Erratum

Purification of recombinantly expressed and cytotoxic human amyloid-beta peptide 1–42

“…Recombinant A␤(1-42) purification methods described so far are complicated [18], end with A␤(1-42) fusion proteins [19] or only parts of A␤(1-42) are expressed and purified [20].…”

Metal complexes designed to bind to amyloid-β for the diagnosis and treatment of Alzheimer's disease

“…The methionine is oxidised during the production of the monomeric peptide but maintains similar properties to the non-oxidised Ab 42 . 54 A single 35Mox Ab 42 protofilament consists of two b-sheets (b1 and b2) that run along the fibril axis forming a parallel b-sandwich stabilized by inter-bsheet side-chain interactions. Residues 17-26 define sheet b1 and residues 31-42 form sheet b2 with a connecting loop containing residues 27-30.…”

“…The methionine is oxidised during the production of the monomeric peptide but maintains similar properties to the non-oxidised Ab 42 . 54 the side-chains of residues Asp23 and Lys28. Residue Lys28 also forms close contacts with residues Ile32 and Leu34 of b2.…”

Polyhistidine Affinity Chromatography: From the Idea to a Method of Broad Applicability and the Pitfalls in-between

“…The rest was noncleaved fusion protein still containing the histidine tail and the NANP-repeat sequence. [8] Transfer of the Amyloid Peptide into a Physiological Buffer…”

“…The entire procedure comprised four columns: a first Ni-NTA column to purify the fusion protein, a C18-HPLC column for CNBr cleavage, a sulfopropyl column to transfer the peptide from an acidic milieu to a neutral milieu and a second Ni-NTA column to remove the fusion protein. [8] The sulfopropyl and the Ni-NTA columns were operated in a tandem configuration where the Ni-NTA acted more like a filter by allowing the peptide to pass quickly but retaining the fusion protein. This allowed the procedure to be accomplished within minutes.…”