Results 161 to 170 of about 3,583 (208)

The mycotoxin definition reconsidered towards fungal cyclic depsipeptides

open access: yesJournal of Environmental Science and Health, Part C: Environmental Carcinogenesis and Ecotoxicology Reviews, 2016
Currently, next to the major classes, cyclic depsipeptides beauvericin and enniatins are also positioned as mycotoxins. However, as there are hundreds more fungal cyclic depsipeptides already identified, should these not be considered as mycotoxins as ...
Lien Taevernier   +2 more
exaly   +2 more sources

The cyclization of peptides and depsipeptides

Journal of Peptide Science, 2003
AbstractConstricting the peptide backbone into a more defined conformational form through cyclization is an activity evolved in nature and in synthetic work, the latter straddling only the most recent decades. The resulting conformational constraints increase the probability of an optimum response with bio‐receptors.
John S Davies
exaly   +3 more sources

Depsipeptide Synthesis

ChemInform, 2007
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
Maciej, Stawikowski, Predrag, Cudic
openaire   +2 more sources

Depsipeptide Dendrimers

Chemistry - A European Journal, 2000
The convergent synthesis of a new class of chiral dendrimers is described. Owing to their structural resemblance to depsipeptides they are called depsipeptide dendrimers. The ex-chiral pool synthesis starts from (R,R)-, (S,S)-, and meso-tartaric acid as branching units and dipeptides or tripeptides consisting of glycine, (L)-alanine, and (L)-leucine as
J, Kress, A, Rosner, A, Hirsch
openaire   +2 more sources

Marine Depsipeptides as Promising Pharmacotherapeutic Agents

Current Protein and Peptide Science, 2016
Depsipeptides are a group of biologically active peptides that have at least one of the amide bonds replaced by an ester bond. These peptides sometimes present additional chemical modifications, including unusual amino acid residues in their structures.
Marisa Rangel   +2 more
exaly   +3 more sources

Antimitotic Peptides and Depsipeptides

Current Medicinal Chemistry-Anti-Cancer Agents, 2012
Tubulin is the target for an ever increasing number of unusual peptides and depsipeptides that were originally isolated from a wide variety of organisms. Since tubulin is the major component of cellular microtubules, which maintain cell shape in interphase and form the mitotic spindle, most of these compounds are highly toxic to mammalian cells.
Ernest, Hamel, David G, Covell
openaire   +2 more sources

An Expeditious Asymmetric Synthesis of the Polyketide Unit Present in HIV-Inhibitory Depsipeptides Aetheramide A and B

open access: yesSynlett, 2014
The enantioselective synthesis of the polyketide unit present in depsipeptides aetheramide A and B, which possess potent HIV-inhibitory activity, is accomplished from a chiral furyl ...
Kavirayani R Prasad, Omkar Revu
exaly   +2 more sources

Siamese Depsipeptides: Constrained Bicyclic Architectures

Angewandte Chemie - International Edition, 2009
has been designed. Cyclic depsipeptide dimers connected by a CC bond were constructed. Two kind of possible connections can be envisaged, those that share a side chain bond or those that share a backbone bond. Owing to the resulting proximity of both structurally identical cycles, they can be called Siamese depsipeptides. For Siamese depsipeptides, the
Jan Spengler, Fernando Alberício
exaly   +3 more sources

Recent Developments in Depsipeptide Research

Current Medicinal Chemistry, 2002
This review focuses on the major developments in depsipeptide research since 1995. Depsipeptides are bio-oligomers composed of hydroxy and amino acids linked by amide and ester bonds. Many depsipeptides show very promising biological activities, including anticancer, antibacterial, antiviral, antifungal, anti-inflammatory, and anti-clotting or anti ...
C E, Ballard, H, Yu, B, Wang
openaire   +2 more sources

Progress in Depsipeptide‐Based Biomaterials

Macromolecular Bioscience, 2010
AbstractPolydepsipeptides – alternating copolymers of an α‐amino acid and an α‐hydroxy acid – are a group of biodegradable polymers. Versatile polydepsipeptides with or without pendant functional groups, as well as various polymer architectures, for example, providing alternative, random, diblock, triblock, multiblock or graft sequence structures, can ...
Yakai, Feng   +3 more
openaire   +2 more sources

Home - About - Disclaimer - Privacy