scholarly journals Singlet Oxygen-Induced Furan Oxidation for Site-Specific and Chemoselective Peptide Ligation

2016 ◽  
Vol 22 (25) ◽  
pp. 8457-8461 ◽  
Author(s):  
Eirini Antonatou ◽  
Kurt Hoogewijs ◽  
Dimitris Kalaitzakis ◽  
Andreas Baudot ◽  
Georgios Vassilikogiannakis ◽  
...  
Keyword(s):  
Singlet Oxygen ◽  
Site Specific ◽  
Peptide Ligation

Singlet oxygen-mediated one-pot chemoselective peptide–peptide ligation

2017 ◽  
Vol 15 (38) ◽  
pp. 8140-8144 ◽  
Author(s):  
Eirini Antonatou ◽  
Yentl Verleysen ◽  
Annemieke Madder
Keyword(s):  
Singlet Oxygen ◽  
One Pot ◽  
Specific Chemical ◽  
Chemical Ligation ◽  
Site Specific ◽  
Peptide Segments ◽  
Peptide Ligation

We here describe a furan oxidation based site-specific chemical ligation approach using unprotected peptide segments.

Luminescent rhenium(I) perfluorobiphenyl complexes as site-specific labels for peptides to afford photofunctional bioconjugates

2021 ◽  
Author(s):  
Peter Kam-Keung Leung ◽  
Lawrence Cho-Cheung Lee ◽  
Tiffany Ka-Yan Ip ◽  
Hua-Wei Liu ◽  
Shek-Man Yiu ◽  
...  
Keyword(s):  
Singlet Oxygen ◽  
Cysteine Residue ◽  
Site Specific

We report herein new luminescent rhenium(I) perfluorobiphenyl complexes that reacted specifically with the cysteine residue of the π-clamp sequence (FCPF) to afford novel peptide-based imaging reagents, photosensitisers for singlet oxygen...

scholarly journals A Hand-held Fiber-optic Implement for the Site-specific Delivery of Photosensitizer and Singlet Oxygen

2011 ◽  
Vol 87 (6) ◽  
pp. 1330-1337 ◽  
Author(s):  
Adaickapillai Mahendran ◽  
Yasemin Kopkalli ◽  
Goutam Ghosh ◽  
Ashwini Ghogare ◽  
Mihaela Minnis ◽  
...  
Keyword(s):  
Singlet Oxygen ◽  
Fiber Optic ◽  
Site Specific

scholarly journals Engineered peptide ligases for cell signaling and bioconjugation

2020 ◽  
Vol 48 (3) ◽  
pp. 1153-1165
Author(s):  
Clara L. Frazier ◽  
Amy M. Weeks
Keyword(s):  
Protein Engineering ◽  
Specific Protein ◽  
Biological Research ◽  
Biological Applications ◽  
Site Specific ◽  
Challenges And Opportunities ◽  
Future Challenges ◽  
Natural Peptide ◽  
Further Development ◽  
Peptide Ligation

Enzymes that catalyze peptide ligation are powerful tools for site-specific protein bioconjugation and the study of cellular signaling. Peptide ligases can be divided into two classes: proteases that have been engineered to favor peptide ligation, and protease-related enzymes with naturally evolved peptide ligation activity. Here, we provide a review of key natural peptide ligases and proteases engineered to favor peptide ligation activity. We cover the protein engineering approaches used to generate and improve these tools, along with recent biological applications, advantages, and limitations associated with each enzyme. Finally, we address future challenges and opportunities for further development of peptide ligases as tools for biological research.

Site-Specific Hydroxylation at Polyguanosine in Double-Stranded DNA by Nickel(II) in the Presence of SH Compounds:  Comparison with Singlet Oxygen-Induced DNA Damage

2002 ◽  
Vol 15 (8) ◽  
pp. 1017-1022 ◽  
Author(s):  
Shinji Oikawa ◽  
Yusuke Hiraku ◽  
Tatsuhiko Fujiwara ◽  
Isao Saito ◽  
Shosuke Kawanishi
Keyword(s):  
Dna Damage ◽  
Singlet Oxygen ◽  
Site Specific ◽  
Double Stranded Dna

Site-specific DNA damage induced by cobalt(II) ion and hydrogen peroxide: role of singlet oxygen

1989 ◽  
Vol 2 (4) ◽  
pp. 234-239 ◽  
Author(s):  
Koji Yamamoto ◽  
Sumiko Inoue ◽  
Atsuko Yamazaki ◽  
Takeo Yoshinaga ◽  
Shosuke Kawanishi
Keyword(s):  
Hydrogen Peroxide ◽  
Dna Damage ◽  
Singlet Oxygen ◽  
Site Specific

Large-cluster and combined fluorescent and gold immunoprobes

1996 ◽  
Vol 54 ◽  
pp. 892-893
Author(s):  
Richard D. Powell ◽  
James F. Hainfeld ◽  
Carol M. R. Halsey ◽  
David L. Spector ◽  
Shelley Kaurin ◽  
...  
Keyword(s):  
Metal Cluster ◽  
Sulfonyl Chloride ◽  
Gel Filtration ◽  
Cross Linking ◽  
Site Specific ◽  
Fab Fragments ◽  
Cluster Label ◽  
Covalently Linked ◽  
Texas Red ◽  
Fold Excess

Two new types of covalently linked, site-specific immunoprobes have been prepared using metal cluster labels, and used to stain components of cells. Combined fluorescein and 1.4 nm “Nanogold” labels were prepared by using the fluorescein-conjugated tris (aryl) phosphine ligand and the amino-substituted ligand in the synthesis of the Nanogold cluster. This cluster label was activated by reaction with a 60-fold excess of (sulfo-Succinimidyl-4-N-maleiniido-cyclohexane-l-carboxylate (sulfo-SMCC) at pH 7.5, separated from excess cross-linking reagent by gel filtration, and mixed in ten-fold excess with Goat Fab’ fragments against mouse IgG (obtained by reduction of F(ab’)2 fragments with 50 mM mercaptoethylamine hydrochloride). Labeled Fab’ fragments were isolated by gel filtration HPLC (Superose-12, Pharmacia). A combined Nanogold and Texas Red label was also prepared, using a Nanogold cluster derivatized with both and its protected analog: the cluster was reacted with an eight-fold excess of Texas Red sulfonyl chloride at pH 9.0, separated from excess Texas Red by gel filtration, then deprotected with HC1 in methanol to yield the amino-substituted label.

The challenge of detecting modifications on proteins

2020 ◽  
Vol 64 (1) ◽  
pp. 135-153 ◽  
Author(s):  
Lauren Elizabeth Smith ◽  
Adelina Rogowska-Wrzesinska
Keyword(s):  
Mass Spectrometry ◽  
Protein Function ◽  
Chemical Properties ◽  
Lysine Acetylation ◽  
Mass Determination ◽  
Post Translational Modifications ◽  
Site Specific ◽  
The Common

Abstract Post-translational modifications (PTMs) are integral to the regulation of protein function, characterising their role in this process is vital to understanding how cells work in both healthy and diseased states. Mass spectrometry (MS) facilitates the mass determination and sequencing of peptides, and thereby also the detection of site-specific PTMs. However, numerous challenges in this field continue to persist. The diverse chemical properties, low abundance, labile nature and instability of many PTMs, in combination with the more practical issues of compatibility with MS and bioinformatics challenges, contribute to the arduous nature of their analysis. In this review, we present an overview of the established MS-based approaches for analysing PTMs and the common complications associated with their investigation, including examples of specific challenges focusing on phosphorylation, lysine acetylation and redox modifications.

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