02169nas a2200229   4500008004100000022001400041245020700055210006900262260007100331300001400402490000700416520120600423100002401629700002101653700002401674700001701698700002401715700002101739700002501760700002601785856012801811       2010                        eng d  a0022-262300aIsolation, structure, and functional elucidation of a modified pentapeptide, cysteine protease inhibitor (CPI-2081) from streptomyces species 2081 that exhibit inhibitory effect on cancer cell migration0 aIsolation structure and functional elucidation of a modified pen  a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcJUL  a5121-51280 v533 a<p>Cysteine proteases play an important role in cell migration and tumor metastasis. Therefore, their inhibitors are of colossal interest, having potential to be developed as effective antimetastatic drugs for tumor chemotherapy. Traditionally, secondary metabolites from streptomyces show a wide range of diversity with respect to their biological activity and chemical nature. In this article, we have described the characterization of small molecule cysteine protease inhibitor, CPI-2081 (compound 1), a mixture of two novel pentapeptides, compound 1a (736.71 Da), and compound 1b (842.78 Da), isolated from Streptomyces species NCIM2081, following solvent extraction and repeated HPLC based on C18 chemistry, and completely characterized using a variety of both ID and 2D NMR spectroscopy. Further, it was found that nanomolar concentration of compound 1 is able to inhibit papain hydrolytic activity. Also, compound 1 significantly inhibits tumor cell migration at sub cytotoxic concentration, indicating its remarkable potential to be developed as antimetastatic drug, which will make chemotherapy more localized and specific, thereby minimizing the hazardous side effects on normal tissues.</p>1 aSingh, Jay, Prakash1 aTamang, Sudarsan1 aRajamohanan, P., R.1 aJima, N., C.1 aChakraborty, Goutam1 aKundu, Gopal, C.1 aGaikwad, Sushama, M.1 aKhan, Mohammad, Islam  uhttps://library.ncl.res.in/content/isolation-structure-and-functional-elucidation-modified-pentapeptide-cysteine-protease-0