Abstract
Various heterobifunctional glycopeptides containing both 3′‐sulfated Lewis x and peptides containing at least one sulfated tyrosine were constructed onto a pentaerythritol backbone following a common strategy that relies on the condensation, through reductive amination, of aldehydes 9 or 17 with various peptides having a free terminal amino group. The corresponding homodimer of 3′‐sulfated Lewis x linked to pentaerythritol was prepared for comparison of the inhibitory activities. †This paper is dedicated to Professor Gérard Descotes on the occasion of his 70th birthday.
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