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Generated: October 22, 2017

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Title:Methods for inhibition of membrane-fusion-associated events, including Hepatitis B virus transmission
Abstract: The present invention relates to peptides which exhibit potent anti-viral activity. In particular, the invention relates to methods of using such peptides as inhibitory of hepatitis B virus ("HepB") transmission to uninfected cells. The peptides used in the methods of the invention are homologs of the DP-178 and DP-107 peptides, peptides corresponding to amino acid residues 638 to 673, and to amino acid residues 558 to 595, respectively, of the HIV-1.sub.LAI transmembrane protein (TM) gp41.
Inventor(s): Barney; Shawn O'Lin (Cary, NC), Lambert; Dennis Michael (Cary, NC), Petteway; Stephen Robert (Cary, NC)
Assignee: Trimeris, Inc. (Durham, NC)
Filing Date:Jun 07, 1995
Application Number:08/487,355
Claims:1. A method for the inhibition of transmission of a hepatitis B virus to a cell, comprising contacting the virus, in the presence of the cell, with an effective concentration of a peptide having the formula: X-PLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNSQSP-Z; X-PLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGT-Z; X-LLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGTT-Z; X-LVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGTTV-Z; X-LQAGFFLLTRILTIPQSLDSWWTSLNGLGGTTVCL-Z; X-QAGFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLG-Z; X-AGFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQ-Z; X-GFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQN-Z; X-FFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNS-Z; X-FLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNSQ-Z; X-LLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNSQS-Z; X-PGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLEPGSSTTSTGPCRTCMTT-Z, X-PGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGML-Z; X-GYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLP-Z X-YRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVC-Z; X-RWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVC-Z; X-WMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCP-Z; X-MCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPI-Z; X-CLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLI-Z; X-LRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIP-Z; X-RRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPG-Z; X-RFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGS-Z; X-FIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSS-Z; IIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSST-Z X-IFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTT-Z: X-FLFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTS-Z: X-LFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTST-Z: X-FILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTG-Z; X-ILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGP-Z: X-LLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPC-Z; X-LLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCR-Z; X-LCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCRT-Z; X-CLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCRTC-Z; X-LIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCRTCM-Z; or X-IFLLVLLDYQGMLPVCPLIPGSSTTSTGPCRTCMT-Z; (SEQ ID NOS: 239-273, respectively) in which: amino acid residues are presented by the single-letter code; X comprises an amino group, an acetyl group, a 9-fluorenylmethoxy-carbonyl group, a hydrophobic group, or a macromolecule carrier group; Z comprises a carboxyl group, an amido group, a hydrophobic group, or a macromolecular carrier group for an effective period of time so that infection of the cell by the virus is inhibited.

2. The method of claim 1 wherein the peptide has the formula X-PLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNSQSP-Z (SEQ ID NO: 239).

3. The method of claim 1 wherein the peptide has the formula X-PLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGT-Z (SEQ ID NO: 240).

4. The method of claim 1 wherein the peptide has the formula X-LLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGTT-Z (SEQ ID NO: 241).

5. The method of claim 1 wherein the peptide has the formula X-LVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGTTV-Z (SEQ ID NO: 242).

6. The method of claim 1 wherein the peptide has the formula X-LQAGFFLLTRILTIPQSLDSWWTSLNGLGGTTVCL-Z (SEQ ID NO: 243).

7. The method of claim 1 wherein the peptide has the formula X-QAGFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLG-Z (SEQ ID NO: 244).

8. The method of claim 1 wherein the peptide has the formula X-AGFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQ-Z (SEQ ID NO: 245).

9. The method of claim 1 wherein the peptide has the formula X-GFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQN-Z (SEQ ID NO: 246).

10. The method of claim 1 wherein the peptide has the formula X-FFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNS-Z (SEQ ID NO: 247).

11. The method of claim 1 whereint he peptide has the formula X-FLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNSQ-Z (SEQ ID NO: 248).

12. The method of claim 1 wherein the peptide has the formula S-LLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNSQS-Z (SEQ ID NO: 249).

13. The method of claim 1 wherein the peptide has the formula X-PGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTSTG PCRTCMTT-Z (SEQ ID NO: 250).

14. The method of claim 1 wherein the peptide has the formula X-PGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGML-Z (SEQ ID NO: 251).

15. The method of claim 1 wherein the peptide has the formula X-GYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLP-Z (SEQ ID NO: 252).

16. The method of claim 1 wherein the peptide has the formula X-YRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPV-Z (SEQ ID NO: 253).

17. The method of claim 1 wherein the peptide has the formula X-RWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVC-Z (SEQ ID NO: 254).

18. The method of claim 1 wherein the peptide has the formula X-WMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCP-Z (SEQ ID NO: 255).

19. The method of claim 1 wherein the peptide has the formula X-MCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPI-Z (SEQ ID NO: 256).

20. The method of claim 1 wherein the peptide has the formula X-CLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLI-Z (SEQ ID NO: 257).

21. The method of claim 1 wherein the peptide has the formula X-LRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIP-Z (SEQ ID NO: 258).

22. The method of claim 1 wherein the peptide has the formula X-RRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPG-Z (SEQ ID NO: 259).

23. The method of claim 1 wherein the peptide has the formula X-RFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGS-Z (SEQ ID NO: 260).

24. The method of claim 1 wherein the peptide has the formula X-FIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSS-Z (SEQ ID NO: 261).

25. The method of claim 1 wherein the peptide has the formula X-IIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSST-Z (SEQ ID NO: 262).

26. The method of claim 1 wherein the peptide has the formula X-IFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTT-Z (SEQ ID NO: 263).

27. The method of claim 1 wherein the peptide has the formula X-FLFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTS-Z (SEQ ID NO: 264).

28. The method of claim 1 wherein the peptide has the formula X-LFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTST-Z (SEQ ID NO: 265).

29. The method of claim 1 wherein the peptide has the formula X-FILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTG-Z (SEQ ID NO: 266).

30. The method of claim 1 wherein the peptide has the formula X-ILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGP-Z (SEQ ID NO: 267).

31. The method of claim 1 wherein the peptide has the formula X-LLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPC-Z (SEQ ID NO: 268).

32. The method of claim 1 wherein the peptide has the formula X-LLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCR-Z (SEQ ID NO: 269).

33. The method of claim 1 wherein the peptide has the formula X-LCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCRT-Z (SEQ ID NO: 270).

34. The method of claim 1 wherein the peptide has the formula X-CLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCRTC-Z (SEQ ID NO: 271).

35. The method of claim 1 wherein the peptide has the formula X-LIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCRTCM-Z (SEQ ID NO: 272).

36. The method of claim 1 wherein the peptide has the formula X-IFLLVLLDYQGMLPVCPLIPGSSTTSTGPCRTCMT-Z (SEQ ID NO: 273).

37. The method of claim 1 wherein X is an acetyl group, and Z is an amido group.
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