<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>1(8)</volume><submitter>Kaczmarek P</submitter><pubmed_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</pubmed_abstract><journal>ACS medicinal chemistry letters</journal><pagination>390-4</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4007904</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Structure-Activity Studies on Antiproliferative Factor (APF) Glycooctapeptide Derivatives.</pubmed_title><pmcid>PMC4007904</pmcid><pubmed_authors>Grkovic D</pubmed_authors><pubmed_authors>Tocci GM</pubmed_authors><pubmed_authors>Guo L</pubmed_authors><pubmed_authors>Zhang CO</pubmed_authors><pubmed_authors>Adams KM</pubmed_authors><pubmed_authors>Barchi JJ</pubmed_authors><pubmed_authors>Kaczmarek P</pubmed_authors><pubmed_authors>Michejda CJ</pubmed_authors><pubmed_authors>Keay SK</pubmed_authors><pubmed_authors>Koch KR</pubmed_authors></additional><is_claimable>false</is_claimable><name>Structure-Activity Studies on Antiproliferative Factor (APF) Glycooctapeptide Derivatives.</name><description>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</description><dates><release>2010-01-01T00:00:00Z</release><publication>2010 Nov</publication><modification>2025-04-05T10:37:31.922Z</modification><creation>2019-03-27T01:27:30Z</creation></dates><accession>S-EPMC4007904</accession><cross_references><pubmed>24900223</pubmed><doi>10.1021/ml100087a</doi></cross_references></HashMap>