11 documents found, page 1 of 2
Coupling the antimalarial cell penetrating peptide TP10 to classical antimalari...
Aguiar, L; Biosca, A; Lantero, E; Gut, J; Vale, N; Rosenthal, PJ; Nogueira, F; Andreu, D; Fernàndez-Busquets, X; Gomes, PRecently, we disclosed primaquine cell penetrating peptide conjugates that were more potent than parent primaquine against liver stage Plasmodium parasites and non-toxic to hepatocytes. The same strategy was now applied to the blood-stage antimalarial chloroquine, using a wide set of peptides, including TP10, a cell penetrating peptide with intrinsic antiplasmodial activity. Chloroquine-TP10 conjugates displayi...
Interaction and lipid-induced conformation of two cecropin-melittin hybrid pept...
Abrunhosa, F; Faria, S; Gomes, P; Tomaz, I; Pessoa, JC; Andreu, D; Bastos, MThe interaction of two hybrid peptides of cecropin A and melittin [CA(1-8)M(1-18) and CA(1-7)M(2-9)] with liposomes was studied by differential scanning calorimetry (DSC), circular dichroism (CD), and quasi-elastic light scattering (QELS). The study was carried out with large unilamellar vesicles (LUVs) of three different lipid compositions: 1,2-dimyristoil-sn-glycero-3-phosphocholine (DMPG), 1,2-dimyristoylsn-...
Direct kinetic assay of interactions between small peptides and immobilized ant...
Gomes, P; Andreu, DA surface plasmon resonance (SPR) protocol is described for the direct kinetic analysis of small antigenic peptides interacting with immobilized monoclonal antibodies (mAb). High peptide concentrations (up to 2.5 muM) and medium mAb surface densities (about 1.5 ng/mm(2)) are needed to ensure measurable binding levels, and fast buffer flow rates (60 mul/min) are required to minimize diffusion-controlled kinetics...
Binding of small peptides to immobilized antibodies: kinetic analysis by surfac...
Andreu, D; Gomes, PThis unit describes a method for screening small viral peptides as specific antigens using a surface plasmon resonance (SPR) biosensor. The basic protocol in this unit is suited for direct single-step SPR analysis of small ligand-large receptor interactions, where small peptides are used as analytes (injected in the continuous buffer flow) and monoclonal antibodies (MAbs) are immobilized on the SPR sensor chip ...
Probing degeneracy in antigen-antibody recognition at the immunodominant site o...
Gomes, P; Giralt, E; Ochoa, W; Verdaguer, N; Andreu, DAntigen-antibody binding is regarded as one of the most representative examples of specific molecular recognition in nature. The simplistic view of antigenic recognition in terms of a lock-and-key mechanism is obsolete, as it is evident that both antigens and antibodies are flexible and can undergo substantial mutual adaptation. This flexibility is the source of complexities such as degeneracy and nonadditivity...
Antigenicity modulation upon peptide cyclization: application to the GH loop of...
Gomes, P; Giralt, E; Andreu, DFoot-and-mouth disease virus (FMDV) isolate C-1-Barcelona (or C-S30) includes four replacements within its immunodominant site (GH loop, residues 136-150 of capsid protein VP1, YTTSTRGDLAHVTAT), relative to reference strain C-S8cl (YTASAR-GDLAHLTTT). Although one of the mutations in C-S30 ((147)Leu --> Val) is known to be detrimental for antibody recognition, reactivity of this isolate with the neutralizing mon...
Identification of T-cell epitopes in nonstructural proteins of foot-and-mouth d...
Blanco, E; Garcia Briones, M; Sanz Parra, A; Gomes, P; De Oliveira, E; Valero, ML; Andreu, D; Ley, V; Sobrino, FPorcine T-cell recognition of foot-and-mouth disease virus (FMDV) nonstructural proteins (NSP) was tested using in vitro lymphoproliferative responses, Lymphocytes were obtained from outbred pigs experimentally infected with FMDV, Of the different NSP, polypeptides 3A, 3B, and 3C gave the highest stimulations in the in vitro assays. The use of overlapping synthetic peptides allowed the identification of amino a...
Direct single-step surface plasmon resonance analysis of interactions between s...
Gomes, P; Giralt, E; Andreu, DSurface plasmon resonance (SPR) methods have been optimized to permit direct kinetic analysis of the antigenic peptide analytes interacting with immobilized monoclonal antibodies (mAbs). High reproducibility and a significant correlation between SPR and previous ELISA data on the same set of antibodies and peptides were observed. The kinetic data obtained provide further insight into the structure of the main a...
Molecular analysis of peptides from the GH loop of foot-and-mouth disease virus...
Gomes, P; Giralt, E; Andreu, DA foot-and-mouth disease virus (FMDV) field variant, isolate C-S30 (also named C-1-Barcelona), is known to contain four changes within the main antigenic site A (GH loop of capsid protein VP1, residues 136-150), at least one of which (Leu147 --> Val) involves a highly conserved position, critical for antibody recognition in the reference strain C-S8c1. However, immunoenzymatic analysis of FMDV C-S30 showed it w...
A multiply substituted G-H loop from foot-and-mouth disease virus in complex wi...
Ochoa, WF; Kalko, SG; Mateu, MG; Gomes, P; Andreu, D; Domingo, E; Fita, I; Verdaguer, NThe crystal structure of a 15 amino acid synthetic peptide, corresponding to the sequence of the major antigenic site A (G-H loop of VP1) from a multiple variant of foot-and-mouth disease virus (FMDV), has been determined at 2·3 resolution. The variant peptide includes four amino acid substitutions in the loop relative to the previously studied peptide representing FMDV C-S8c1 and corresponds to the loop of a n...