Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Increasing hydrophobicity of residues in an anti-HIV-1 Env peptide synergistically improves potency.

Biophysical journal - 20 Apr 2011

Leung Michael Y K, Cohen Fredric S

Abstract excerpt

T-20/Fuzeon/Enfuvirtide (ENF), a peptide inhibitor of HIV-1 infection, targets the grooves created by heptad repeat 2 (HR2) of Env's coiled-coil, but mutants resistant to ENF emerge. In this study, ENF-resistant mutants--V38A, N43D, N43D/S138A, Q40H/L45M--were combined with modified inhibitory peptides to identify what we believe to be novel ways to improve peptide efficacy. V38A did not substantially reduce...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Drug Synergism
Share to Enfuvirtide
Share to Entropy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to env Gene Products, Human Immunodeficiency Virus

Share to HIV Envelope Protein gp41

Share to Hydrophobic and Hydrophilic Interactions

Share to Protein Stability

Share to Repetitive Sequences, Amino Acid

Source

Open in PubMed Open full text

Identifiers

PMID: 21504732
DOI: 10.1016/j.bpj.2011.02.053
PMCID: PMC3077694

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Increasing hydrophobicity of residues in an anti-HIV-1 Env peptide synergistically improves potency.PMID 21504732Read ↗

Impact of the enfuvirtide resistance mutation N43D and the associated baseline polymorphism E137K on peptide sensitivity and six-helix bundle structure.Semantic proximity Read ↗

Design of Peptide-based Inhibitors for Human Immunodeficiency Virus Type 1 Strains Resistant to T-20Semantic proximity Read ↗

Detailed mechanistic insights into HIV-1 sensitivity to three generations of fusion inhibitors.Semantic proximity Read ↗

Resistance profiles of novel electrostatically constrained HIV-1 fusion inhibitors.Semantic proximity Read ↗

Adding an Artificial Tail-Anchor to a Peptide-Based HIV-1 Fusion Inhibitor for Improvement of Its Potency and Resistance Profile.Semantic proximity Read ↗

Heptad-repeat-2 mutations enhance the stability of the enfuvirtide-resistant HIV-1 gp41 hairpin structure.Semantic proximity Read ↗

Research strategies of the N-peptide fusion inhibitor: a promising direction for discovering novel antiviralsSemantic proximity Read ↗

Mechanism of resistance to S138A substituted enfuvirtide and its application to peptide design.Semantic proximity Read ↗

SC29EK, a Peptide Fusion Inhibitor with Enhanced α-Helicity, Inhibits Replication of Human Immunodeficiency Virus Type 1 Mutants Resistant to EnfuvirtideSemantic proximity Read ↗

Design of a Novel HIV-1 Fusion Inhibitor That Displays a Minimal Interface for Binding AffinitySemantic proximity Read ↗

Biophysical property and broad anti-HIV activity of albuvirtide, a 3-maleimimidopropionic acid-modified peptide fusion inhibitor.Semantic proximity Read ↗

Design of a highly potent HIV-1 fusion inhibitor targeting the gp41 pocket.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.