86060-85-7Relevant articles and documents
Mimicking the function of eggshell matrix proteins: The role of multiplets of charged amino acid residues and self-assembly of peptides in biomineralization
Ajikumar, Parayil Kumaran,Vivekanandan, Subramanian,Lakshminarayanan, Rajamani,Jois, Seetharama D. S.,Kini, R. Manjunatha,Valiyaveettil, Suresh
, p. 5476 - 5479 (2005)
(Figure Presented) An eggshell finish: Designed peptides can be used as a tool to unravel the structure-activity relationships of eggshell matrix proteins. The ordered arrangement of doublets of charged residues on the peptide and its self-assembling characteristics play a key role in the biomimetic nucleation of polycrystalline calcite crystal aggregates (see picture), which models that initiated by the goose eggshell matrix protein, ansocalcin.
Synthesis of aryl esters of protected amino acids from aryl sulfonates
Pudhom, Khanitha,Vilaivan, Tirayut
, p. 5939 - 5942 (2007/10/03)
Aryl esters of Boc- and Fmoc-protected amino acids derived from electron-deficient phenols have been prepared in good yields from aryl 4- nitrobenzenesulfonates in the presence of 1-hydroxy-benzotriazole as catalyst.
9-Fluorenylmethyl Pentafluorophenyl Carbonate as a Useful Reagent for the Preparation of N-9-Fluorenylmethyloxycarbonylamino Acids and their Pentafluorophenyl Esters
Schoen, Istvan,Kisfaludy, Lajos
, p. 303 - 305 (2007/10/02)
9-Fluorenylmethyl pentafluorophenyl carbonate is a useful reagent for the efficient, side reaction-free introduction of N-9-fluorenylmethyloxycarbonyl protecting group into amino acids and for the subsequent preparation of their pentafluorophenyl esters.Some new compounds of both types are described.
