A peptide conjugate of vitamin E succinate targets breast cancer cells with high ErbB2 expression.

Overexpression of erbB2 is associated with resistance to apoptosis. We explored whether high level of erbB2 expression by cancer cells allows their targeting using an erbB2-binding peptide (LTVSPWY) attached to the proapoptotic alpha-tocopheryl succinate (alpha-TOS). Treating erbB2-low or erbB2-high cells with alpha-TOS induced similar levels of apoptosis, whereas alpha-TOS-LTVSPWY induced greater levels of apoptosis in erbB2-high cells.

Comblike dendrimers containing Tn antigen modulate natural killing and induce the production of Tn specific antibodies.

Comblike glycodendrimers were prepared by the chemoselective ligation of cysteine-modified glycopeptides (1-7) with a 3-maleimidopropionate-modified linear synthetic carrier (8). Glycodendrimers bearing mono-, di-, or tri-Tn clusters (9-11) were tested as inhibitors using plant and mammalian lectins. In the former group, the Codium fragile lectin showed moderate discrimination among 9, 10, and 11.

Molecular Dynamics Study of the Effect of the γ-Abu Insert on the Conformational Behavior of the Glycopeptide Dendrimers Based on the Oligolysine Scaffold in N, N'-dimethylformamide.

Abstract Glycodendrimers bearing Tn (α-D-GalNAc-(1→O)-Ser/Thr), an identified tumor-associated carbohydrate antigen, hold promise in the post-surgery treatment of a variety of tumors such as metastatic breast cancer. We used molecular dynamics (MD) techniques to examine structural differences taking place during synthesis of two classes of tetravalent Multiple Antigen Glycopeptides (MAG) that differ only by the y-Abu insert in the structure of the oligolysine core. Each of the selected intermediates of the synthesis was modeled, subjected to the 2 ns run in N,N'-dimethylformamide (DMF) and geometrically characterized.

Molecular dynamics study of the effect of the gamma-Abu insert on the conformational behavior of the glycopeptide dendrimers based on the oligolysine scaffold in N, N'-dimethylformamide.

Glycodendrimers bearing Tn (alpha-D-GalNAc-(1 --> O)-Ser/Thr), an identified tumor-associated carbohydrate antigen, hold promise in the post-surgery treatment of a variety of tumors such as metastatic breast cancer. We used molecular dynamics (MD) techniques to examine structural differences taking place during synthesis of two classes of tetravalent Multiple Antigen Glycopeptides (MAG) that differ only by the gamma-Abu insert in the structure of the oligolysine core. Each of the selected intermediates of the synthesis was modeled, subjected to the 2 ns run in N,N'-dimethylformamide (DMF) and geometrically characterized.

Peptides and multiple antigen peptides from Schistosoma mansoni glyceraldehyde 3-phosphate dehydrogenase: preparation, immunogenicity and immunoprotective capacity in C57BL/6 mice.

Four monoepitopic MAPs (MAP A, B, C and E) and one bis-diepitopic MAP B-E derived fromthe primary sequence of Schistosoma mansoni glyceraldehyde 3-phosphate dehydrogenase, previously tested in BALB/c mice, were examined for their immunogenicity and protective capacity in C57BL/6 mice. Despite multimerization into MAPs, MAP Aand MAP C were poorly immunogenic. In contrast toBALB/c mice, MAP E was non-immunogenic in C57BL/6 mice.

Differences in immunogenicity and vaccine potential of peptides from Schistosoma mansoni glyceraldehyde 3-phosphate dehydrogenase.

Six peptides, A, B1, B, C, D and E derived from the primary sequence of Schistosoma mansoni glyceraldehyde 3-phosphate dehydrogenase (SG3PDH) were selected based on lowest homology to human G3PDH and used for immunization of BALB/c mice. Peptides B1 and D induced immunoglobulin (Ig) G1, IgG2a and IgG2b antibodies that reacted with native and denatured SG3PDH, and were associated with significant (P<0.05) increase in fecundity and burden of challenge worms, respectively.

Tailoring an antibacterial peptide of human lysosomal cathepsin G to enhance its broad-spectrum action against antibiotic-resistant bacterial pathogens.

Neutrophils contain several cationic antimicrobial proteins or peptides (CAPs) that exert antibiotic-like action against bacteria. These host-derived antibiotics kill susceptible bacteria by oxygen-independent mechanisms. Considerable interest in their activity has been generated in recent years due not only to their likely important role in innate host defense against infection, but also their possible use as therapeutic agents in treating infections caused by antibiotic-resistant pathogens.

Peptide and glycopeptide dendrimers. Part II.

Recent progress in peptide and glycopeptide chemistry make the preparation of peptide and glycopeptide dendrimers of acceptable purity, with designed structural and immunochemical properties reliable. New methodologies using unprotected peptide building blocks have been developed to further increase the possibilities of their design and improve their preparation and separation. The sophisticated design of peptide and glycopeptide dendrimers has led to their use as antigens and immunogens, for serodiagnosis and other biochemical uses including drug delivery.

Isoproterenol induced rat endomyocardial damage in relationship to local capillary geometry.

Isoproterenol (2 mg/kg) injected subcutaneously into male Sprague-Dawley rats elicited morphological damage in the endomyocardium which was analyzed 16 h following injection. Our aim was to study the relationship between damaged individual myocytes and their capillary supply. Myocardial tissue sections were differentially stained in order to distinguish arteriolar (AC) and venular (VC) capillary portions.