LEADER 03894nam 22006375 450 001 996597072303316 005 20240530135844.0 010 $a3-319-65639-2 024 7 $a10.1007/978-3-319-65639-7 035 $a(CKB)4100000001037499 035 $a(DE-He213)978-3-319-65639-7 035 $a(MiAaPQ)EBC5589137 035 $a(Au-PeEL)EBL5589137 035 $a(OCoLC)1066193920 035 $a(MiAaPQ)EBC6422716 035 $z(PPN)258872799 035 $a(PPN)221254714 035 $a(EXLCZ)994100000001037499 100 $a20171103d2018 u| 0 101 0 $aeng 135 $aurnn#008mamaa 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 10$aSelf-Assembled Molecules ? New Kind of Protein Ligands $eSupramolecular Ligands /$fedited by Irena Roterman, Leszek Konieczny 205 $a1st ed. 2018. 210 $cSpringer International Publishing$d2018 210 1$aCham :$cSpringer International Publishing :$cImprint: Springer,$d2018. 215 $a1 online resource (XII, 136 p. 98 illus., 44 illus. in color.) 311 $a3-319-65638-4 327 $aSupramolecular Protein Ligands ? Unexplored Teritory Of Potential Pharmacological Activity -- Supramolecular Congo Red As Specific Ligand Of Antibodies Engaged In Immune Complex -- Protein Conditioning For Binding Congo Red And Other Supramolecular Ligands -- Metal Ions Introduced To Proteins By Supramolecular Ligands -- Possible Mechanism Of Amyloidogenesis Of V Domains -- Supramolecular Structures As Carrier Systems Enabling The Use Of Metal Ions In Antibacterial Therapy -- Congo Red Interactions With Single-Walled Carbon Nanotubes. 330 $aThis book is an open access under a CC BY license. The subject of this book relates to protein ligands with particular structural and complexation properties. They are composed of self-assembled molecules, capable of penetrating as a unit into proteins outside the binding site. The ribbon-like supramolecular system only permits the penetration of self-assembled molecules into the protein-body and formation of stable complexes. Supramolecular Congo red and similar compounds fit these requirements. Destabilized protein fragments enable the penetration of such ligands, with susceptibility to supramolecular ligand binding often associated with protein function. As a result, complexation modifies their functional effects. The activity of enzymes is inhibited by arresting them in the complexed state, but ?naturally irreversible? complexation as in the case of immune complexation, is enhanced instead. This property offers many attractive possibilities of using supramolecular ligands as described in this book. 606 $aMedicine 606 $aProteins  606 $aBiology?Technique 606 $aBiomedicine, general$3https://scigraph.springernature.com/ontologies/product-market-codes/B0000X 606 $aProtein Science$3https://scigraph.springernature.com/ontologies/product-market-codes/L14040 606 $aProtein-Ligand Interactions$3https://scigraph.springernature.com/ontologies/product-market-codes/L14060 606 $aBiological Techniques$3https://scigraph.springernature.com/ontologies/product-market-codes/L28000 615 0$aMedicine. 615 0$aProteins . 615 0$aBiology?Technique. 615 14$aBiomedicine, general. 615 24$aProtein Science. 615 24$aProtein-Ligand Interactions. 615 24$aBiological Techniques. 676 $a610 702 $aRoterman$b Irena$4edt$4http://id.loc.gov/vocabulary/relators/edt 702 $aKonieczny$b Leszek$4edt$4http://id.loc.gov/vocabulary/relators/edt 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a996597072303316 996 $aSelf-Assembled Molecules ? New Kind of Protein Ligands$94153803 997 $aUNISA