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Indian Journal of Biochemistry and Biophysics (IJBB) >
IJBB Vol.48 [2011] >
IJBB Vol.48(5) [October 2011] >
| Title: | Structure-activity relationship of buffalo antibacterial hepcidin analogs |
| Authors: | Chanu, Khangembam Victoria
Kumar, Ashok
Kumar, Satish |
| Keywords: | Anti-microbial peptide
Circular dichroism spectroscopy
 -Structure
Minimum inhibitory concentration
Hepcidin analogs
Staphylococcus aureus
E. coli |
| Issue Date: | Oct-2011 |
| Publisher: | NISCAIR-CSIR, India |
| Abstract: | Hepcidin is an anti-microbial peptide
expressed predominantly in the liver of many species. Based on the amino acid
sequence deduced from buffalo (Bubalus bubalis) hepcidin cDNA (Accession
no. EU399814), six peptides Hepc1-25,
Hepc6-25, Hepc7-25, Hepc9-25, Hepc11-25
and Hepc15-25 were synthesized using solid-phase
fluorenylmethoxycarbonyl (Fmoc) chemistry. CD spectroscopy revealed different
spectra of the peptides in different solvents and in all the cases b-structure was found to be dominant with less a-helix as predicted. Quantitation of secondary structure indicated
the highest
b-structure for all the six peptides in SDS solution, when used as
mimetic for membrane-like environment. The CD spectra of all the peptides taken
in water showed that degree of randomness decreased with increase in chain
length of the peptide. Out of the six peptides, only Hepc1-25, Hepc6-25
and Hepc7-25 showed antibacterial activity against Staphylococcus
aureus (Gram-positive bacteria).
The peptides did not show any sensitivity toward E. coli (Gram-negative
bacteria). Minimum inhibitory concentration (MIC) showed the lowest value for
Hepc7-25 as an antibacterial agent, followed by Hepc6-25 and
Hepc1-25. The peptides Hepc9-25, Hepc11-25 and
Hepc15-25 with more random structure did not show any antimicrobial
activity The study demonstrated that 5 amino acids at N-terminal in buffalo
hepcidin can be truncated without loss of antimicrobial activity and further
reduction of length of the analog from 20 to 19 amino acids resulted increase
in the activity because of increase in -structure of the peptide shown by CD
spectroscopy. |
| Page(s): | 325-330 |
| CC License: |  CC Attribution-Noncommercial-No Derivative Works 2.5 India |
| ISSN: | 0975-0959 (Online); 0301-1208 (Print) |
| Source: | IJBB Vol.48(5) [October 2011]
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