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Water‐soluble fatty acid derivatives as acylating agents for reversible lipidization of polypeptides
Author(s) -
Hossein Ekrami,
Ann R. Kennedy,
WeiChiang Shen
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00910-2
Subject(s) - palmitic acid , chemistry , conjugate , peptide , cysteine , yield (engineering) , fatty acid , aqueous solution , biochemistry , chromatography , organic chemistry , stereochemistry , enzyme , mathematical analysis , materials science , mathematics , metallurgy
A novel method allowing the conjugation of a fatty acid to a peptide or protein in aqueous buffer is described in this paper. l ‐Cysteinyl 2‐pyridyl disulfide (CPD) (III), which was obtained by reacting l ‐cysteine (I) with 2,2‐dithiopyridine (II), was reacted with the N ‐hydroxysuccinimide ester of palmitic acid (IV) to yield a water‐soluble derivative of palmitic acid, termed Pal‐CPD (V). Pal‐CPD (V) could be reacted with a sulfhydryl‐containing peptide or protein in aqeous buffer to yield the palmitic acid‐derivatized conjugate (VI). The palmitic acid‐derivatized Bowman‐Birk protease inhibitor (BBI), synthesized using this conjugation method, was demonstrated to have 140‐fold higher uptake into Caco‐2 cell monolayers compared to native‐BBI. The biological activity of the conjugate, as assessed using an in vitro transformation assay, was retained.