scholarly journals Development of a Multifunctional Benzophenone Linker for Peptide Stapling and Photoaffinity Labelling

ChemBioChem ◽  
2016 ◽  
Vol 17 (8) ◽  
pp. 689-692 ◽  
Author(s):  
Yuteng Wu ◽  
Lasse B. Olsen ◽  
Yu Heng Lau ◽  
Claus Hatt Jensen ◽  
Maxim Rossmann ◽  
...  
Keyword(s):  
Photoaffinity Labelling ◽  
Peptide Stapling

Photoreaction of N-butyl 3,4-dimethoxy-6-nitrobenzamide with butylamine. A model study for lysine-directed photoaffinity labelling

1987 ◽  
Vol 52 (7) ◽  
pp. 1780-1785 ◽  
Author(s):  
Petr Kuzmič ◽  
Libuše Pavlíčková ◽  
Milan Souček
Keyword(s):  
Nitro Group ◽  
Aromatic Ring ◽  
Ultraviolet Irradiation ◽  
Title Compound ◽  
Reductive Coupling ◽  
Photoaffinity Labelling ◽  
Photolysis Rate ◽  
Model Study ◽  
A Minor

Ultraviolet irradiation of the title compound I in the presence of butylamine gave predominantly products of nucleophilic photosubstitution by the amine, i.e., nitroanilines IIa and IIb. Besides, small amounts of products of hydrolysis (phenol III) and reductive coupling (azoxybenzene IV) were also formed. Comparison of the overall photolysis rate of I with that of 3,4-dimethoxy-1-nitrobenzene (V) indicates a minor loss of reactivity, most probably due to some deviation from coplanarity of the activating nitro group and the aromatic ring.

Diversity-Oriented Peptide Stapling: A Third Generation Copper-Catalysed Azide-Alkyne Cycloaddition Stapling and Functionalisation Strategy

2017 ◽  
Vol 23 (14) ◽  
pp. 3490-3495 ◽  
Author(s):  
Phuong Thu Tran ◽  
Christian Ørnbøl Larsen ◽  
Tobias Røndbjerg ◽  
Martina De Foresta ◽  
Micha B. A. Kunze ◽  
...  
Keyword(s):  
Third Generation ◽  
Peptide Stapling

Nucleotides part XXX Chemical synthesis of adenylyl-(2? ? 5?)-adenylyl-(2? ? 5?)-8-azidoadenosine, and activation and photoaffinity labelling of RNase L by [32P]p5?A2?p5?A2?p5?N38A

1989 ◽  
Vol 72 (6) ◽  
pp. 1354-1361 ◽  
Author(s):  
Ramamurthy Charubala ◽  
Wolfgang Pfleiderer ◽  
Robert W. Sobol ◽  
Shi Wu Li ◽  
Robert J. Suhadolnik
Keyword(s):  
Chemical Synthesis ◽  
Rnase L ◽  
Photoaffinity Labelling

The nucleophilic aromatic photosubstitution in photoaffinity labelling. A model study of a cycloheximide derivative.

1985 ◽  
Vol 26 (20) ◽  
pp. 2489-2492 ◽  
Author(s):  
A. Castelló ◽  
J. Marquet ◽  
M. Moreno-Mañas ◽  
X. Sirera
Keyword(s):  
Photoaffinity Labelling ◽  
Model Study

scholarly journals Photoaffinity labelling of human poly(ADP-ribose) polymerase catalytic domain

1997 ◽  
Vol 322 (2) ◽  
pp. 469-475 ◽  
Author(s):  
Hyuntae KIM ◽  
Myron K. JACOBSON ◽  
Véronique ROLLI ◽  
Josiane MÉNISSIER-de MURCIA ◽  
Joseph REINBOLT ◽  
...  
Keyword(s):  
Catalytic Domain ◽  
Insertion Site ◽  
Site Directed Mutagenesis ◽  
Crystallographic Structure ◽  
Reverse Phase Hplc ◽  
Reverse Phase ◽  
Photoaffinity Labelling ◽  
Adenine Ring ◽  
Boronate Affinity Chromatography ◽  
Binding Residues

Photoaffinity labelling of the human poly(ADP-ribose) polymerase (PARP) catalytic domain (40 kDa) with the NAD+ photoaffinity analogue 2-azido-[α-32P]NAD+ has been used to identify NAD+-binding residues. In the presence of UV, photoinsertion of the analogue was observed with a stoichiometry of 0.73 mol of 2-azido-[α-32P]NAD+ per mol of catalytic domain. Competition experiments indicated that 3-aminobenzamide strongly protected the insertion site. Residues binding the adenine ring of NAD+ were identified by trypsin digestion and boronate affinity chromatography in combination with reverse-phase HPLC. Two major NAD+-binding residues, Trp1014 of peptide Thr1011–Trp1014 and Lys893 of peptide Ile879 –Lys893, were identified. The site-directed mutagenesis of these two residues revealed that Lys893, but not Trp1014, is critical for activity. The close positioning of Lys893 near the adenine ring of NAD+ has been confirmed by the recently solved crystallographic structure of the chicken PARP catalytic domain [Ruf, Ménissier-de Murcia, de Murcia and Schulz (1996) Proc. Natl. Acad. Sci. U.S.A. 93, 7481–7485].

scholarly journals A Physical Organic Approach to Tuning Reagents for Selective and Stable Methionine Bioconjugation

2019 ◽  
Author(s):  
Alec Christian ◽  
Shang Jia ◽  
Patricia Zhang ◽  
Arismel Tena Meza ◽  
Matthew S. Sigman ◽  
...  
Keyword(s):  
Structural Features ◽  
Data Driven ◽  
Live Cells ◽  
Design And Synthesis ◽  
Use Of Data ◽  
Physical Organic ◽  
Driving Stability ◽  
Peptide Stapling ◽  
Insight Into ◽  
Unique Chemical

We report a data-driven, physical organic approach to the development of new methionine-selective bioconjugation reagents with tunable adduct stabilities. Statistical modeling of structural features described by intrinsic physical organic parameters was applied to the development of a predictive model and to gain insight into features driving stability of adducts formed from the chemoselective coupling of oxaziridine and methionine thioether partners through Redox Activated Chemical Tagging (ReACT). From these analyses, a correlation between sulfimide stabilities and sulfimide  (C=O) stretching frequencies was revealed. We ex-ploited the rational gains in adduct stability exposed by this analysis to achieve the design and synthesis of a bis-oxaziridine reagent for peptide stapling. Indeed, we observed that a macrocyclic peptide formed by ReACT stapling at methionine exhibited improved uptake into live cells compared to an unstapled congener, highlighting the potential utility of this unique chemical tool for thioether modification. This work provides a template for the broader use of data-driven approaches to bioconjugation chemistry and other chemical biology applications.

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