Design of S–S bond containing maleimide-conjugated closo-dodecaborate (SSMID): identification of unique modification sites on albumin and investigation of intracellular uptake. Issue 22 (12th April 2019)

• Record Type: Journal Article
• Authors: Ishii, Satomu; Sato, Shinichi; Asami, Hiroya; Hasegawa, Tomoko; Kohno, Jun-Ya; Nakamura, Hiroyuki
• Is Part Of: Organic & biomolecular chemistry. Volume 17:Issue 22(2019)
• Page Start: 5496
• Page End: 5499
• Publication Date: 2019-04-12
• Subjects: Chemistry, Organic -- Periodicals; Bioorganic chemistry -- Periodicals; Chemistry, Physical organic -- Periodicals; 547
• DOI: 10.1039/c9ob00584f
• Languages: English
• ISSNs: 1477-0520

Abstract

Abstract : The S–S bond containing maleimide-conjugated closo -dodecaborate (SSMID) was synthesised to identify the binding sites in bovin serum albumin (BSA). Abstract : An S–S bond containing maleimide-conjugated closo -dodecaborate (SSMID) was synthesised for identification of albumin binding sites. Three Lys residues, Lys221, Lys413 and Lys431, were identified as SSMID modification sites in addition to Cys34 in bovin serum albumin (BSA). Fluorescent-labelled MID-BSA was found to be accumulated in the cytosol of HeLa cells.