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 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.

scholarly journals REP-X: An Evolution-guided Strategy for the Rational Design of Cysteine-less Protein Variants

2019 ◽  
Author(s):  
Kevin Dalton ◽  
Tom Lopez ◽  
Vijay Pande ◽  
Judith Frydman
Keyword(s):  
Rational Design ◽  
Biochemical Characterization ◽  
Cysteine Residue ◽  
Rational Approach ◽  
Protein Activity ◽  
Methanococcus Maripaludis ◽  
Site Specific ◽  
Protein Variants ◽  
Group Ii Chaperonin ◽  
Reduced Activity

AbstractSite-specific labeling of proteins is often a prerequisite for biophysical and biochemical characterization. Chemical modification of a unique cysteine residue is among the most facile methods for site-specific labeling of proteins. However, many proteins have multiple reactive cysteines, which must be mutated to other residues to enable labeling of unique positions. This trial-and-error process often results in cysteine-free proteins with reduced activity or stability. Herein we describe a general methodology to rationally engineer cysteine-less proteins. Briefly, natural variation across orthologues is exploited to identify suitable cysteine replacements compatible with protein activity and stability. As a proof-of-concept, we recount the successful engineering of a cysteine-less mutant of the group II chaperonin from methanogenic archaeon Methanococcus maripaludis. A webapp, REP-X (Replacement at Endogenous Positions from eXtant sequences), which enables users to design their own cysteine-less protein variants, will make this rational approach widely available.

Site-specific immobilization of an L-lactate dehydrogenase via an engineered surface cysteine residue

1993 ◽  
Vol 15 (1) ◽  
pp. 29-34 ◽  
Author(s):  
Helmut K. W. Kallwass ◽  
Wendy Parris ◽  
Emma L. A. Macfariane ◽  
Marvin Gold ◽  
J. Bryan Jones
Keyword(s):  
Lactate Dehydrogenase ◽  
Cysteine Residue ◽  
Site Specific

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

Site-specific PEGylation of a mutated-cysteine residue and its effect on tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL)

Biomaterials ◽  
2013 ◽  
Vol 34 (36) ◽  
pp. 9115-9123 ◽  
Author(s):  
Li-Qiang Pan ◽  
Hai-Bin Wang ◽  
Jun Lai ◽  
Ying-Chun Xu ◽  
Chen Zhang ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Cysteine Residue ◽  
Site Specific ◽  
Necrosis Factor
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