Fisheries and Aquatic Sciences

The Korean Society of Fisheries and Aquatic Science (한국수산과학회)
권호 표지
DOI QR코드

DOI QR Code

Peptide Inhibitor for Human Immunodeficiency Virus Type 1 (HIV-1) Protease from a Thermolysin Hydrolysate of Oyster Proteins

  • Lee, Tae-Gee (Department of Hotel Culinary & Nurition, Jeonnam Provincial College)
  • Received : 2009.11.23
  • 심사 : 2010.03.03
  • 발행 : 2010.03.31
Download PDF
⟨ Previous Next ⟩

초록

A peptide that inhibits HIV-1 protease was isolated from a hydrolysate of oyster (Crassostrea gigas) proteins digested with thermolysin. The peptide was using membrane filtration, gel permeation chromatography, ion exchange chromatography, and reverse-phase high performance liquid chromatography. Amino acid sequence of the peptide was determined to be Val-Phe-Glu-Leu. Chemically synthesized Val-Phe-Glu-Leu showed an $IC_{50}$ value of 106 ${\mu}M$.

키워드

참고문헌

  1. Achour A, Lachgar A, Astgen A, Chams V, Bizzini B, Tapiero H and Zagury D. 1997. Potentialization of IL-2 effects on immune cells by oyster extract (JCOE) in normal and HIV-infected individuals. Biomed Pharmacother 51, 427-429. https://doi.org/10.1016/S0753-3322(97)82320-7
  2. Chin KP, Lowe MA, Tong MJ and Koehler AL. 1987. Vibrio vulnificus infection after raw oyster ingestion in a patient with liver disease and acquired immune deficiency syndrome-related complex. Gastroenterology 92, 796-799. https://doi.org/10.1016/0016-5085(87)90035-7
  3. Huddleston JA and Brownlee Go. 1982. The sequence of the nucleoprotein gene of human influenza A virus, strain A/NT/60/68. Nucleic Acids Res 10, 1029-1038. https://doi.org/10.1093/nar/10.3.1029
  4. Hur JM, Park JG, Park JC, Hyun KH, Lee KY, Miyashiro H and 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
  5. Ichimura T, Otake T, Mori H and 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
  6. Ichimura T, Watanabe O and Maruyama S. 1998. Inhibition of HIV-1 protease by water-soluble lignin-like substance from an edible mushroom Fuscoporiaobliqua. Biosci Biotechnol Biochem 62, 575-577. https://doi.org/10.1271/bbb.62.575
  7. 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 and Mitsuya H. 1993. In vitro anti-human immunodeficiency virus (HIV) activities of transition state mimeric HIV protease inhibitors containing allophenylnorstatine. Antimicrob Agents Chemother 37, 810-817. https://doi.org/10.1128/AAC.37.4.810
  8. Kohl NE, Emini EA, Schleif WA, Davis LJ, Heimbach JC, Dixon RAF, Scolnick EM and 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
  9. Matayoshi ED, Wang GT, Krafft GA and 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
  10. Palmenberg AC, Kirby EM, Janda MR, Darke NL, Duke GM, Potratz KF and Collett MS. 1984. The nucleotide and deduced amino acid sequences of the encephalomyocarditis viral polyprotein coding region. Nucleic Acids Res 12, 2969-2985. https://doi.org/10.1093/nar/12.6.2969
  11. Pearl LH and Taylor WR. 1987. A structural model for the retroviral proteases. Nature 329, 351-354. https://doi.org/10.1038/329351a0
  12. Richards AD, Roberts R, Dunn BM, Graves MC and 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
  13. Roberts NA, Martin JA, Kinchington D, Broadhurst AV, Craig JC, Duncan IB, Galpin SA, Handa BK, Kay J, Krohn A, Lambert RW, Merrett JR, Mills JS, Parkes KEB, Redshaw S, Ritchie AJ, Taylor DL, Thomas GJ and Machin PJ. 1990. Rational design of peptide-based HIV proteinase inhibitors. Science 248, 358-361. https://doi.org/10.1126/science.2183354
  14. Ross EE, Guyer L, Varnes J and Rodrick G. 1994. Vibrio vulnifieus and molluscan shellfish: The necessity of education for high-risk individuals. J Am Diet Assoc 94, 312-314. https://doi.org/10.1016/0002-8223(94)90375-1
  15. Seelmeier S, Schmidt H, Turk V and 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
  16. Stella S, Saddler G, Sarubbi E, Colombo L, Stefanelli S, Denaro M, Selva E. 1991. Isolation of -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
  17. Toh H, Ono M, Saigo K and Miyata T. 1985. Retroviral protease-like sequence in the yeast transposon Ty 1. Nature 315, 691.
  18. Yoshikawa T, Naito Y, Masui K, Fujii T, Boku Y, Nakagawa S, Yoshida N and Kondo M. 1997. Free radical-scavenging activity of Crassostera gigas extract (JCOE). Biomed & Pharmacother 51, 328-332. https://doi.org/10.1016/S0753-3322(97)88050-X