Yes, certainly, but it could be interesting to have more information

I can help. Please provide more information.

Hi,i am going to make peptide from a gene as a treatment for cancerous cells but i do not know how long it shoud be to deliver to target cells easily and also i want to add peptide transduction domain to the peptide for insertion however i dont know what it should be and how can provide it commercially.

Again, Not enough information. The questions you ask have no real answers unless you describe the gene, the type of cancer cells? what do you want to deliver? are you designing a Cell Penetrating Peptide (CPP)? what should be the cargo? is it a protein? an antibody? a toxic molecule? What type pf Transduction domain do you refer to? and before you can provide it commercially, it has to work in a scientific and small scale setting.

You can try lots of different peptides. It depends on the length. We used to use prodomains of ADAM family members as treatments for cancer. The amino acids are about 100. You can try this.

Dear Tarlan, You may better to search for anticancer peptides, and till I know there are short peptides of multiple activities and You can check them as natural models to design your own peptide. For example:

• Source:Hyalophora cecropia

• Class:Cecropin A (XXA; insects, invertebrates, animals; ZZHa; ZZP)

• Sequence:KWKLFKKIEKVGQNIRDGIIKAGPAVAVVGQATQIAK

• Length:37

• Structure:Helix

• Additional info:2 alpha-helix. Helix1: 5-21; Helix2: 24-37. MOA: It inhibits HIV by suppressing viral gene expression (J Gen Virol 1998; 79:731-40). Transgenic plants: expression of this peptide in rich improved plant resistance to pathogens (Plant Biotechnol J. 2008 Aug;6(6):585-608).

• Crucial residues: The S-S bridge; C-terminal Met

• Activity: Gram+ & Gram-, Virus, Cancer cells

• Net charge:6

• Source:Orange-thighed frog

• Class:Caerin 1.6 (XXA, frog)

• Class:Caerin 1.6 (XXA, frog, amphibians, animals)

• Sequence:GLFSVLGAVAKHVLPHVVPVIAEK

• Length:24

• Structure:Helix

• Additional info:It contains two amphipathic helices separated by a region of less-defined helicity and greater flexibility.

• Crucial residues:CAERIN 1.6.1 Which is missing two residues at the N-terminus losts antimicrobial activity.

• Activity: Gram+ & Gram-, Cancer cells

• Net charge:3

• Source:Australian blue mountains tree frog, Litoria citropa

• Class:Citropin 1.2 (XXA, frog, amphibians, animals)

• Sequence:GLFDIIKKVASVVGGL

• Length:16

• Structure:Unknown

• Additional info:The solution structure is an amphipathic alpha-helix with well-defined hydrophobic and hydrophilic regions.

• Crucial residues: Pro is critical for membrane penetrating (PNAS USA 97: 8245-8250, 2000).

• Activity: Gram+, Fungi, Cancer cells

• Net charge:1

• Source:Cow Bos taurus

• Sequence:GGLRSLGRKILRAWKKYGPIIVPIIRIG

• Length:28

• Structure:Helix

• Additional info:BMAP-28 has broad antimicrobial activities and confers protection in animal models of bacterial infection or sepsis. Furthermore, BMAP-28 and its isomers demonstrated anti-leishmanial activities against intracellular amastigotes within a macrophage infection model. Interestingly, the D-amino acid form is more active against parasites than either BMAP-28 (the L form) or the sequence reversed form (Lynn MA et al 2011 PLoS Negl Trop Dis. 5(5):e1141). Updated 7/2/2011.

• Crucial residues: Pro is critical for membrane penetrating (PNAS USA 97: 8245-8250, 2000).

• Activity: Gram+ & Gram-, Virus, Fungi, Cancer cells

• Net charge:7

All the Best

SATPdb will be helpful to you for designing anticancer peptides with no toxicity to normal cells

SATPdb: a database of structurally annotated therepeutic peptides.

http://crdd.osdd.net/raghava/satpdb/

paper link

http://nar.oxfordjournals.org/content/early/2015/11/01/nar.gkv1114.full

You can also try PEPstrMOD: structure prediction of peptides containing natural, non-natural and modified residues (http://osddlinux.osdd.net/raghava/pepstrmod/)

paper link (http://www.biologydirect.com/content/10/1/73).

You can design your peptide with desired secondary structure or specific dihedral angle for specific residues plus much more utilities for peptide prediction and designing.