1hu5
From Proteopedia
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SOLUTION STRUCTURE OF OVISPIRIN-1
Overview
We studied three model antibacterial peptides that resembled the, N-terminal 18 amino acids of SMAP-29, an alpha-helical, antimicrobial, peptide of sheep. Although the parent compound, ovispirin-1 (KNLRR IIRKI, IHIIK KYG), was potently antimicrobial, it was also highly cytotoxic to, human epithelial cells and hemolytic for human erythrocytes. Single, residue substitutions to ovispirin-1 yielded two substantially less, cytotoxic peptides (novispirins), with intact antimicrobial properties., One of these, novispirin G-10, differed from ovispirin-1 only by, containing glycine at position 10, instead of isoleucine. The other, novispirin T-7, contained threonine instead of isoleucine at position 7., We determined the three-dimensional solution structures of all three, peptides by circular dichroism spectroscopy and two-dimensional nuclear, magnetic resonance spectroscopy. Although all retained an amphipathic, helical structure in 2,2,2-trifluoroethanol, they manifested subtle, fine-structural changes that evidently impacted their activities greatly., These findings show that simple structural modifications can 'fine-tune', an antimicrobial peptide to minimize unwanted cytotoxicity while retaining, its desired activity.
About this Structure
1HU5 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides., Sawai MV, Waring AJ, Kearney WR, McCray PB Jr, Forsyth WR, Lehrer RI, Tack BF, Protein Eng. 2002 Mar;15(3):225-32. PMID:11932493
Page seeded by OCA on Sun Nov 25 03:04:36 2007
