caa a22 4500 477136869 CHVBK 20180405111721.0 cr unu---uuuuu 170330e19970101xx s 000 0 eng 10.1007/BF00127968 doi (NATIONALLICENCE)springer-10.1007/BF00127968 Selective dimerization of cysteines in glycopeptides and phosphopeptides [Elektronische Daten] [Ralf Hoffmann, Laszlo Otvos Jr.] Summary: To study the influence of phosphorylation and oxidation on the repeat domains of human Tau protein, we faced the challenge to selectively dimerize two cysteine-containing peptides in the presence of a nearby phosphate group. To this end, we were able to demonstrate the utility of a selective dimerization approach by forming disulfide bonds in unprotected phosphopeptides and extended the methodology to unprotected glycopeptides. Activation of one cysteine of a peptide chain with 2,2′-dithiodipyridine and coupling this thiopyridyl-peptide to another peptide chain, containing an unprotected cysteine residue, yielded the mixed dimers in high purities and reasonable yields. Phosphate or sugar side chains on either peptide component remained unaffected during the activation and dimerization processes. While for mixed dimers the activated peptides were isolated by chromatography, homodimers were obtained by a simple one-pot reaction after 1 h. We demonstrate that cysteines can be dimerized in unprotected phosphopeptides and glycopeptides, without any side reactions affecting these posttranslational modifications. ESCOM Science Publishers B.V., 1997 Alzheimer's disease nationallicence Disulfide bond formation nationallicence Peptide nationallicence Repeat domains nationallicence Tau protein nationallicence Thiopyridyl activation nationallicence DCM : dichloromethane nationallicence DMF : N,N′-dimethylformamide nationallicence DTP : 2,2′-dithiodipyridine nationallicence Fmoc : 9-fluorenylmethyloxycarbonyl nationallicence HPLC : high-performance liquid chromatography nationallicence MALDI : matrix-assisted laser desorption/ionization nationallicence MS : mass spectrometry nationallicence NFT : neurofibrillary tangles nationallicence PHF : paired helical filaments nationallicence PKC : protein kinase C nationallicence RP : reversed phase nationallicence τ : human Tau protein nationallicence TFA : trifluoroacetic acid nationallicence Hoffmann Ralf The Wistar Institute, 3601 Spruce Street, 19104, Philadelphia, PA, U.S.A. aut Otvos Jr. Laszlo The Wistar Institute, 3601 Spruce Street, 19104, Philadelphia, PA, U.S.A. aut Letters in Peptide Science Kluwer Academic Publishers 3/6(1997-01-01), 371-377 0929-5666 3:6<371 1997 3 10989 https://doi.org/10.1007/BF00127968 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00127968 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Hoffmann Ralf The Wistar Institute, 3601 Spruce Street, 19104, Philadelphia, PA, U.S.A aut NATIONALLICENCE 700 1- Otvos Jr Laszlo The Wistar Institute, 3601 Spruce Street, 19104, Philadelphia, PA, U.S.A aut NATIONALLICENCE 773 0- Letters in Peptide Science Kluwer Academic Publishers 3/6(1997-01-01), 371-377 0929-5666 3:6<371 1997 3 10989 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer