Hydrocarbon double-stapling remedies the proteolytic instability of a lengthy peptide therapeutic

Proceedings of the National Academy of Sciences of the United States of America

Volumn 107, Issue 32, 2010, Pages 14093-14098

  Bird, Gregory H ^a,b   Madani, Navid ^c   Perry, Alisa F ^a,b   Princiotto, Amy M ^c   Supko, Jeffrey G ^d   He, Xiaoying ^d   Gavathiotis, Evripidis ^a,b   Sodroski, Joseph G ^c,e   Walensky, Loren D ^a,b  

^a BOSTON CHILDREN S HOSPITAL   (United States)

^b DANA FARBER CANCER INSTITUTE   (United States)

^c HARVARD MEDICAL SCHOOL   (United States)

^d MASSACHUSETTS GENERAL HOSPITAL   (United States)

^e HARVARD SCHOOL OF PUBLIC HEALTH   (United States)

Author keywords

Alpha helix; Fusion inhibitor; HIV 1; Protease resistance; Stapled peptide

Indexed keywords

ACID PROTEINASE; ENFUVIRTIDE; EXENDIN 4; HYDROCARBON; ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; HUMAN IMMUNODEFICIENCY VIRUS FUSION INHIBITOR; PEPTIDE;

ALPHA HELIX; ANTIVIRAL ACTIVITY; ARTICLE; DRUG ABSORPTION; DRUG TARGETING; FUSION GENE; HUMAN IMMUNODEFICIENCY VIRUS 1; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN STRUCTURE; BIOAVAILABILITY; CHEMISTRY; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS INFECTION; STRUCTURE ACTIVITY RELATION;

ANTI-HIV AGENTS; BIOLOGICAL AVAILABILITY; HIV FUSION INHIBITORS; HIV INFECTIONS; HUMANS; HYDROCARBONS; PEPTIDES; STRUCTURE-ACTIVITY RELATIONSHIP;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 77956294635     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1002713107     Document Type: Article

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