t-20

Enfuvirtide acetate salt is a linear synthetic peptide made of 36 amino acids. It has an acetylated N-terminus and a carboxamide C-terminus.

Tet-20, a synthetic cathelicidin-derived peptide with biological activity, has been evaluated for its efficacy as an infection-resistant coating on medical devices. Upon surface tethering to implants, Tet-20 demonstrates broad-spectrum antimicrobial properties, inhibits biofilm formation, and maintains non-toxicity to eukaryotic cells both in vitro and in vivo.

MAIT-203, a cyclopentyalanin-derived peptidomimetic, effectively disrupts the interaction between adenomatous polyposis coli (APC) and Asef (RhoGEF4), without affecting APC-Sam68 or APC-striatin interactions. It binds to APC-ARM domains with a K i of 0.015 μM and a K d of 0.036 μM, notably inhibiting the migration and invasion of colorectal cancer cells.

MAIT-203 acetate is a cyclopentylglycine-derived peptidomimetic that effectively inhibits the interaction between adenomatous polyposis coli (APC) and Asef (RhoGEF4), while not affecting the APC-Sam68 or APC-striatin interactions. It binds to APC-ARM with a Ki of 0.015 μM and a Kd of 0.036 μM, significantly impeding the migration and invasion of colorectal cancer cells.

Amyloid-β (25-35) (Aβ (25-35)) is an 11-residue fragment of the Aβ protein that retains the physical and biological characteristics of the full length peptide. It forms fibrils that react to thioflavin T and Congo red and are organized in a cross-β arrangement of β-strands similar to Aβ (1-40) and Aβ (1-42) fibrils. Aggregated Aβ (25-35) decreases the viability of rat adrenal PC12 cells. It also decreases the viability of primary rat cortical neurons at concentrations ranging from 1 nM to 30 μM. In vivo, intracerebral injection of Aβ (25-35) (20 nmol) in rats induces lesions of neuronal and tissue loss. Aggregated Aβ (25-35) administered intracerebroventricularly to rats induces learning and memory impairments in the Y-maze, novel object recognition, and contextual fear conditioning tests.

Siamycin I is a tricyclic peptide originally isolated from Streptomyces and has antiviral and antibacterial activities. It is active against laboratory strains and clinical isolates of HIV-1 (ED50s = 0.05-0.45 and 0.89-5.7 μM, respectively), as well as the CBL-20 strain of HIV-2 (ED50 = 0.45 μM), in vitro. Siamycin I inhibits HIV-induced fusion of C8166 T cells with HIV-1-infected CEM-SS cells with an ED50 value of 0.08 μM. It is also active against B. subtilis, M. luteus, and S. aureus (MICs = 1.6-6.3 μg/ml). Siamycin I inhibits autophosphorylation of the E. faecalis quorum sensing kinase FsrC induced by gelatinase biosynthesis-activating pheromone (GBAP).

TPP-1, a peptide inhibitor, targets the interaction between programmed cell death protein 1 (PD-1) and its ligand (PD-L1), binding specifically to PD-L1 with a dissociation constant (Kd) of 94.67 nM. At a concentration of 20 µM, TPP-1 effectively counteracts the PD-L1-induced suppression of IFN-γ production in anti-CD3-stimulated isolated human CD4+ T cells. Furthermore, TPP-1 demonstrates significant efficacy in reducing tumor volume in a mouse xenograft model of HL-60 leukemia. This model involved HL-60 cells co-cultured with anti-CD3-activated isolated human CD4+ T cells, with TPP-1 administration at a dosage of 4 mg/kg showing notable antitumor activity.

HPV16-E711-20 epitope is a well-known HLA-A*0201-restricted human cytotoxic T lymphocyte (CTL) epitope of the HPV16 E7 protein, demonstrating high-affinity binding to HLA-A2 in vitro.