Residue-based control of helix shape in beta-peptide oligomers
Article Abstract:
Recent research has indicated that short beta-peptides of trans-APC very frequently adopt a 12-helical folding pattern. This has relevance to other research which shows the formation of 14-helix patterns by short oligomers of beta-substituted beta-amino acids. It seems likely that changing torsional preferences about the C-alpha-C-beta bonds of individual residues can have a significant impact on beta-peptide secondary structure. Beta-peptides offer predictable residue-based conformational control, and may therefore be well suited to molecular design efforts.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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A peptide antibiotic from human skin
Article Abstract:
Animals and plants use antimicrobial peptides in their epithelia to avoid opportunistic infections. Research shows that the human skin in contact with microorganisms contains an antimicrobial shield of inducible endogenous peptide antibiotics. The peptide, isolated from human psoriatic skin, has been termed human beta-defensin-2 and is active against yeasts and Gram-negative bacteria. It is the second beta-defensin to be found in humans.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Non-haemolytic beta-amino-acid oligomers
Article Abstract:
A beta-amino-acid oligomer (beta-peptide) that mimics the activity of medium-sized peptides used by host organisms as a defence against microbial invasion has been developed. The beta-peptide was found to be effective against four bacterial species.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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