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chymotrypsinpepsin1. H-Tyr-D-Dap-Phe-Lys-NH 2C Ot˝ < 15 min stabile*2. H-Tyr-D-Lys-Phe-Dap-NH 2C Ostabile stabile3. stabile stabileH-Tyr-D-Orn-Phe-Dap-NH 2C O4. stabile stabileH-Tyr-D-Orn-Phe-Lys-NH 2C O5. H-Tyr-D-Lys 2 -Gly-Phe-Dap 5 - NH-CH 2 -CH 2 -NH(CO)NH 2t˝ > 2.5 h stabileC O6. t˝ ~ 2 h stabileH-Tyr-D-Orn 2 -Gly-Phe-Lys 5 - NH-CH 2 -CH 2 -NH(CO)NH 2C O7. t˝ > 2.5 h stabileH-Tyr-D-Lys 2 -Gly-Phe-Dap 5 - Val-Val-Gly-NH-CH 2 -CH 2 -NH(CO)NH 2C O8. H-Tyr-D-Ala-Gly-Phe-Glu-Val-Val-Gly-NH-CH 2 -CH 2 -NH(CO)NH 2 t˝ ~ 15 min t˝ ~ 1 h9. t˝ < 15 min t˝ < 1 hH-Tyr-D-Ala-Gly-Phe-Gln-Val-Val-Gly-NH-CH 2 -CH 2 -NH(CO)NH 2Fig. 2. Proteolytic stability of peptides 1-9 and localization of the peptide bonds hydrolyzedby chymotrypsin and pepsin. The peptide bonds hydrolyzed by chymotrypsin and pepsin areindicated by black and gray arrows, respectively; *“stable”(stabile) means that nodegradation products were observed even after 2.5 h of incubation with the protease;t values mean t 1/2 .References1. Szewczuk, Z., Gibbs, B.F., Yue, S-Y., Purisima, E.O., Konishi, Y. Biochemistry 31, 9132-9140(1992).2. Szewczuk, Z., Wilczyński, A., Dyba, M., Petry, I., Siemion, I.Z., Wieczorek, Z. Peptides 21, 1849-1858 (2000).3. Filip, K., Oleszczuk, M., Pawlak, D., Wojcik, J., Chung, N.N., Schiller, P.W., Izdebski, J. J. PeptideSci. 9, 649-657 (2003).441