CKS-17

CKS-17 is a synthetic retroviral envelope peptide whose sequence is homologous to the endogenous retroviral transmembrane envelope protein. It has been shown to suppress a variety of immune functions, dysregulate cytokines, and elevate intracellular cAMP. CKS-17 is a heptadecapeptide that isolated from a highly conserved area of the immunosuppressive retroviral envelope protein p15E. Dimerization of CKS-17 is achieved through cysteine-disulfide linkage, and its dimer has a naturally existing cysteine at the carboxyl terminus, which appears in the retroviral peptides based on CKS-17. It has ability to immunosuppressive activity both in vitro and in vivo.

Previous studies have revealed that CKS-17 peptide inhibits monocyte superoxide generation, natural killer cell activity, polyclonal B-cell activation, and monocyte-mediated killing via inactivating interleukin-1. CKS-17 is covalently attached to bovine serum albumin to form a CKS-17-BSA conjugate, which inhibits the proliferation of lymphocytes in response to mitogens or alloantigens.