• Devjani Banerjee Ashok & Rita Patel Institute of Integrated Study & Research In Biotechnology And Allied Sciences (ARIBAS), New V V Nagar, Gujarat. India
  • Tejas Gohil Sardar Patel University, ARIBAS, Anand
  • Sunil Trivedi Smt. L P Patel Institute Of Medical Laboratory Tech


Antimicrobial peptide (AMPs), Capra hircus (Goat), Defensin, Mass spectrometry, Oligomerization


Objective: The aim of the present study was to isolate an antimicrobial peptide from heart tissue of Capra hircus (Goat) and to check its antibacterial activity against antibiotic resistant and antibiotic sensitive bacterial strains.

Methods: Total protein was extracted from heart tissue of goat using extraction buffer, purified by cation exchange column chromatography and tested in vitro for antibacterial activity against MTCC bacterial strains as well as clinical isolates using the agar well diffusion method. MIC was also checked by microbroth dilution method. Mass spectrometry was performed for partially purified protein fraction.

Results: The present work revealed that crude protein extracted from the heart tissue of goat was found to have antimicrobial activity. Partially purified protein fraction also showed the zone of inhibition and MIC value against all the bacteria tested. Mass spectrometry data showed the molecular weight of the peptide to be ~6.5 kD along with peptide to be present in the oligomeric form.

Conclusion: The present study showed that the defens in is an antimicrobial peptide with broad range of effect which is present in dimer, trimer and oligomeric form.



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Author Biography

Tejas Gohil, Sardar Patel University, ARIBAS, Anand

Integrated Biotechnology, PhD Scholar


Zasloff M. Antimicrobial peptides of multicellular organisms. Nat 2002;415:389-95.

Bechinger B. The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy. Biochim Biophys Acta 1999;1462:157-83.

Zhu Q, Hu J, Mulay S, Esch F, Shimasaki S. Structure of novel human graneulocyte peptide with anti-ACTH activity. Natl Acad Sci USA 1987;85:592-5.

Daher KA, Selsted ME, Lehrer RI. Direct inactivation of viruses by human granulocyte defensins. J Virol 1986;60:1068-74.

Lehrer RI, Ganz T. Defensins of vertebrate animals. Curr Opin Immunol 2002;14:96–102.

Matutte B, Storey KB, Knoop FC, Conlon JM. Induction of synthesis of an antimicrobial peptide in the skin of the freeze tolerant frog, Rana sylvatica, in response to environmental stimuli. FEBS 2000;483:135-8.

CLSI: Performance standards for antimicrobial susceptibility testing; Twenty-First information supplement. Clinical Laboratory Standard Institute 2011;M100 Suppl 30:S-21.

Taneja, Sharma. ESBL’s detection in clinical microbiology: why and how? Indian J Med Res 2008;127:297-300.

Townsend SM, Hurrell E, Caubill-Barron J, Loc-Carrillo C, Forsythe SJ. Characterization of an extended-spetrum beta lactamase Enteobacter hormaechei nosocomial outbreak, and other Enterobacter hormaechei misidentified as Cronobacter (Enterobacter) sakazaki. Microbiol 2008;154:3659-67.

Suresh A, Verma C. Modelling study of dimerization in mammalian defensins. BMC Bioinf 2006;7:S17.

Hoover DM, Rajashankar KR, Bluementhal R, Puri A, Oppenheim JJ, Chertov O, et al. The structure of human ï¢-defensin-2 shows evidence of higher order oligomerization. J Biol Chem 2000;275:32911-8.



How to Cite

Banerjee, D., T. Gohil, and S. Trivedi. “ANTIMICROBIAL ACTIVITY OF OLIGOMERIC β–DEFENSIN ISOLATED FROM HEART TISSUE OF CAPRA HIRCUS”. International Journal of Pharmacy and Pharmaceutical Sciences, vol. 7, no. 3, Mar. 2015, pp. 131-5,



Original Article(s)