Search results for "Peptoid"
showing 10 items of 12 documents
PeptoSomes for Vaccination: Combining Antigen and Adjuvant in Polypept(o)ide-Based Polymersomes.
2017
In this work, the first vaccine is reported based on a PeptoSome, which contains a model antigen (SIINFEKL) and adjuvant (CpG). PeptoSomes are polypept(o)ide-based polymersomes built of a block-copolymer with polysarcosine (PSar) as the hydrophilic block (X n = 111) and poly(benzyl-glutamic acid) (PGlu(OBn)) as the hydrophobic one (X n = 46). The polypept(o)ide is obtained with low dispersity index of 1.32 by controlled ring-opening polymerization. Vesicle formation by dual centrifugation technique allows for loading of vesicles up to 40 mol%. PeptoSomes are characterized by multiangle dynamic light scattering, static light scattering, and cryogenic transmission electron microscopy (cryoTEM…
Identification from a Positional Scanning Peptoid Library of in Vivo Active Compounds That Neutralize Bacterial Endotoxins
2005
4 pages, 3 figures, 1 table.-- PMID: 15715495 [PubMed].-- Printed version published Feb 24, 2005.-- Supporting information available at: http://pubs.acs.org/doi/suppl/10.1021/jm040834i
Solvent effects on the conformational preferences of model peptoids. MP2 study.
2014
The influence of aqueous environment on the main-chain conformation (ω0, ϕ, and ψ dihedral angles) of two model peptoids: N-acetyl-N-methylglycine N’-methylamide (Ac-N(Me)-Gly-NHMe) (1) and N-acetyl-N-methylglycine N’,N’-dimethylamide (Ac-N(Me)-Gly-NMe2) (2) was investigated by MP2/6-311++G(d,p) method. The Ramachandran maps of both studied molecules with cis and trans configuration of the N-terminal amide bond in the gas phase and in water environment were obtained and all energy minima localized. The polarizable continuum model was applied to estimate the solvation effect on conformation. Energy minima of the Ac-N(Me)-Gly-NHMe and Ac-N(Me)-Gly-NMe2 have been analyzed in terms of the possi…
Soft X-ray tomography of phenotypic switching and the cellular response to antifungal peptoids in Candida albicans.
2009
The opportunistic pathogen Candida albicans can undergo phenotypic switching between a benign, unicellular phenotype and an invasive, multicellular form that causes candidiasis. Increasingly, strains of Candida are becoming resistant to antifungal drugs, making the treatment of candidiasis difficult, especially in immunocompromised or critically ill patients. Consequently, there is a pressing need to develop new drugs that circumvent fungal drug-resistance mechanisms. In this work we used soft X-ray tomography to image the subcellular changes that occur as a consequence of both phenotypic switching and of treating C. albicans with antifungal peptoids, a class of candidate therapeutics unaf…
Small molecule inhibitors of Apaf-1-related caspase- 3/-9 activation that control mitochondrial-dependent apoptosis
2006
10 pages, 5 figures.-- PMID: 16341125 [PubMed].-- Available online Dec 9, 2005.
A positional scanning combinatorial library of peptoids as a source of biological active molecules: identification of antimicrobials
2003
9 pages, 4 figures, 2 schemes, 3 tables.-- PMID: 12959560 [PubMed].-- Printed version published in issue Sep-Oct 2003.-- Supporting information available at: http://pubs.acs.org/doi/suppl/10.1021/cc020075u
Peptidomimetics – An infinite reservoir of metal binding motifs in metabolically stable and biologically active molecules
2020
The involvement of metal ions in interactions with therapeutic peptides is inevitable. They are one of the factors able to fine-tune the biological properties of antimicrobial peptides, a promising group of drugs with one large drawback - a problematic metabolic stability. Appropriately chosen, proteolytically stable peptidomimetics seem to be a reasonable solution of the problem, and the use of D-, β-, γ-amino acids, unnatural amino acids, azapeptides, peptoids, cyclopeptides and dehydropeptides is an infinite reservoir of metal binding motifs in metabolically stable, well-designed, biologically active molecules. Below, their specific structural features, metal-chelating abilities and anti…
Polypeptoid-block-polypeptide Copolymers: Synthesis, Characterization, and Application of Amphiphilic Block Copolypept(o)ides in Drug Formulations an…
2013
We report the synthesis of polysarcosine-block-polyglutamic acid benzylester (PSar-block-PGlu(OBn)) and polysarcosine-block-polylysine-ε-N-benzyloxycarbonyl (PSar-block-PLys(Z)) copolymers. The novel polypeptoid-block-polypeptide copolymers (Copolypept(o)ides) have been synthesized by ring-opening polymerization (ROP) of N-carboxyanhydrides (NCAs). Polymerization conditions were optimized regarding protecting groups, block sequence and length. While the degree of polymerization of the PSar block length was set to be around 200 or 400, PGlu(OBn) and PLys(Z) block lengths were varied between 20 to 75. The obtained block copolymers had a total degree of polymerization of 220-475 and dispersity…
Polypept(o)ides: Hybrid Systems Based on Polypeptides and Polypeptoids.
2015
Polypept(o)ides combine the multifunctionality and intrinsic stimuli-responsiveness of synthetic polypeptides with the "stealth"-like properties of the polypeptoid polysarcosine (poly(N-methyl glycine)). This class of block copolymers can be synthesized by sequential ring opening polymerization of α-amino acid N-carboxy-anhydrides (NCAs) and correspondingly of the N-substituted glycine N-carboxyanhydride (NNCA). The resulting block copolymers are characterized by Poisson-like molecular weight distributions, full end group integrity, and dispersities below 1.2. While polysarcosine may be able to tackle the currently arising issues regarding the gold standard PEG, including storage diseases i…
Poly-sarcosine and poly(ethylene-glycol) interactions with proteins investigated using molecular dynamics simulations
2018
Nanoparticles coated with hydrophilic polymers often show a reduction in unspecific interactions with the biological environment, which improves their biocompatibility. The molecular determinants of this reduction are not very well understood yet, and their knowledge may help improving nanoparticle design. Here we address, using molecular dynamics simulations, the interactions of human serum albumin, the most abundant serum protein, with two promising hydrophilic polymers used for the coating of therapeutic nanoparticles, poly(ethylene-glycol) and poly-sarcosine. By simulating the protein immersed in a polymer-water mixture, we show that the two polymers have a very similar affinity for the…