Cell-penetrating Peptides Development

Cell-penetrating peptides are capable of carrying peptides, nucleic acids, small molecule drugs and viral particles across cell membranes and into cells. CD Formulation provides professional cell-penetrating peptide drug delivery development services, including molecular design.

What is a Cell-penetrating Peptide

Cell-penetrating peptides (CPPs) are relatively short amphiphilic and cationic peptides (7-30 amino acid residues) that can rapidly cross cell membranes. Due to their efficacy in cellular internalization and their low cytotoxicity, they can be used for the delivery of molecular bioactive cargoes. Due to their polypeptide properties, cell-penetrating peptides are normally catabolized upon entry into the cell, have good biocompatibility and are usually less toxic to cells. Cell entry studies of biomolecule drugs mediated by membrane-penetrating peptides have flourished since then. Currently, cell-penetrating peptides have become a powerful carrier tool for biomolecules to cross cell membranes and thus for intracellular transport.

Molecular Design of Cell-penetrating Peptides

In the molecular design of cell-penetrating peptides, cationic and hydrophobic characteristics need to be considered together. The design concept of the cell-penetrating peptide is to contain the same hydrophilic nuclear localization sequence and to couple this sequence with a hydrophobic sequence of the viral fragment. By integrating cationic amino acid residues, hydrophobic fragments, and amphipathic structures in different ways in the same peptide molecule, more efficient cell-penetrating peptides can be constructed and derived.

The correlation between the internalization effect of cell-penetrating peptides and cationic residues has been demonstrated. The molecular design of cell-penetrating peptides is mainly focused on small cationic peptides. The uptake efficiency of polycationic cell-penetrating peptides depends on the sequence length and the position of arginine residues in the peptide sequence. In addition to the cationic part, the lipophilic part is also important for cellular uptake.

Hydrophobicity can be achieved by adding aliphatic or aromatic structures. Several studies of cell-penetrating peptide mimics have confirmed that aromatic activation is superior to aliphatic. Lipidation is achieved by attaching hydrocarbon chains (alkyl groups) of different lengths to the N-terminal or other suitable functional groups of known cell-penetrating peptides. This alkylation modification improves the internalization of the cell-penetrating peptide by enhancing the hydrophobic interaction with the membrane. In addition to the integration of aliphatic chains, the hydrophobicity of peptide molecules can also be enhanced by the introduction of hydrophobic amino acids.

Membrane-penetrating Peptide as a Carrier for Drug Delivery

Membrane-penetrating peptides as drug delivery carriers allow drugs to enter cells and even cross the epithelial cells and blood-brain barrier, and are beginning to be used in the treatment of many diseases.

• Application of membrane piercing peptides as carriers in tumor therapy

Some small molecules of antitumor chemotherapeutic drugs are linked to membrane penetrating peptides to improve their membrane penetration, drug delivery efficiency, half-life and aggregation in tumor cells.

• Cellular membrane penetrating peptides cross the epithelial cells and blood-brain barrier

The main obstacle to the non-injectable route of administration of macromolecular drugs, or to their crossing the blood-brain barrier, is their inability to effectively penetrate the epithelium and endothelium. An important application of membrane penetrating peptides is their ability to act as carriers to carry peptides and proteins across the intestinal tract, lung epithelium, and across the blood-brain barrier.

• Antibacterial and antiviral applications of membrane piercing peptides

Antimicrobial peptides usually have the advantages of being amphiphilic and strongly cationic, thermally stable, producing low resistance and being largely non-toxic to eukaryotic cells. Antimicrobial peptides act on the lipid membrane of bacteria or fungi to kill microorganisms by forming pores in the membrane or increasing the permeability of the cell membrane.

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