Elastase recognition sequences

Cotton is a much weaker ion exchanger than the DEAE or SP supports described earlier. In its underivatized state, cotton is hydrophilic and nonionic. We have confirmed this by packing underivatized cotton into an empty HPLC column, then introducing proteins. Elastase did not bind, even under weak buffer conditions. However, when cotton was derivatized with an elastase-recognition-sequence, elastase was retained. 

Figure 4A Structure of peptido-cellulose conjugate oriented with the amino-terminal portion of the sequence anchored to carboxymethylcellulose allowing solution solvation for binding of the elastase recognition sequence illustrating active site uptake of elastase, B Structure depicting arginine salt bridge from the protein surface with carboxylate group of carboxymethylcellulose.

Edwards, J.V., Batiste, S.L., Gibbins, B.M., Goheen, S.C. Synthesis and activity of NH2- and COOH-terminal elastase recognition sequences on cotton. (In press)... 

Figure 3 (A) Design of cellulose conjugates ofelastase inhibitors based on the tripeptide recognition sequence (B) ofelastase. Representative structure of the peptide on cellulose. (C) Illustration of modified cotton gauze to selectively bind elastase preventing degradation of growth factors andfibronectin.

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