Browsing by Author "Chaikof, Elliot"

Now showing items 1-4 of 4

    • Glycopeptide Analogues of PSGL-1 Inhibit P-Selectin In Vitro and In Vivo 

      Krishnamurthy, Venkata R; Sardar, Mohammed Y. R.; Yu, Ying; Song, Xuezheng; Haller, Carolyn; Dai, Erbin; Wang, Xiacong; Hanjaya-Putra, Donny; Sun, Lijun; Morikis, Vasilios; Simon, Scott I.; Woods, Robert; Cummings, Richard D.; Chaikof, Elliot L. (2015)
      Blockade of P-selectin/PSGL-1 interactions holds significant potential for treatment of disorders of innate immunity, thrombosis, and cancer. Current inhibitors remain limited due to low binding affinity or by the recognized ...

    • An immobilized liquid interface prevents device associated bacterial infection in vivo 

      Chen, Jiaxuan; Howell, Caitlin; Haller, Carolyn A; Patel, Madhukar S; Ayala, Perla; Moravec, Katherine A.; Dai, Erbin; Liu, Liying; Sotiri, Irini; Aizenberg, Michael; Aizenberg, Joanna; Chaikof, Elliot L. (Elsevier BV, 2017)
      Virtually all biomaterials are susceptible to biofilm formation and, as a consequence, device-associated infection. The concept of an immobilized liquid surface, termed slippery liquid-infused porous surfaces (SLIPS), ...

    • In situ regeneration of bioactive coatings enabled by an evolved Staphylococcus aureus sortase A 

      Ham, Hyun Ok; Qu, Zheng; Haller, Carolyn A.; Dorr, Brent M.; Dai, Erbin; Kim, Wookhyun; Liu, David R.; Chaikof, Elliot L. (Nature Publishing Group, 2016)
      Surface immobilization of bioactive molecules is a central paradigm in the design of implantable devices and biosensors with improved clinical performance capabilities. However, in vivo degradation or denaturation of surface ...

    • Reprogramming the specificity of sortase enzymes 

      Dorr, Brent; Ham, Hyun Ok; An, Chihui; Chaikof, Elliot L.; Liu, David Ruchien (Proceedings of the National Academy of Sciences, 2014)
      Staphylococcusaureus sortase A catalyzes the transpeptidation of an LPXTG peptide acceptor and a glycine-linked peptide donor and has proven to be a powerful tool for site-specific protein modification. The substrate ...