For therapeutic agents to exert their pharmacological effects, need to cross the biological membranes and enter into the systemic circulation to reach the site of action. A 16 amino acid long testis specific THP3 peptide identified using phage display approach was synthesized by solid phase peptide synthesis, purified using RP-HPLC and characterized by mass spectrometry (MALDI). The CD spectra of THP-3 peptide obtained in water and apolar solvents like trifluroethanol and hexafluroisopropanol. The peptide in water adopted mostly beta and coiled structures. Addition of apolar solvents led to significant changes in CD spectra of peptide due to decrease in dielectric constants. These changes in conformations of testis specific homing peptides may be play a role in molecular interaction of peptide and plasma membrane of the testicular cells.
Blood-testis barrier, Peptide, CD spectra, Conformation, Ellipticity
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