@article{d109b0e906da49038bf261db6ef0d67c,
title = "Modulation of co-stimulatory signal from CD2–CD58 proteins by a grafted peptide",
abstract = "Peptides were designed to inhibit the protein–protein interaction of CD2 and CD58 to modulate the immune response. This work involved the design and synthesis of eight different peptides by replacing each amino acid residue in peptide 6 with alanine as well as grafting the peptide to the sunflower trypsin-inhibitor framework. From the alanine scanning studies, mutation at position 2 of the peptide was shown to result in increased potency to inhibit cell adhesion interactions. The most potent peptide from the alanine scanning was further studied for its detailed three-dimensional structure and binding to CD58 protein using surface plasmon resonance and flow cytometry. This peptide was used to graft to the sunflower trypsin inhibitor to improve the stability of the peptide. The grafted peptide, SFTI-a1, was further studied for its potency as well as its thermal, chemical, and enzymatic stability. The grafted peptide exhibited improved activity compared to our previously grafted peptide and was stable against thermal and enzymatic degradation.",
keywords = "CD2, CD58, alanine scanning, cell adhesion, immunomodulation, protein–protein interaction",
author = "Pravin Parajuli and Rushikesh Sable and Leeza Shrestha and Achyut Dahal and Ted Gauthier and Veena Taneja and Seetharama Jois",
note = "Funding Information: Part of the funding for this project was supported by the National Institute of General Medical Sciences of the National Institute of Health under grant number GM103424. R. Sable was supported by the Louisiana Biomedical Research Network an Institutional Development Award (IDeA) from the National Institute of General Medical Sciences?of the National Institutes of Health under grant number P20 GM103424 and the LBRN Summer Research Program supported by the Louisiana of Board of Regents under grant number?LEQSF(2015-20)-INBRE-Match. The authors would like to thank the NMR and mass spectrometry facility at Louisiana State University, Baton Rouge. We would also like to thank the BBC core facility and HPC, LONI, for the computational facility. Funding Information: Part of the funding for this project was supported by the National Institute of General Medical Sciences of the National Institute of Health under grant number GM103424. R. Sable was supported by the Louisiana Biomedical Research Network an Institutional Development Award (IDeA) from the National Institute of General Medical Sciences of the National Institutes of Health under grant number P20 GM103424 and the LBRN Summer Research Program supported by the Louisiana of Board of Regents under grant number LEQSF(2015‐20)‐INBRE‐Match. The authors would like to thank the NMR and mass spectrometry facility at Louisiana State University, Baton Rouge. We would also like to thank the BBC core facility and HPC, LONI, for the computational facility. Publisher Copyright: {\textcopyright} 2020 John Wiley & Sons A/S.",
year = "2021",
month = mar,
doi = "10.1111/cbdd.13797",
language = "English (US)",
volume = "97",
pages = "607--627",
journal = "Chemical Biology and Drug Design",
issn = "1747-0277",
publisher = "Blackwell",
number = "3",
}