DOI QR코드

DOI QR Code

Isolation of HIV-1 Pretense Inhibiting Peptide from Thermolysin Hydrolysate of Manila Clam Proteins

  • Lee, Tae-Gee (Department of Marine Food Industry, Namdo Provincial College of Jeonnam) ;
  • Yeum, Dong-Min (Department of Food Processing & Baking, Yangsan College)
  • Published : 2003.06.01

Abstract

A peptide inhibiting HIV-1 pretense was isolated from the hydrolysate of manila clam (Ruditapes philippinarum) proteins digested with thermolysin. The peptide was purified by using membrane filtration, gel permeation chromatography, ion exchange chromatography, and reverse phase HPLC, The amino acid sequence of the peptide was determined to be Ile-Tyr-Glu-Gly. This tetrapeptide sequence exists in some proteins of Physarum polycephalum and Mycobacterium smegmatis. Chemically synthesized Ile-Tyr-Glu-Gly showed the $IC_{50}$/ value of 22.3 $\mu$M.

References

  1. Kohl NE, Emini EA, Schleif WA, Davis LJ, Heimbach JC, Dixon RAF, Scolnick EM, Sigal IS. 1988. Active human immunodeficiency virus protease is required for viral infectivity. Proc Natl Acad Sci USA 85: 4686-4690 https://doi.org/10.1073/pnas.85.13.4686
  2. Mimoto T, Imai J, Tanaka S, Hattori N, Kisanuki S, Akaji K, Kiso Y. 1991. KNI-102, a novel tripeptide HIV protease inhibitor containing allophenylnorstatine as a transition-state mimic. Chem Pharm Bull 39: 3088-3090 https://doi.org/10.1248/cpb.39.3088
  3. Kageyama S, Mimoto T, Murakawa Y, Nomizu M, Ford H Jr, Shirasaka T, Gulnik S, Erickson J, Takada K, Hayashi H, Broder S, Kiso Y, Mitsuya H. 1993. In vitro anti-hwnan immunodeficiency virus (HIV) activities of transition state mimetic HIV protease inhibitors containing allophenylnorstatine. Antimicrob Agents Chemother 37: 810-817 https://doi.org/10.1128/AAC.37.4.810
  4. Stella S, Saddler G, Sarubbi E, Colombo L, Stefanelli S, Denaro M, Selva E. 1991. Isolation of α-MAPI from fermentation broths during a screening program for HIV-1 protease inhibitors. J Antibiotics 44: 1019-1022 https://doi.org/10.7164/antibiotics.44.1019
  5. Ichimura T, Watanabe O, Maruyama S. 1998. Inhibition of HIV-1 protease by water-soluble lignin-like substance from an edible mushroom Fuscoporia obliqua. Biosci Biotechnol Biochem 62: 575-577 https://doi.org/10.1271/bbb.62.575
  6. Ichimura T, Otake T, Mori H, Maruyama S. 1999. HIV-1 protease inhibition and anti-HIV effect of natural and synthetic water-soluble lignin-like substances. Biosci Biotechnol Biochem 63: 2202-2204 https://doi.org/10.1271/bbb.63.2202
  7. Hur JM, Park JG, Park JC, Hyun KH, Lee KY, Miyashiro H, Hattori M. 2002. Inhibition effects of ninety nine Korean plants on human immunodeficiency virus type 1 protease activity. Nutraceuticals & Food 7: 123-127 https://doi.org/10.3746/jfn.2002.7.2.123
  8. Roberts NA, Martin JA, Kinchington D, Broadhurst A V, Craig JC, Duncan IB, Galpin SA, Handa BK, Kay J, Krohn A, Lambert RW, Merrett JH, Mills JS, Parkes KEB, Redshaw S, Ritchie AJ, Taylor DL, Thomas GJ, Machin PJ. 1990. Rational design of peptide-based HIV proteinase inhibitors. Science 248: 358-361 https://doi.org/10.1126/science.2183354
  9. Toh H, Ono M, Saigo K, Miyata T. 1985. Retroviral protease-like sequence in the yeast transposon Ty1. Nature 315:691 https://doi.org/10.1038/315691a0
  10. Pearl LH, Taylor WR. 1987. A structural model for the retroviral proteases. Nature 329: 351-354 https://doi.org/10.1038/329351a0
  11. Seelmeier S, Schmidt H, Turk V, von der Helm K. 1988. Human immunodeficiency virus has an aspartic-type protease that can be inhibited by pepstatin A. Proc Natl Acad Sci USA 85: 6612-6616 https://doi.org/10.1073/pnas.85.18.6612
  12. Matayoshi ED, Wang GT, Krafft GA, Erickson J. 1990. Novel fluorogenic substrates for assaying retroviral proteases by resonance energy transfer. Science 247: 954-958 https://doi.org/10.1126/science.2106161
  13. Richards AD, Roberts R, Dunn BM, Graves MC, Kay J.1989. Effective blocking of HIV-1 proteinase activity by characteristic inhibitors of aspartic proteinases. FEBS Lett 247: 113-117 https://doi.org/10.1016/0014-5793(89)81251-7
  14. Condra JH, Schleif WA, Blahy OM, Gabryelski LJ, Graham DJ, Quintero JC, Rhodes A, Robbins HL, Roth E, Shivaprakash M, Titus D, Yang T, Teppler H, Squires KE, Deutsch PJ, Emini EA. 1995. In vivo emergence of HIV-1 variants resistant to multiple protease inhibitors. Nature 374: 569-571 https://doi.org/10.1038/374569a0
  15. Vandekerckhove J, Weber K. 1978. The amino acid sequence of Physarum actin. Nature 276: 720-721 https://doi.org/10.1038/276720a0
  16. Hase T, Wakabayashi S, Matsubara H, Imai T, Matsumoto T, Tobari J. 1979. Mycobacterium smegmatis ferredoxin. A unique distribution of cysteine residues constructing ironsulfur clusters. FEBS Lett 103: 224-228 https://doi.org/10.1016/0014-5793(79)81332-0
  17. Jacobsen H, Yasargil K, Winslow DL, Craig JC, Krohn A, Duncan IB, Mous J. 1995. Characterization of human immunodeficiency virus type 1 mutants with decreased sensitivity to proteinase inhibitor Ro 31-8959. Virology 206: 527-534 https://doi.org/10.1016/S0042-6822(95)80069-7