scholarly journals Folding and fluorescence enhancement with strong odd–even effect for a series of merocyanine dye oligomers

2021 ◽  
Author(s):  
Xiaobo Hu ◽  
Alexander Schulz ◽  
Joachim O. Lindner ◽  
Matthias Grüne ◽  
David Bialas ◽  
...  

A series of merocyanine (MC) oligomers with a varying number of chromophores from two to six has been synthesized via a peptide synthesis strategy.

1990 ◽  
Vol 134 (1) ◽  
pp. 23-33 ◽  
Author(s):  
N. Joe Maeji ◽  
Andrew M. Bray ◽  
H. Mario Geysen

2016 ◽  
Vol 52 (72) ◽  
pp. 10886-10889 ◽  
Author(s):  
Yonghui Liu ◽  
Wenpeng Zhang ◽  
Qianqian He ◽  
Fan Yu ◽  
Tianbang Song ◽  
...  

We have designed and synthesized MUC1-fibroblast stimulating lipopeptide 1 conjugates as potential self-adjuvanting cancer vaccines using a linear solid phase peptide synthesis strategy.


RSC Advances ◽  
2014 ◽  
Vol 4 (60) ◽  
pp. 31564-31572 ◽  
Author(s):  
Anindya Basu ◽  
Biswajit Mishra ◽  
Sharmistha Dey ◽  
Susanna Su Jan Leong

Intein based bioprocessing strategy for producing antimicrobial peptide candidate was found to be more sustainable compared to solid phase peptide synthesis strategy (SPPS).


2015 ◽  
Vol 15 (2) ◽  
pp. 84 ◽  
Author(s):  
Toto Subroto ◽  
Ari Hardianto ◽  
Abdul Alim Kahari ◽  
Tika Pradnjaparamita

Current highly effective conventional vaccine to halt the spread of bird flu has not been invented yet because of susceptiblemutation of influenza virus. In spite of undergoing mutation which causes the amino acid sequence change, influenzaviruses maintain conservation at ectodomain of M2 protein, especially M2e(2-16) (SLLTEVETPIRNEW). The use ofconserved epitope M2e(2-16) in epitope-based vaccine potentially produces universal influenza vaccine. In designingepitope-based vaccine, the M2e(2-16) needs to be coupled with T helper epitope, P25, which is subsequently mentioned asM2e(2-16)-K-P25 (SLLTEVETPIRNEWGKKKL IPNASLIENCTKAEL). The M2e(2-16)-K-P25 was synthesized usingconvergent solid phase peptide synthesis strategy because of the size of the sequence. In this strategy, four peptideprecursors of M2e(2-16)-K-P25; SLLTEVETP (F1), IRNEWGK (F2), KLIPNASLI (F3), and ENCTKAEL (F4); were synthesizedin advance. After the precursors ready, coupling reaction was performed to obtain M2e(2-16)-K-P25. In the previousresearch, F3 has been obtained in high purity through Fmoc/tBu solid phase peptide synthesis method. In this conductedresearch, the three remaining precursors; F1, F2, and F4; were synthesized by the same method. Each peptide was analysedby thin layer chromatography, HPLC, and mass spectroscopy methods. F1, F2 and F4 were successfully synthesized andeach of them was detected at 1490.0, 1874.8 and 1881.9 amu, respectively. However, F1 was not possible to purify becauseof its insolubility in various solvents.


2019 ◽  
Author(s):  
Lukas P Smaga ◽  
Nicholas W Pino ◽  
Gabriela E Ibarra ◽  
Vishnu Krishnamurthy ◽  
Jefferson Chan

Controlled light-mediated delivery of biological analytes enables the investigation of highly reactivity molecules within cellular systems. As many biological effects are concentration dependent, it is critical to determine the location, time, and quantity of analyte donation. In this work, we have developed the first photoactivatable donor for formaldehyde (FA). Our optimized photoactivatable donor, photoFAD-3, is equipped with a fluorescence readout that enables monitoring of FA release with a concomitant 139-fold fluorescence enhancement. Tuning of photostability and cellular retention enabled quantification of intracellular FA release through cell lysate calibration. Application of photoFAD-3 uncovered the concentration range necessary for arresting wound healing in live cells. This marks the first report where a photoactivatable donor for any analyte has been used to quantify intracellular release.


Author(s):  
luis camacho III ◽  
Bryan J. Lampkin ◽  
Brett VanVeller

We describe a method to protect the sensitive stereochemistry of the thioamide—in analogy to the protection of the functional groups of amino acid side chains—in order to preserve the thioamide moiety during peptide elongation.<br>


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