Structure-Activity Studies on Antiproliferative Factor (APF) Glycooctapeptide Derivatives.

ABSTRACT: Antiproliferative factor (APF), a sialylated glycopeptide secreted by explanted bladder epithelial cells from interstitial cystitis/painful bladder syndrome (IC/PBS) patients, and its unsialylated analogue (as-APF) significantly decrease proliferation of bladder epithelial cells and/or certain carcinoma cell lines in vitro. We recently reported a structure-activity relationship profile for the peptide portion of as-APF and revealed that truncation of the C-terminal alanine did not significantly affect antiproliferative activity. To better understand the structural basis for the maintenance of activity of this truncated eight amino acid as-APF (as-APF8), we synthesized several amino acid-substituted derivatives and studied their ability to inhibit bladder epithelial cell proliferation in vi

SUBMITTER: Kaczmarek P 

PROVIDER: S-EPMC4007904 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature