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Mirabamides A-D, depsipeptides from the sponge Siliquariaspongia mirabilis that inhibit HIV-1 fusion.
TLDR
Four new cyclic depsipeptides termed mirabamides A-D (1-4) have been isolated from the marine sponge Siliquariaspongia mirabilis and shown to potently inhibit HIV-1 fusion and demonstrate that these peptides can act at the early stages of HIV- 1 entry. Expand
Increased fitness of drug resistant HIV-1 protease as a result of acquisition of compensatory mutations during suboptimal therapy.
TLDR
The evolution and fitness of viral populations appearing in a patient who received protease monotherapy indicates that the viral population in the patient does not have to represent the fittest possible variants, and thus antiretroviral therapy may drive the viral populations first through a lower fitness level and then to a higher fitness level. Expand
Solution Structure of the Monovalent Lectin Microvirin in Complex with Manα(1–2)Man Provides a Basis for Anti-HIV Activity with Low Toxicity*
TLDR
It is suggested that gp120 behaves as a clustered glycan epitope and that multivalent-protein interactions achievable with CVN but not MVN are required for inhibition of some viruses. Expand
Differential inhibition of HIV-1 and SIV envelope-mediated cell fusion by C34 peptides derived from the C-terminal heptad repeat of gp41 from diverse strains of HIV-1, HIV-2, and SIV.
TLDR
Of particular interest is the finding that the C34 peptide derived from the EHO strain of HIV-2 is a broad spectrum, highly potent inhibitor of Env-mediated cell fusion with IC(50) values spanning a very narrow range from only 4 to 25 nM over the entire panel of HIV -1 and SIV envelope glycoproteins tested. Expand
Peptides from Second Extracellular Loop of C-C Chemokine Receptor Type 5 (CCR5) Inhibit Diverse Strains of HIV-1*
TLDR
The data provide new insights into HIV-1 gp120-CCR5 interactions that can be used for inhibitor design and suggest that gp120 has separate binding sites for the CCR5 N terminus and ECL2, the ECL1 binding site is present prior to CD4 engagement, and it is conserved across C CR5- and CXCR4-using strains. Expand
Drug resistance mutations can affect dimer stability of HIV‐1 protease at neutral pH
TLDR
The results indicate that reductions in drug affinity may be due to the combined effects of mutations on both dimer stability and inhibitor binding, and differs significantly from a previously reported value of 23 nM obtained indirectly from inhibitor binding measurements. Expand
Sequestering of the Prehairpin Intermediate of gp41 by Peptide N36Mut(e,g) Potentiates the Human Immunodeficiency Virus Type 1 Neutralizing Activity of Monoclonal Antibodies Directed against the
TLDR
It is shown that N36Mut(e,g) prolongs the temporal window during which the virus is susceptible to neutralization by the bivalent Fab 3674 and that bivalentFab 3674-N36Mut and N36mut neutralize HXB2 and SF162 strains of HIV-1, as well as isolates of diverse primary B and C HIV- 1 strains, synergistically in a Env-pseudotyped virus neutralization assay. Expand
Dissection of the pH dependence of inhibitor binding energetics for an aspartic protease: direct measurement of the protonation states of the catalytic aspartic acid residues.
TLDR
Comparison of the thermodynamic and structural data for pepstatin binding with human cathepsin D, a lysosomal aspartic protease that shares 35% sequence identity with plasmepsin II, suggests that the energetic differences between these two proteins are due to a higher interdomain flexibility in plasmepin II. Expand
Structural Basis of HIV-1 Neutralization by Affinity Matured Fabs Directed against the Internal Trimeric Coiled-Coil of gp41
TLDR
Crystal structures of the N-HR mimetic 5-Helix with two Fabs suggest that both neutralization properties and affinity for the target can be attributed, at least in part, to the differences in the interactions of the CDR-H2 loops with the antigen. Expand
Post X‐ray crystallographic studies of chymosin: the existence of two structural forms and the regulation of activity by the interaction with the histidine‐proline cluster of κ‐casein
TLDR
The preliminary incubation of the enzyme with a pentapeptide corresponding to the histidine‐proline cluster of the specific substrate κ‐casein results in a 200‐fold increase of the hydrolysis rate for the enzyme ‘slow substrate’, suggesting that the cluster is an allosteric effector that promotes the conversion of the enzymes into the active form. Expand
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