Unknown

Dataset Information

0

Discovery of peptide inhibitors targeting human programmed death 1 (PD-1) receptor.


ABSTRACT: Blocking the interaction of human programmed death 1 (hPD-1) and its ligand hPD-L1 has been a promising immunotherapy in cancer treatment. In this paper, using a computational de novo peptide design method, we designed several hPD-1 binding peptides. The most potent peptide Ar5Y_4 showed a KD value of 1.38 ± 0.39 ?M, comparable to the binding affinity of the cognate hPD-L1. A Surface Plasmon Resonance (SPR) competitive binding assay result indicated that Ar5Y_4 could inhibit the interaction of hPD-1/hPD-L1. Moreover, Ar5Y_4 could restore the function of Jurkat T cells which had been suppressed by stimulated HCT116 cells. Peptides described in this paper provide promising biologic candidates for cancer immunotherapy or diagnostics.

SUBMITTER: Li Q 

PROVIDER: S-EPMC5323130 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Discovery of peptide inhibitors targeting human programmed death 1 (PD-1) receptor.

Li Qiao Q   Quan Lina L   Lyu Jiankun J   He Zenghui Z   Wang Xia X   Meng Jiajia J   Zhao Zhenjiang Z   Zhu Lili L   Liu Xiaofeng X   Li Honglin H  

Oncotarget 20161001 40


Blocking the interaction of human programmed death 1 (hPD-1) and its ligand hPD-L1 has been a promising immunotherapy in cancer treatment. In this paper, using a computational de novo peptide design method, we designed several hPD-1 binding peptides. The most potent peptide Ar5Y_4 showed a KD value of 1.38 ± 0.39 μM, comparable to the binding affinity of the cognate hPD-L1. A Surface Plasmon Resonance (SPR) competitive binding assay result indicated that Ar5Y_4 could inhibit the interaction of h  ...[more]

Similar Datasets

| S-EPMC7416570 | biostudies-literature
| 2368689 | ecrin-mdr-crc
| S-EPMC5058683 | biostudies-literature
| S-EPMC4752817 | biostudies-literature
| S-EPMC3863817 | biostudies-other
| S-EPMC7481633 | biostudies-literature
| S-EPMC8928662 | biostudies-literature
| S-EPMC5363530 | biostudies-literature
| S-EPMC6986404 | biostudies-literature
| S-EPMC6803548 | biostudies-literature