Journal: PLoS ONE

Article Title: Rationally Designed Interfacial Peptides Are Efficient In Vitro Inhibitors of HIV-1 Capsid Assembly with Antiviral Activity

doi: 10.1371/journal.pone.0023877

Figure Lengend Snippet: (A) Ribbon model of the three dimensional structure of the CTD dimer . The two monomers are represented in green or blue. Helix 9 is labelled. (B) Sequence of CAC1 including helix 9 residues, and of designed CAC1-derived peptides. (C) Variation in <λ> of the fluorescence emission spectrum of wild-type dimeric CTD with the concentration of added CAC1C. Fitting to a 1∶1 binding isotherm as described is indicated by a thin line. A similar affinity constant was obtained when the fluorescence intensity at 315 nm instead of <λ> was represented. (D) Variation in fluorescence emission intensity at 315 nm of wild-type dimeric CTD with the concentration of added CAC1M.

Article Snippet: CAC1 (E 175 QASQEVKNWMTETLLVQNA 194 ) , CAC1-derived peptides CAC1C (E 175 SASSSVKAWMTETLLVQNA 194 ),CAC1M(SE 175 SAASSVKAWMTETLLVAN 193 TSS) and a control, non CTD-binding, thioredoxin binding peptide (ESLPDYGDDSDDNTLGTEEQRSIVNVSQ) derived from pea chloroplast fructose-1,6-biphosphatase (Fbase), were synthesized and purified by Genscript, NJ, USA.

Techniques: Sequencing, Derivative Assay, Fluorescence, Concentration Assay, Binding Assay

Journal: PLoS ONE

Article Title: Rationally Designed Interfacial Peptides Are Efficient In Vitro Inhibitors of HIV-1 Capsid Assembly with Antiviral Activity

doi: 10.1371/journal.pone.0023877

Figure Lengend Snippet: Parameters for self-association and CTD binding of CAC1-derived peptides a .

Article Snippet: CAC1 (E 175 QASQEVKNWMTETLLVQNA 194 ) , CAC1-derived peptides CAC1C (E 175 SASSSVKAWMTETLLVQNA 194 ),CAC1M(SE 175 SAASSVKAWMTETLLVAN 193 TSS) and a control, non CTD-binding, thioredoxin binding peptide (ESLPDYGDDSDDNTLGTEEQRSIVNVSQ) derived from pea chloroplast fructose-1,6-biphosphatase (Fbase), were synthesized and purified by Genscript, NJ, USA.

Techniques: Binding Assay

Journal: PLoS ONE

Article Title: Rationally Designed Interfacial Peptides Are Efficient In Vitro Inhibitors of HIV-1 Capsid Assembly with Antiviral Activity

doi: 10.1371/journal.pone.0023877

Figure Lengend Snippet: (A) Mapping on the CTD sequence of the residues affected by peptide binding. Red, green or blue circles denote residues affected by binding of CAC1, CAC1C or CAC1M, respectively. (B, C) Surface model of one of the monomeric subunits in the CTD dimer. In (B) the residues involved in the CTD dimerization interface are coloured magenta. The ribbon tracing of the helix 9 main chain is superimposed. In (C) the residues affected by binding of the peptides are colored as follows: bright red, residues affected by binding of any peptide; dark red, orange or brown, residues affected by binding of CAC1 and CAC1C, CAC1 and CAC1M, or CAC1C and CAC1M, respectively.

Article Snippet: CAC1 (E 175 QASQEVKNWMTETLLVQNA 194 ) , CAC1-derived peptides CAC1C (E 175 SASSSVKAWMTETLLVQNA 194 ),CAC1M(SE 175 SAASSVKAWMTETLLVAN 193 TSS) and a control, non CTD-binding, thioredoxin binding peptide (ESLPDYGDDSDDNTLGTEEQRSIVNVSQ) derived from pea chloroplast fructose-1,6-biphosphatase (Fbase), were synthesized and purified by Genscript, NJ, USA.

Techniques: Sequencing, Binding Assay