23632-78-2Relevant academic research and scientific papers
Visible Light-Mediated Synthesis of Se?S Bond-Containing Peptides
Arsenyan, Pavel,Dimitrijevs, Pavels,Lapcinska, Sindija
supporting information, p. 3968 - 3972 (2021/07/26)
A visible light-initiated method has been developed for preparation of Se?S bond-containing peptides. The method is based on generation of sulfur-centered radical employing organic dye. The protocol is tolerant to unprotected peptides with “sensitive” amino acids. The stability of Se?S bond is evaluated in buffers at different pH (3.0–10.0) and also in the presence of oxidants and reducing agents. Additionally, the ability of Se?S bond to serve as an oxidation sensitive linker in biocompatible materials has been confirmed. (Figure presented.).
Synthesis and Structure-Activity Relationships of Ring-Opened Bengamide Analogues against Methicillin-Resistant Staphylococcus aureus?
Yu, Chen-Xi,Wei, Bing-Yan,Kong, Xue-Qing,Yang, Cai-Guang,Nan, Fa-Jun
, p. 671 - 676 (2021/02/12)
Methicillin-resistant Staphylococcus aureus (MRSA) has become a major threat on public health because of the increase of clinically isolated strains that exhibit resistance to many antibiotics. Therefore, development of new antibiotics for the treatment of MRSA infection is a sustained challenge. We have previously identified a ring-opened bengamide analogue L472-2 that displays moderate activity against the growth of S. aureus. In our previous work, we started from L472-2 and identified a class of analogues containing alkynyl groups which have the potential to activate SaClpP activity but moderate antibacterial activity. Herein, we focused on the antibacterial activity of L472-2, and a novel series of ring-opened bengamide analogues were synthesized and their activities were evaluated against MRSA. By conducting a compact analysis of the structure-activity relationships (SAR) of these analogues, we found that an adamantane ethanol ester bengamide 2j showed excellent antibacterial activity towards six S. aureus strains, including MRSA, while it does not activate ClpP. Therefore, these bengamide analogues represent a new class of candidates that suppress MRSA viability.
Glycopeptide derivatives for the preservation and protection of biological materials and microorganisms
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Page/Page column 58-60, (2018/11/06)
The present invention relates to a compound of the following formula (I): in which at least one and only one group chosen among R5, R6 and R7 is a group of the following formula: The present invention relates also to uses
One-pot mechanosynthesis of aromatic amides and dipeptides from carboxylic acids and amines
?trukil, Vjekoslav,Bartolec, Boris,Portada, Tomislav,Dilovi?, Ivica,Halasz, Ivan,Margeti?, Davor
supporting information, p. 12100 - 12102 (2013/01/16)
Environmentally friendly one-pot synthesis of amides, bis-amides and dipeptides by mechanochemical carbodiimide-mediated coupling of carboxylic acids and amines is described; high reaction yields and simple aqueous work-up allow for the clean, practical and fast preparation of a variety of compounds containing the amide bond from readily accessible reagents.
Development of supramolecular organo-gel based on tripeptide skeletons
Azuma, Eriko,Kuramochi, Kouji,Tsubaki, Kazunori
body text, p. 680 - 684 (2010/07/15)
Boc-Ser-Val-Gly-OCH2Ph (31) showed high gelation abilities in the aromatic solvents, particularly in toluene. The minimum gelation concentration of 31 in toluene was 10 mg/ml, suggesting that 2500 molecules of toluene were immobilized by each m
Self-assembly of β-turn forming synthetic tripeptides into supramolecular β-sheets and amyloid-like fibrils in the solid state
Maji, Samir Kumar,Haldar, Debasish,Drew, Michael G. B.,Banerjee, Arijit,Das, Apurba Kumar,Banerjee, Arindam
, p. 3251 - 3259 (2007/10/03)
We have described here the self-assembling properties of the synthetic tripeptides Boc-Ala(1)-Aib(2)-Val(3)-OMe 1, Boc-Ala(1)-Aib(2)-Ile(3)-OMe 2 and Boc-Ala(1)-Gly(2)-Val(3)-OMe 3 (Aib=α-amino isobutyric acid, β-Ala=β-alanine) which have distorted β-turn conformations in their respective crystals. These turn-forming tripeptides self-assemble to form supramolecular β-sheet structures through intermolecular hydrogen bonding and other noncovalent interactions. The scanning electron micrographs of these peptides revealed that these compounds form amyloid-like fibrils, the causative factor for many neurodegenerative diseases including Alzheimer's disease, Huntington's disease and Prion-related encephalopathies.
Synthesis of a novel esterase-sensitive cyclic prodrug of a hexapeptide using an (acyloxy)alkoxy promoiety
Gangwar, Sanjeev,Pauletti, Giovanni M.,Siahaan, Teruna J.,Stella, Valentino J.,Borchardt, Ronald T.
, p. 1356 - 1362 (2007/10/03)
Synthetic methodology for preparing novel esterase-sensitive cyclic prodrugs of peptides with increased protease stability and cell membrane permeability compared to linear peptides is described. Cyclic prodrug 1 of the hexapeptide H-Trp-Ala-Gly-Gly-Asp-Ala-OH linked by the N-terminal amino group to the C-terminal carboxyl group via an (acyloxy)alkoxy promoiety was synthesized. A convergent synthetic approach involving Boc[[(alaninyloxy)methyl]carbonyl]-N-tryptophan (2) and H-Ala-Gly-Gly-Asp(OBzl)-OTce (3) was used. The key fragment 2 has the promoiety inserted between the Ala and the Trp residues. Fragment 3 was synthesized by a solution-phase approach using standard Boc-amino acid chemistry. These fragments were coupled to produce the protected linear hexapeptide, which after deprotection was cyclized using standard high-dilution techniques to yield cyclic prodrug 1. In pH 7.4 buffer (HBSS) at 37°C, cyclic prodrug 1 was shown to degrade quantitatively to the hexapeptide (t( 1/4 ) = 206 ± 11 min). The rate of hydrolysis of cyclic prodrug 1 was significantly faster in human blood (t( 1/4 ) = 132 ± 4 min) than in HBSS. Paraoxon, a known inhibitor of esterases, slowed this hydrolysis of cyclic prodrug 1 to a value (t( 1/4 ) = 198 ± 9 min) comparable to the chemical stability. In human blood, cyclic prodrug 1 was shown to be 25-fold more stable than the linear hexapeptide.
Efficient amounts of additives for peptide coupling mediated by a water-soluble carbodiimide in aqueous media
Nozaki, Sukekatsu
, p. 1 - 2 (2007/10/03)
The optimal amounts of HOBt, HOSu, and HONb for enhancement of peptide coupling mediated by EDC in aqueous media were found to be less than equimolar against the C-component or the carbodiimide. A combination of EDC and 0.1 equimolar amount of HOBt was sh
Cyclic prodrugs of peptides and peptide nucleic acids having improved metabolic stability and cell membrane permeability
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, (2008/06/13)
Provided are cyclic prodrugs of biologically active peptides and peptide nucleic acids exhibiting improved cell membrane permeability and enzymatic stability, containing 3-(2'-hydroxy-4',6'-dimethyl phenyl)-3,3-dimethyl propionic acid and its deriveatives and acyloxyalkoxy linkers. Also provided are pharmaceutical compositions containing effective amounts of these cyclic prodrugs in combination with pharmaceutically acceptable carriers, excipients, or diluents.
Synthesis of rat parathymosin α fragment 1-28 and examination of its inhibitory activity towards the restoring activity of thymosin α1 on the impaired T-lymphocytes of uremic patients
Abiko,Sekino
, p. 2647 - 2652 (2007/10/02)
A fragment corresponding to N-terminal octaeicosapeptide of rat parathymosin α was synthesized by assembling 5 peptide fragments, followed by deprotection with 1 M trifluoromethanesulfonic acid-thioanisole (molar ratio 1:1) in trifluoroacetic acid in the
