ISSN: 0973-7510

E-ISSN: 2581-690X

Vikas D. Dighe1, Arvind Kumar Singh1, Dimpal Thakuria1 and Satish Kumar1
1Division of Animal Biotechnology, Indian Veterinary Research Institute, Izaatnagar-243122, India.
J Pure Appl Microbiol. 2014;8(5):4171-4176
© The Author(s). 2014
Received: 12/05/2014 | Accepted: 30/06/2014 | Published: 31/10/2014

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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© The Author(s) 2014. Open Access. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License which permits unrestricted use, sharing, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.