| Human prostate tumor cell invasion and metastasis rely, in part, on cellular adhesion to extracellular matrix proteins and cell migration. A synthetic D-amino acid peptide, HYD1 (KIKMVISWKG), was previously identified to promote adhesion in tumor cells originating from breast, prostate, ovarian, and pancreatic tissues. To identify the minimal bioactive sequence of HYD1, alanine substitution and peptide truncation analyses were conducted using the PC3N prostate cancer cell line. Bioactivity was assessed through cell adhesion, migration, and ERK signaling assays. The segment KMVIXW was critical for cell adhesion, while effective migration inhibition required the sequence XKMVISWXX. Activation of ERK signaling was associated with the sequence IKMVISWXX. The shortest peptide capable of performing all three functions was ISWKG. HYD1 contains overlapping functional domains essential for promoting adhesion, blocking migration, and activating ERK signaling. These findings offer a foundation for developing new compounds targeting cancer cell adhesion and migration.
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