Cell penetrating peptide TAT can kill cancer cells via membrane disruption after attachment of camptothecin.
Peptides
; 63: 143-9, 2015 Jan.
Article
en En
| MEDLINE
| ID: mdl-25496911
ABSTRACT
Attachment of traditional anticancer drugs to cell penetrating peptides is an effective strategy to improve their application in cancer treatment. In this study, we designed and synthesized the conjugates TAT-CPT and TAT-2CPT by attaching camptothecin (CPT) to the N-terminus of the cell penetrating peptide TAT. Interestingly, we found that TAT-CPT and especially TAT-2CPT could kill cancer cells via membrane disruption, which is similar to antimicrobial peptides. This might be because that CPT could perform as a hydrophobic residue to increase the extent of membrane insertion of TAT and the stability of the pores. In addition, TAT-CPT and TAT-2CPT could also kill cancer cells by the released CPT after they entered cells. Taken together, attachment of CPT could turn cell penetrating peptide TAT into an antimicrobial peptide with a dual mechanism of anticancer action, which presents a new strategy to develop anticancer peptides based on cell penetrating peptides.
Palabras clave
Texto completo:
1
Base de datos:
MEDLINE
Asunto principal:
Fragmentos de Péptidos
/
Camptotecina
/
Productos del Gen tat del Virus de la Inmunodeficiencia Humana
/
Péptidos de Penetración Celular
/
Antineoplásicos Fitogénicos
Límite:
Humans
Idioma:
En
Revista:
Peptides
Año:
2015
Tipo del documento:
Article
País de afiliación:
China