Inactivated pepsin fragments for modulating immune system activity against human malignant tumor cells
AssigneeThe Zhabilov Trust
InventorHarry H. Zhabilov
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Abstract
Isolated anti-cancer peptides are disclosed which are characterized by the amino acid sequences TLTSGGGAIALPPSMAAPPLGPVAPLTGAIHAPTXG; TLSTATGGAIPPVAAMPPGLVAPTHGPAIHP; CCATSGPCGAVMILTPHLTA; MTLTTGSGAIAPAMPPGLPPHTGAIHAPM; and NXVPVSVEGYXQITLDSITX and a significant in vitro binding affinity for gp96. The peptides exhibit anti-tumor, anti-cancer activity in vivo. Also disclosed is an isolated antiviral peptide is characterized by the amino acid sequence GDEPLENYLDTEYF and a significant in vitro binding affinity for HIV-1 gp 120 and gp 41, and human CD4 cells. The peptide exhibits anti-retroviral activity in vivo, particularly anti-HIV-1 activity.
Claims32
An isolated irreversibly inactivated anti-cancer pepsin characterized by the amino acid sequence of SEQ ID:
- NO. 1
An isolated irreversibly inactivated anti-cancer pepsin characterized by the amino acid sequence of SEQ ID:
- NO. 2.
A thirty one amino acid pepsinogen fragment having a binding affinity for human gp96.
An isolated irreversibly inactivated anti-cancer pepsin characterized by the amino acid sequence of SEQ ID:
- NO. 3.
A composition comprising an IPF gp96 complex, wherein said composition demonstrates superantigen activity.
A complex of gp96 and IPF, wherein the complex activates major histocompatibility complex (HMC)-restricted manner.
An isolated irreversibly inactivated anti-cancer pepsin characterized by the amino acid sequence of SEQ ID:
- NO. 4.
An isolated irreversibly inactivated anti-cancer pepsin characterized by the amino acid sequence of SEQ ID:
- NO. 5.
Dependencies are inferred from the claim text.