Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic
Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic
About this item
Full title
Author / Creator
Publisher
United States: National Academy of Sciences
Journal title
Language
English
Formats
Publication information
Publisher
United States: National Academy of Sciences
Subjects
More information
Scope and Contents
Contents
The pharmacologic utility of lengthy peptides can be hindered by loss of bioactive structure and rapid proteolysis, which limits bioavailability. For example, enfuvirtide (Fuzeon, T20, DP178), a 36-amino acid peptide that inhibits human immunodeficiency virus type 1 (HIV-1) infection by effectively targeting the viral fusion apparatus, has been rel...
Alternative Titles
Full title
Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_jstor_primary_25708861
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_jstor_primary_25708861
Other Identifiers
ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.1002713107
