{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T05:30:34Z","timestamp":1787031034588,"version":"build-2736575974"},"reference-count":30,"publisher":"Korean Cancer Association","issue":"2","license":[{"start":{"date-parts":[[2021,8,3]],"date-time":"2021-08-03T00:00:00Z","timestamp":1627948800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/3.0\/"}],"funder":[{"DOI":"10.13039\/501100002855","name":"Chinese Ministry of Science and Technology","doi-asserted-by":"crossref","award":["2014AA020702"],"award-info":[{"award-number":["2014AA020702"]}],"id":[{"id":"10.13039\/501100002855","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100007162","name":"Guangdong Science and Technology Department","doi-asserted-by":"publisher","award":["2016B030231001"],"award-info":[{"award-number":["2016B030231001"]}],"id":[{"id":"10.13039\/501100007162","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100007162","name":"Guangdong Science and Technology Department","doi-asserted-by":"publisher","award":["2017B020230002"],"award-info":[{"award-number":["2017B020230002"]}],"id":[{"id":"10.13039\/501100007162","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["e-crt.org"],"crossmark-restriction":true},"short-container-title":["Cancer Res Treat"],"published-print":{"date-parts":[[2022,4,15]]},"abstract":"<jats:p>PurposeThe purpose of this study was to optimize a peptide (nABP284) that binds to programmed cell death protein 1 (PD-1) by a computer-based protocol in order to increase its affinity. Then, this study aimed to determine the inhibitory effects of this peptide on cancer immune escape by coculturing improving cytokine-induced killer (ICIK) cells with cancer cells.Materials and MethodsnABP284 that binds to PD-1 was identified by phage display technology in our previous study. AutoDock and PyMOL were used to optimize the sequence of nABP284 to design a new peptide (nABPD1). Immunofluorescence was used to demonstrate that the peptides bound to PD-1. Surface plasmon resonance was used to measure the binding affinity of the peptides. The blocking effect of the peptides on PD-1 was evaluated by a neutralization experiment with human recombinant programmed death-ligand 1 (PD-L1) protein. The inhibition of activated lymphocytes by cancer cells was simulated by coculturing of human acute T lymphocytic leukemia cells (Jurkat T cells) with human tongue squamous cell carcinoma cells (Cal27 cells). The anticancer activities were determined by coculturing ICIK cells with Cal27 cells in vitro.ResultsA high-affinity peptide (nABPD1, KD=11.9 nM) for PD-1 was obtained by optimizing the nABP284 peptide (KD=11.8 \u03bcM). nABPD1 showed better efficacy than nABP284 in terms of increasing the secretion of interkeulin-2 by Jurkat T cells and enhancing the in vitro antitumor activity of ICIK cells.ConclusionnABPD1 possesses higher affinity for PD-1 than nABP284, which significantly enhances its ability to block the PD-1\/PD-L1 interaction and to increase ICIK cell-mediated antitumor activity by armoring ICIK cells.<\/jats:p>","DOI":"10.4143\/crt.2021.424","type":"journal-article","created":{"date-parts":[[2021,8,2]],"date-time":"2021-08-02T22:33:55Z","timestamp":1627943635000},"page":"362-374","update-policy":"https:\/\/doi.org\/10.4143\/crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Engineering a High-Affinity PD-1 Peptide for Optimized Immune Cell-Mediated 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