Synthesis of biologically active pentapeptide analogs of the N-terminal part of lipoprotein from the outer membrane of Escherichia coli.

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Abstract
The lipoprotein1) from the outer membrane of Escherichia coli and other Enterobacteriaceae is a potent polyclonal activator for B lymphocytes. To determine the molecular structure responsible for the biological activities of lipoprotein, a series of oligopeptide analogs of its N-terminal part were synthesized. 2,3) S-[2,3-bis(palmitoyloxy)-(2-RS)-propyl]-N-palmitoyl-(R)-cysteinyl-(S)-seryl-(S)-seryl-(S)-asparaginyl-(S)-alanine was an active mitogen and polyclonal B lymphocyte activator in vitro and in vivo. 4.apprx.6) It also supplements Salmonella vaccins. 7) In this paper we describe a new synthesis of S-[2,3-bis(palmitoyloxy)-(2R and 2S)-propyl]-N-palmitoyl-(R)-cysteinyl-(S)-seryl-(S)-asparaginyl-(S)- alanine (1 and 3) and their N-(2,2,2,-trichloroethoxycarbonyl) (2 and 4) by using the N-(2,2,2-trichloroethoxycarbonyl)cysteinyl intermediates, which prevents the racemization of their cysteinyl parts in the condensation steps.