WO2005123771B1 - Oligomeric peptides and their use for the treatment of hiv infections - Google Patents

Oligomeric peptides and their use for the treatment of hiv infections

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Publication number
WO2005123771B1
WO2005123771B1 PCT/EP2005/052833 EP2005052833W WO2005123771B1 WO 2005123771 B1 WO2005123771 B1 WO 2005123771B1 EP 2005052833 W EP2005052833 W EP 2005052833W WO 2005123771 B1 WO2005123771 B1 WO 2005123771B1
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WO
WIPO (PCT)
Prior art keywords
vir
seq
amino acid
cysteine
peptide
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Ceased
Application number
PCT/EP2005/052833
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French (fr)
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WO2005123771A3 (en
WO2005123771A2 (en
Filing date
Publication date
Priority to US11/629,883 priority Critical patent/US20070123465A1/en
Priority to EP05752836.6A priority patent/EP1756160B1/en
Priority to AU2005254736A priority patent/AU2005254736B2/en
Priority to EA200700062A priority patent/EA011037B1/en
Priority to AP2007003877A priority patent/AP2081A/en
Priority to CN200580019909A priority patent/CN100577686C/en
Priority to BRPI0511005-0A priority patent/BRPI0511005A/en
Priority to JP2007515966A priority patent/JP4782782B2/en
Priority to MXPA06014393A priority patent/MXPA06014393A/en
Priority to CA002569807A priority patent/CA2569807A1/en
Application filed filed Critical
Publication of WO2005123771A2 publication Critical patent/WO2005123771A2/en
Publication of WO2005123771A3 publication Critical patent/WO2005123771A3/en
Publication of WO2005123771B1 publication Critical patent/WO2005123771B1/en
Anticipated expiration legal-status Critical
Priority to NO20070296A priority patent/NO20070296L/en
Ceased legal-status Critical Current

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Abstract

The invention relates to oligomeric peptides with biological activity against HIV infection having the amino acid sequence (Z1-LE-X1-IP-X2-X3-X4-P-X5-X6-X7-X8- X9-X10-K-X11-X12-X13-X14-X15-Z2)n, wherein n indicates the number of monomeric peptide chains, whereby n is 2, 3 or 4; X1 is a lysine, alanine, or aspartic acid; X2 is a cysteine, methionine or isoleucine; X3 is a serine, cysteine, lysine or glycine; X4 is an isoleucine, alanine, phenylalanine or cysteine; X5 is a proline, D-proline or a substituted L-or D-proline; X6 is a cysteine or glutamic acid; X7 is an amino acid with a hydrophobic or an aromatic side chain or cysteine; X8 is an amino acid with a hydrophobic or an aromatic side chain or cysteine; X9 is an amino acid with an aromatic side chain; X10 is a glycine, alanine or asparagine; X11 is a proline, aspartic acid, octahydroindolyl-2-carboxylic acid or D­1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid; X12 is a phenylalanine, alanine, glycine, glutamic acid or D-1,2,3,4­tetrahydroisoquinoline-3-carboxylic acid; X13 is an amino acid with a hydrophobic or an aromatic side chain; X14 is an amino acid with a hydrophobic or an aromatic side chain; X15 is a phenylalanine or deletion; Z1 is NH2 or a sequence of 1 to 10 amino acid residues; Z2 is COOH or a sequence of 1 to 10 amino acid residues; and oligomeric peptides which are fragments thereof and/or derivatives, especially amidated, alkylated, acylated, sulfated, pegylated, phosphorylated and/or glycosylated derivatives, and mutants thereof; and with the proviso that (a) if X12 is alanine, glycine, glutamic acid, or D-1,2,3,4­tetrahydroisoquinoline-3-carboxylic acid than X13, X14 and X15 are phenylalanine, valine and phenylalanine respectively; and/or (b) if X12 is phenylalanine, than X13, X14 and X15 are valine, phenylalanine and a deletion, respectively; and (c) there are at maximum three cysteine residues in a peptide; and (d) the oligomeric peptide has not the sequence (LEAIPCSIPPEFLFGKPFVF)2 (VIR-576); and (e) the monomeric peptide chains are not linked by peptide bonds between the N- terminus of one peptide chain to the C-terminus of another peptide chain.

Claims

- 48 -AMENDED CLAIMS received by the International Bureau on 10 February 2006 (10.02.2006)
1. Oligomeric peptides, with biological activity against infection by HIV, comprising monomelic peptide chains of the amino acid sequence
(Zi-LE-Xl-IP-X2~X3~X4~P~Xs~X6~X7~X8~ X9~Xl0"K-Xll-Xl2-Xl3-Xl4-Xl5-Z2)n, wherein n indicates the number of monomeric peptide chains, whereby n is 2, 3 or 4;
Xi is a lysine, alanine, or aspartic acid;
X2 is a cysteine, methionine or isoleucine;
X3 is a serine, cysteine, lysine or glycine;
X4 is an isoleucine, alanine, phenylalanine or cysteine;
X5 is a proline, D-proline or a substituted L-or D-proline;
X6 is a cysteine or glutamic acid;
X7 is an amino acid with a hydrophobic or an aromatic side chain or cysteine;
X8 is an amino acid with a hydrophobic or an aromatic side chain or cysteine;
X9 is an amino acid with an aromatic side chain;
Xi0 is a glycine, alanine or asparagine;
Xu is a proline, aspartic acid, octahydroindolyl-2-carboxylic acid or D- l,2,3,4-tetrahydroisoquinoline-3-carboxylic acid;
Xi2 is a phenylalanine, alanine, glycine, glutamic acid or D-1, 2,3,4- tetrahydroisoquinoline-3-carboxy!ic acid;
Xi3 is an amino acid with a hydrophobic or an aromatic side chain;
Xi4 is an amino acid with a hydrophobic or an aromatic side chain;
Xi5 is a phenylalanine or deletion;
Zi is NH2 or a sequence of 1 to 10 amino acid residues;
Z2 is COOH or a sequence of 1 to 10 amino acid residues; and oligomeric peptides with biological activity against infection by HIV which are fragments thereof and/or derivatives, especially amidated, - 49 -
alkylated, acylated, sulfated, pegylated, phosphorylated and/or glycosylated derivatives, and mutants thereof;
and with the proviso that
(a) if X12 is alanine, glycine, glutamic acid, or D-1, 2, 3,4- tetrahydroisoquinoline-3-carboxylic acid than Xi3, XM and Xi5 are phenylalanine, valine and phenylalanine respectively; and/or
(b) if Xi2 is phenylalanine, than Xi3, X14 and X15 are valine, phenylalanine and a deletion, respectively; and
(c) there are at maximum three cysteine residues in any monomeric peptide chain of an oligomeric peptide; and
(d) the oligomeric peptide is not (LEAIPCSIPPEFLFGKPFVF)2 (VIR- 576);. and
(e) the monomeric peptide chains are not linked by peptide bonds between the N- terminus of one peptide chain to the C-terminus of another peptide chain.
2. Oligomeric peptides according to claim 1 with a biological activity against infection by HIV having the amino acid sequence
(Z1-LE-Xi-IP-X2-X3-X4-P-X5-X6-X7-X8- X9-Xio-K-Xu-FVF-Z2)n, wherein n indicates the number of monomeric peptide, whereby n is 2, 3 or 4;
Xi is a lysine, alanine or aspartic acid;
X2 is a cysteine, methionine or isoleucine;
X3 is a serine, cysteine or glycine;
X4 is a isoleucine or cysteine;
X5 is a proline, D-proline or any substituted L- or D-proline;
Xβ is a cysteine or glutamic acid;
X7 is a phenylalanine, cysteine, valine, isoleucine or 3,3-diphenylalanine;
X8 is a phenylalanine, leucine, alanine, glycine, cysteine, D-I, 2,3,4- tetrahydroisoquinoline-3-carboxylic acid or L-l,2,3,4-tetrahydro- isoquino!ine-3-carboxylic acid; - 50-
X9 is an amino acid with an aromatic side chain;
X10 is a glycine or asparagine;
Xu is a proline or D-l,2,3,4-tetrahydroisoquinoline-3-carboxy!ic;
Z1 is NH2 or a sequence of 1 to 10 amino acid residues;
Z2 is COOH or a sequence of 1 to 10 amino acid residues; and oligomeric peptides with biological activity against infection by HIV which are fragments thereof and/or derivatives, especially amidated, alkylated, acylated, sulfated, pegylated, phosphorylated and/or glycosylated derivatives, and mutants thereof.
3. Oligomeric peptides according to claims 1 to 2 with a biological activity against infection by HIV, having the amino acid sequence
(ZrLE-Xi-IP-X^-IP-Xs-Xe-Xy-Xs-F-Xio-KPFVF-Z^n, wherein n indicates the number of monomeric peptide chains, whereby n is 2, 3 or 4;
Xi is a lysine, alanine or aspartic acid;
X2 is a cysteine, methionine or isoleucine;
X3 is a serine or glycine;
X5 is a L-proline, D-proline or any substituted L- or D-proline
X6 is a cysteine or glutamic acid;
X7 is a phenylalanine or valine;
X8 is a phenylalanine, leucine, alanine or L-l,2,3,4-tetrahydro- isoquinoline-3-carboxylic acid;
X10 is a glycine or asparagine;
Z1 is NH2 or a sequence of 1 to 10 amino acid residues;
Z2 is COOH or a sequence of 1 to 10 amino acid residues, and and oligomeric peptides with biological activity against infection by HIV which are fragments and/or derivatives, especially amidated, alkylated, acylated, sulfated, pegylated, phosphorylated and/or glycosylated derivatives, and mutants thereof. - 51 -
4. Oligomeric peptides according to anyone of the claims 1 to 3, having the amino acid sequence
(ZI-LEAIP-X2-SIP-X5-X6-V-X8-FNKPFVF-Zz)n/ wherein n indicates the number of monomeric peptide chains, whereby n is 2, 3 or 4;
X2 and X6 are cysteines, or X2 is methionine and X6 is glutamic acid
X5 is a D-proline or L-proline;
X8 is an amino acid with a hydrophobic or an aromatic side chain or lysine;
Z1 is NH2 or a sequence of 1 to 10 amino acid residues;
Z2 is COOH or a sequence of 1 to 10 amino acid residues; and oligomeric peptides which are fragments and/or derivatives, especially amidated, alkylated, acylated, sulfated, pegylated, phosphorylated and/or glycosylated derivatives, and mutants thereof, with biological activity against infection by HIV,
with the proviso that at least one of the following is true:
X2 and X6 are cysteines; X5 is D-proline; or X8 is not lysine.
5. Oligomeric peptides of any of claims 1 to 4, wherein the monomeric peptide chains are crosslinked.
6. Oligomeric peptides according to anyone of the claim 1 to 5, wherein the cysteine residues at positions 6 and 11, 6 and 12, 7 and 12, or 8 and 13 are connected by an intramolecular disulfide bond.
7. Oligomeric peptide according to anyone of the claims 1 to 6, wherein the leucine residue at amino acid position 1 and the glutamic acid at amino acid position 2 are covalently linked by an N-alkylated amide bond or by an ester bond or by a reduced peptide bond or by a retro-inverso peptide bond or by an N-alkylated retro-inverso peptide bond.
8. Oligomeric peptide according to anyone of the claim 1 to 5 or 7, wherein at least two monomeric peptide chains both have at least one single cysteine residue, which are covalently linked to each other through a disulfide bond.
9. Oligomeric peptide according to anyone of the claims 1 to 7, wherein the monomeric peptide chains are covalently linked to each other via at least one amide bond between a COOH group of an acidic amino acid side chain and an NH2 group of a basic amino acid side chain.
10. Oligomeric peptide according to anyone of the claims 1 to 9, wherein the monomeric peptide chains are connected to each other via a bifunctional spacer molecule selected from the group of organic spacers with two thiol groups, organic spacers with two amino groups, organic spacers with two carboxyl groups and organic spacers with one carboxyl group and one amino group.
11. Oligomeric peptide according to anyone of the claims 1 to 10, comprising two or four monomeric peptide chains, and at least one lysine-core which covalently links the monomeric peptide chains.
12. Peptides according to anyone of the claims 1 to 11 with one of the following amino acid sequences
VIR-574 (LEAIPMSIPPEFLFGKPFVF)z-K-G SEQ ID NO. 2
VIR-577 (LEAIPMCIPPEFLFGKPFVF)2 SEQ ID NO. 3
VIR-673 (LEAIPMSIPPEFLFGKPFVF-miniPEG-C-amideh SEQ ID NO. 4
VIR-674 (LEAIPCSIPPCVA(D-Tic)NKP(D-Tic)FVF)2 SEQ ID NO. 5
VIR-675 (LEAIPMSIPPEFLFGKPFVF)2 SEQ ID NO. 6
VIR-676 (LEAIPMSIPpE(3,3-diphenylalanine)AFNKPFVF)2 SEQ ID NO. 7
VIR-677 (LEAIPMCIPPECFFNKPFVF)2 SEQ ID NO. 8
VIR-678 (LEAIPMCIPPECLFGKPFVF)2 SEQ ID NO. 9 - 53 -
VIR-679 (LEAIPCSIPPCVFFGKPFVF)2 SEQ ID NO. 10
VIR-680 (LEAIPCSIPPCFLFGKPFVF)2 SEQ ID NO. 11
VIR-681 (LEAIPCSIPPCVGFGKPFVF)2 SEQ ID NO. 12
VIR-682 (LEAIPCSIPpCVFFNKPFVF)2 SEQ ID NO. 13
VIR-683 (LEAIPCSIPPCFLFNKPFVF)2 SEQ ID NO. 14
VIR-684 (LEDIPCSIPPCVAFNKPFVF)2 SEQ ID NO. 15
VIR-685 (LEKIPCSIPpCVAFNKPFVF);, SEQ ID NO. 16
VIR-686 (LEAIPMGIPpEV(D-Tic)FNKPFVF)2 SEQ ID NO. 17
VIR-687 (LEAIPMGIPpEV(L-TiC)FNKPFVF)2 SEQ ID NO. 18
VIR-688 (LEKIPMSIPpEV(D-TiC)FNKPFVF)2 SEQ ID NO. 19
VIR-689 (LEKIPMSIPpEV(L-TiC)FNKPFVF)2 SEQ ID NO. 20
VIR-690 (LEKIPIGIPpEV(D-TiC)FNKPFVF)2 SEQ ID NO. 21
VIR-691 (LEKIPIGIPpEV(L-TiC)FNKPFVF)2 SEQ ID NO. 22
VIR-692 (N-Me-LEAIPMSIPPEFLFGKPFVF)2 SEQ ID NO. 23
VIR-693 (LEAIPMSCPPEFCFGKPFVF)2 SEQ ID NO. 24
VIR-694 (LEAIPMSIPPEFLFGKPFVF-miniPEG)2 SEQ ID NO. 25
VIR-695 (LEAIPCSIPPEVA(D-TiC)NKP(D-TiC)FVF)2 SEQ ID NO. 26
VIR-696 (LEAIPCSIPpE(3,3-diphenylalanine)AFNKPFVF)2 SEQ ID NO. 27
VIR-697 (LEAIPMCIPPEVFFNKPFVF)2 SEQ ID NO. 28
VIR-698 (LEAIPMCIPPEVLFGKPFVF)2 SEQ ID NO. 29
VIR-699 (LEAIPCSIPPEVFFGKPFVF)2 SEQ ID NO. 30
VIR-700 (LEAIPCSIPPEFLFGKPFVF)2 SEQ ID NO. 31
VIR-701 (LEAIPCSIPpEVGFGKPFVF)2 SEQ ID NO. 32
VIR-702 (LEAIPCSIPpEVFFNKPFVF)2 SEQ ID NO. 33
VIR-703 (LEAIPCSIPpEFLFNKPFVF)2 SEQ ID NO. 34
VIR-704 (LEDIPCSIPpEVAFNKPFVF)2 SEQ ID NO. 35
VIR-705 (LEKIPCSIPpEVAFNKPFVF) 2 SEQ ID NO. 36
VIR-706 (LEAIPCGIPpEV(D-TiC)FNKPFVF)2 SEQ ID NO. 37
VIR-707 (LEAIPCGIPpEV(L-TiC)FNKPFVF)2 SEQ ID NO. 38
VIR-708 (LEKIPCSIPpEV(D-TiC)FNKPFVF)2 SEQ ID NO. 39
VIR-709 (LEKIPCSIPpEV(L-TiC)FNKPFVF)2 SEQ ID NO. 40
VIR-710 (LEKIPCGIPpEV(D-TiC)FNKPFVF)2 SEQ ID NO. 41
VIR-711 (LEKIPCGIPpEV(L-TiC)FNKPFVF)2 SEQ ID NO. 42
VIR-712 (N-Me-LEAIPCSIPPEFLFGKPFVF)2 SEQ ID NO. 43
VIR-713 (LEAIPMSCPPEFLFGKPFVF)2 SEQ ID NO. 44 - 54 -
VIR-714 (LEAIPCSIPPEFLFGKPFVF-(miniPEG)2-amide)2 SEQ ID NO. 45
VIR-715 (N-Me-LEAIPCSIPPEFLFGKPFVF-(miniPEG)2-amide)2 SEQ ID NO. 46
VIR-716 (N-Me-LEKIPCSIPPEFLFGKPFVF)2 SEQ ID NO. 47
VIR-717 (N-Me-LEDIPCSIPPEFLFGKPFVF)2 SEQ ID NO. 48
VIR-718 (LEKIPIGIPpEV(L-TiC)FNKPFVF) 2-KA SEQ ID NO. 49
VIR-719 (N-Me-LEAIPCSIPpEFLFGKPFVF)2 SEQ ID NO. 50
VIR-720 (LEKIPIGIPpEV(L-Tic)FNKPFVF-miniPEG-C)2 SEQ ID NO. 51
VIR-721 (LEKIPCaPpCVAFNKPFVF)2 SEQ ID NO. 52
VIR-722 (N-Me-LEDIPCSIPpCVAFNKPFVF-miniPEG-C);, SEQ ID NO. 53
VIR-723 (LEAIPCSIPPEFLFGKPFVF-(miniPEG)2-C)2 SEQ ID NO. 54
13. The oligomeric peptides according to anyone of claims 1 to 12, which interact with the fusion peptide of HIV.
14. The oligomeric peptides according to anyone of claims 1 to 13, which have an IC50 of equal or below 6500 nM, such as VIR-574, VIR-577 and VIR- 673.
15. Nucleic acids coding for the monomeric peptide chains of any of the monomeric peptides according to claim 12, except the nucleic acids encoding the monomeric peptide chains of VIR-674, VIR-675, VIR-676, VIR-677, VIR-678, VIR-679, VIR-680, VIR-681, VIR-682, VIR-683, VIR- 684, VIR-685, VIR-686, VIR-687, VIR-688, VIR-689, VIR-690, VIR-691, VIR-692, VIR-693 and VIR-694.
16. Antibodies binding specifically to the oligomeric peptides according to anyone of the claims 1 to 12.
17. A medicament comprising at least one of the oligomeric peptides according to anyone of the claims 1 to 14, nucleic acids of claim 15 and/or antibodies of claim 16.
18. The medicament of claim 17 in galenic formulations for oral, intravenous, intramuscular, intracutaneous, subcutaneous and/or intrathecal administration. - 55 -
19. The medicament of claim 17 or 18 comprising at least one further therapeutic agent.
20. The medicament of claim 19, wherein the said at least one further therapeutic agent is a viral protease inhibitor, a reverse transcriptase inhibitor, a fusion inhibitor, a cytokine, a cytokine inhibitor, a glycosylation inhibitor or a viral mRNA inhibitor.
21. Use of the oligomeric peptides according to anyone of the claims 1 to 12 for the manufacturing of a medicament for the treatment of HIV infections.
22. An assay for determining molecules capable of interaction with the fusion peptide of HIV, comprising at least one oligomeric peptide according to anyone of the claims 1 to 12.
23. Use of an oligomeric peptides according to anyone of the claims 1 to 12 in an assay according to claim 22.
24. A diagnostic agent comprising at least one oligomeric peptides according to anyone of the claims the 1 to 12, nucleic acids according to claim 15 or antibodies according to claim 16.
25. Use of the diagnostic agent according to claim 24 for testing isolated blood, plasma, tissue, urine, semen and/or cerebrospinal fluid for HIV infection.
PCT/EP2005/052833 2004-06-18 2005-06-17 Oligomeric peptides and their use for the treatment of hiv infections Ceased WO2005123771A2 (en)

Priority Applications (11)

Application Number Priority Date Filing Date Title
MXPA06014393A MXPA06014393A (en) 2004-06-18 2005-06-17 Oligomeric peptides and their use for the treatment of hiv infections.
AU2005254736A AU2005254736B2 (en) 2004-06-18 2005-06-17 Oligomeric peptides and their use for the treatment of HIV infections
EA200700062A EA011037B1 (en) 2004-06-18 2005-06-17 Oligomeric peptides and their use for the treatment of hiv infections
AP2007003877A AP2081A (en) 2004-06-18 2005-06-17 Oligomeric peptides and their use for the treatment of HIV infections
CN200580019909A CN100577686C (en) 2004-06-18 2005-06-17 Oligomeric peptide and its use for treating HIV infection
BRPI0511005-0A BRPI0511005A (en) 2004-06-18 2005-06-17 oligomeric peptides and their use for the treatment of HIV infections
JP2007515966A JP4782782B2 (en) 2004-06-18 2005-06-17 Oligomer peptides and their use for the treatment of HIV infection
US11/629,883 US20070123465A1 (en) 2004-06-18 2005-06-17 Oligomeric peptides and their use for the treatment of hiv infections
EP05752836.6A EP1756160B1 (en) 2004-06-18 2005-06-17 Oligomeric peptides and their use for the treatment of hiv infections
CA002569807A CA2569807A1 (en) 2004-06-18 2005-06-17 Oligomeric peptides and their use for the treatment of hiv infections
NO20070296A NO20070296L (en) 2004-06-18 2007-01-16 Oligomeric peptides and their use in the treatment of HIV infections

Applications Claiming Priority (6)

Application Number Priority Date Filing Date Title
US58038404P 2004-06-18 2004-06-18
US60/580,384 2004-06-18
EP04014304 2004-06-18
EP04014304.2 2004-06-18
US67586105P 2005-04-29 2005-04-29
US60/675,861 2005-04-29

Publications (3)

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WO2005123771A2 WO2005123771A2 (en) 2005-12-29
WO2005123771A3 WO2005123771A3 (en) 2006-02-09
WO2005123771B1 true WO2005123771B1 (en) 2006-04-27

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Country Status (13)

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US (1) US20070123465A1 (en)
EP (1) EP1756160B1 (en)
JP (1) JP4782782B2 (en)
CN (1) CN100577686C (en)
AP (1) AP2081A (en)
AU (1) AU2005254736B2 (en)
BR (1) BRPI0511005A (en)
CA (1) CA2569807A1 (en)
EA (1) EA011037B1 (en)
MX (1) MXPA06014393A (en)
NO (1) NO20070296L (en)
WO (1) WO2005123771A2 (en)
ZA (1) ZA200705769B (en)

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CN103965300A (en) * 2005-11-02 2014-08-06 Ambrx公司 Biosynthetic Polypeptide Fusion Inhibitors
US9212205B2 (en) * 2007-07-26 2015-12-15 University Of Rochester Nucleic acid binding compounds and methods of use
CN101993485B (en) * 2009-08-20 2013-04-17 重庆富进生物医药有限公司 Peptide analog homologous dimer capable of accelerating insulin secretion and application thereof
GR1007010B (en) * 2009-10-08 2010-10-07 Χημικα Και Βιοφαρμακευτικα Εργαστηρια Πατρων Αε (Cbl-Patras), INSULINOID Peptides
WO2011103409A1 (en) * 2010-02-18 2011-08-25 Advanced Proteome Therapeutics Inc. Site-specific modification of proteins through chemical modification enabling protein conjugates, protein dimer formation, and stapled peptides
WO2011110049A1 (en) * 2010-03-12 2011-09-15 中国人民解放军军事医学科学院毒物药物研究所 Anti-hiv fusion polypeptide and use thereof
WO2011127624A1 (en) * 2010-04-13 2011-10-20 中国人民解放军军事医学科学院毒物药物研究所 Anti-hiv peptide
CN102180951B (en) * 2011-05-03 2012-09-26 中国医学科学院病原生物学研究所 Cholesterol modified anti-human immunodeficiency virus (HIV) polypeptide medicament and application thereof
JP6290187B2 (en) 2012-05-11 2018-03-07 クランツ，アレクサンダー Site-specific labeling and targeted delivery of proteins for the treatment of cancer
CA2913387C (en) * 2013-06-12 2024-05-21 Pharis Biotec Gmbh Peptides with antagonistic activities against natural cxcr4
CN109922818B (en) * 2016-09-06 2024-02-20 主线生物科学公司 CXCR4 antagonists and methods of use
WO2018087146A1 (en) * 2016-11-09 2018-05-17 Pharis Biotec Gmbh Protransducine-c: gene transfer activator
WO2021060439A1 (en) * 2019-09-26 2021-04-01 日油株式会社 Heterobifunctional monodispersed polyethylene glycol having peptide linker
WO2022202785A1 (en) * 2021-03-22 2022-09-29 美智子 甲賀 Peptide, and cell fusion agent and pharmaceutical composition for cancer therapy containing said peptide
WO2024197259A1 (en) * 2023-03-23 2024-09-26 Brandeis University Transcytotic intercellular gelation enables cell spheroids

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DE50015216D1 (en) * 1999-11-08 2008-07-31 Ipf Pharmaceuticals Gmbh HUMAN CIRCULATIVE VIRUS INHIBITING PEPTIDE (VIRIP) AND ITS USE
JP4505336B2 (en) * 2002-12-19 2010-07-21 イーペーエフ ファルマシューティカルス ゲゼルシャフト ミット ベシュレンクテル ハフツング Peptides and their use for the treatment of HIV infection

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