Open AccessAn approach to the targeted attachment of peptides and proteins to solid supports.
Author(s) -
Klaus Hofmann,
Yoshiaki Kiso
Publication year - 1976
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.73.10.3516
Subject(s) - avidin , biotinylation , biocytin , biotin , amide , peptide , avidity , chemistry , biochemistry , combinatorial chemistry , molecule , sepharose , antibody , biology , organic chemistry , endocrinology , immunology , enzyme , central nervous system
A novel approach to affinity columns is described that is based on the high avidity of biotinylated molecules for avidin attached to solid supports. Biocytin amide [Nepsilon-(+)-biotinyllysine amide] was coupled to the COOH-terminal carboxyl group of corticotropin(1-24) [ACTH(1-24)] to form [biocytin25]ACTH(1-25) amide. The ability of this peptide to stimulate steroidogenesis of bovine adrenocortical cells was within experimental error identical to that of ACTH(1-24). The peptide also binds to avidin and avidin-Sepharose, forming stable complexes. Thus, with biotin as the anchor, the adrenocorticotropically active segment of the ACTH molecule was attached to a solid support in a targeted manner. The general applicability of this principle for the attachment of peptides and proteins to solid supports is discussed.