the slower cross-linking reaction involving a lysine residue on a neighbouring subunit. Hydrolysis of the actin-bound reagent limits the extent of cross-linking. Quantitative analysis of the amounts of cross-linked oligomers seen on polyacrylamide gels containing sodium dodecyl sulphate suggests that neither the binding of the reagent to actin nor the formation of cross-links introduces strain into the structure. The cross-links do not join together different F-actin filaments, and evidence is presented that suggests that the cross-links join subunits of the same long-pitched helix.
Knight et al. (Fri,) conducted a other in F-actin cross-linking. p-NN'-phenylenebismaleimide was evaluated on F-actin cross-linking. p-NN'-phenylenebismaleimide acts as a specific cross-linking agent for F-actin, joining subunits of the same long-pitched helix without introducing structural strain.
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