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Synthesis and Anti‐Cancer Activity of Cysteine‐Deleted Tachyplesin Analogs
Author(s) -
Eitel Anna,
Hendrickson Nathan,
HeylClegg Deborah,
Evans Hedeel,
Guthrie Jeffrey
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.lb175
Subject(s) - cancer cell , peptide , cancer , chemistry , cysteine , viability assay , cell , population , biochemistry , membrane , mtt assay , antimicrobial peptides , biology , enzyme , medicine , genetics , environmental health
Research investigating anti‐cancer agents is an exciting and important part of medicinal chemistry due to its prevalence in the population. Tachyplesin, an antimicrobial peptide isolated from the horseshoe crab, has been shown to kill cancer cells. The positive charges of the arginine and lysine residues allow for specificity for bacterial and cancer cell membranes, as they are attracted to negatively charged components that these cells express on the surface. The hydrophobic part then penetrates into the lipid membrane, disrupting membrane structure by creating holes and leading to cell death. Our lab has studied a linear version of this peptide, CDT, as an antibiotic, but it had not been tested for effects against cancer cells. In this study, the anti‐cancer effects of CDT and its analogs, where sequence and stereochemical configuration were modified, were studied using A549 lung cancer cells. An MTT assay was performed to calculate percent cell viability with relation to increasing concentrations of peptide. Results indicate that the D‐analogs of CDT have stronger anti‐cancer effects than CDT itself.