Abstract:
:Antimicrobial peptides (AmPs) are small proteins that are used by the innate immune system to combat bacterial infection in multicellular eukaryotes. There is mounting evidence that these peptides are less susceptible to bacterial resistance than traditional antibiotics and could form the basis for a new class of therapeutic agents. Here we report the rational design of new AmPs that show limited homology to naturally occurring proteins but have strong bacteriostatic activity against several species of bacteria, including Staphylococcus aureus and Bacillus anthracis. These peptides were designed using a linguistic model of natural AmPs: we treated the amino-acid sequences of natural AmPs as a formal language and built a set of regular grammars to describe this language. We used this set of grammars to create new, unnatural AmP sequences. Our peptides conform to the formal syntax of natural antimicrobial peptides but populate a previously unexplored region of protein sequence space.
journal_name
Naturejournal_title
Natureauthors
Loose C,Jensen K,Rigoutsos I,Stephanopoulos Gdoi
10.1038/nature05233subject
Has Abstractpub_date
2006-10-19 00:00:00pages
867-9issue
7113eissn
0028-0836issn
1476-4687pii
nature05233journal_volume
443pub_type
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